Continued from EC 1.13.11
EC 1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases) [continued]
EC 1.13.12 With incorporation of one atom of oxygen (internal monooxygenases or internal mixed function oxidases)
EC 1.13.99 Miscellaneous
EC 1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
EC 1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
EC 1.14.12 With NADH or NADPH as one donor, and incorporation of two atoms of oxygen into one donor
EC 1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen
EC 1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
EC 1.14.15 With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen
EC 1.14.16 With reduced pteridine as one donor, and incorporation of one atom of oxygen
EC 1.14.17 With reduced ascorbate as one donor, and incorporation of one atom of oxygen
EC 1.14.18 With another compound as one donor, and incorporation of one atom of oxygen
EC 1.14.99 Miscellaneous
Accepted name: arginine 2-monooxygenase
Reaction: L-arginine + O2 = 4-guanidinobutanamide + CO2 + H2O
Other name(s): arginine monooxygenase; arginine decarboxylase; arginine oxygenase (decarboxylating); arginine decarboxy-oxidase
Systematic name: L-arginine:oxygen 2-oxidoreductase (decarboxylating)
Comments: A flavoprotein. Also acts on canavanine and homoarginine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9027-36-5
References:
1. Olomucki, A., Pho, D.B., Lebar, R., Delcambe, L. and Thoai, N.V. Arginine oxygénase décarboxylante. V. Purification et nature flavinique. Biochim. Biophys. Acta 151 (1968) 353-366. [PMID: 4295160]
2. Thoai, N.V. and Olomucki, A. Arginine décarboxy-oxydase. I. Caract&egrav;res et nature de l'enzyme. Biochim. Biophys. Acta 59 (1962) 533-544.
3. Thoai, N.V. and Olomucki, A. Arginine décarboxy-oxydase. II. Oxydation de la canavanine et de l'homoarginine en β-guanidopropionamide et en δ-guanidovaleramide. Biochim. Biophys. Acta 59 (1962) 545-552.
Accepted name: lysine 2-monooxygenase
Reaction: L-lysine + O2 = 5-aminopentanamide + CO2 + H2O
Other name(s): lysine oxygenase; lysine monooxygenase; L-lysine-2-monooxygenase
Systematic name: L-lysine:oxygen 2-oxidoreductase (decarboxylating)
Comments: A flavoprotein (FAD). Also acts on other diamino acids.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9031-22-5
References:
1. Nakazawa, T., Hori, K. and Hayaishi, O. Studies on monooxygenases. V. Manifestation of amino acid oxidase activity by L-lysine monooxygenase. J. Biol. Chem. 247 (1972) 3439-3444. [PMID: 4624115]
2. Takeda, H. and Hayaishi, O. Crystalline L-lysine oxygenase. J. Biol. Chem. 241 (1966) 2733-2736. [PMID: 5911646]
3. Takeda, H., Yamamoto, S., Kojima, Y. and Hayaishi, O. Studies on monooxygenases. I. General properties of crystalline L-lysine monooxygenase. J. Biol. Chem. 244 (1969) 2935-2941. [PMID: 5772467]
Accepted name: tryptophan 2-monooxygenase
Reaction: L-tryptophan + O2 = (indol-3-yl)acetamide + CO2 + H2O
Systematic name: L-tryptophan:oxygen 2-oxidoreductase (decarboxylating)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37256-65-8
References:
1. Kosuge, T., Heskett, M.G. and Wilson, E.E. Microbial synthesis and degradation of indole-3-acetic acid. I. The conversion of L-tryptophan to indole-3-acetamide by an enzyme system from Pseudomonas savastanoi. J. Biol. Chem. 241 (1966) 3738-3744. [PMID: 5916389]
2. Kuo, T.T. and Kosuge, T. Factors influencing the production and further metabolism of indole-3-acetic acid by Pseudomonas savastanoi. J. Gen. Appl. Microbiol. 15 (1969) 51-63.
Accepted name: lactate 2-monooxygenase
Reaction: (S)-lactate + O2 = acetate + CO2 + H2O
Other name(s): lactate oxidative decarboxylase; lactate oxidase; lactic oxygenase; lactate oxygenase; lactic oxidase; L-lactate monooxygenase; lactate monooxygenase; L-lactate-2-monooxygenase
Systematic name: (S)-lactate:oxygen 2-oxidoreductase (decarboxylating)
Comments: A flavoprotein (FMN). Formerly EC 1.1.3.2.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9028-72-2
References:
1. Hayaishi, O. and Sutton, W.B. Enzymatic oxygen fixation into acetate concomitant with the enzymatic decarboxylation of L-lactate. J. Am. Chem. Soc. 79 (1957) 4809-4810..
2. Sutton, W.B. Mechanism of action and crystalization of lactic oxidative decarboxylase from Mycobacterium phlei. J. Biol. Chem. 226 (1957) 395-405.
Accepted name: Renilla-luciferin 2-monooxygenase
Reaction: Renilla luciferin + O2 = oxidized Renilla luciferin + CO2 + hν
For diagram click here
Glossary: Renilla luciferin = 2,8-dibenzyl-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one
Other name(s): Renilla-type luciferase; aequorin; luciferase (Renilla luciferin)
Systematic name: Renilla-luciferin:oxygen 2-oxidoreductase (decarboxylating)
Comments: From the soft coral coelenterate Renilla reniformis. The luciferin is bound to a luciferin-binding protein (BP-LH2). The bioluminescent reaction between the luciferin complex, luciferase and oxygen is triggered by calcium ions. In vivo, the excited state luciferin—luciferase complex undergoes the process of nonradiative energy transfer to an accessory protein, Renilla green fluorescent protein, which results in green bioluminescence. In vitro, Renilla luciferase emits blue light in the absence of any green fluorescent protein.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 61869-41-8
References:
1. Cormier, M.J., Hori, K. and Anderson, J.M. Bioluminescence in coelenterates. Biochim. Biophys. Acta 346 (1974) 137-164. [PMID: 4154104]
2. Hori, K., Anderson, J.M., Ward, W.W. and Cormier, M.J. Renilla luciferin as the substrate for calcium induced photoprotein bioluminescence. Assignment of luciferin tautomers in aequorin and mnemiopsin. Biochemistry 14 (1975) 2371-2376. [PMID: 237531]
3. Shimomura, O. and Johnson, F.H. Chemical nature of bioluminescence systems in coelenterates. Proc. Natl. Acad. Sci. USA 72 (1975) 1546-1549. [PMID: 236561]
4. Charbonneau, H. and Cormier, M.J. Ca2+-induced bioluminescence in Renilla reniformis. Purification and characterization of a calcium-triggered luciferin-binding protein. J. Biol. Chem. 254 (1979) 769-780. [PMID: 33174]
5. Anderson, J.M., Charbonneau, H. and Cormier, M.J. Mechanism of calcium induction of Renilla bioluminescence. Involvement of a calcium-triggered luciferin binding protein. Biochemistry 13 (1974) 1195-1200. [PMID: 4149963]
6. Lorenz, W.W., McCann, R.O., Longiaru, M. and Cormier, M.J. Isolation and expression of a cDNA encoding Renilla reniformis luciferase. Proc. Natl. Acad. Sci. USA 88 (1991) 4438-4442. [PMID: 1674607]
Accepted name: Cypridina-luciferin 2-monooxygenase
Reaction: Cypridina luciferin + O2 = oxidized Cypridina luciferin + CO2 + hν
For diagram click here.
Glossary: Cypridina-luciferin = (3-{3,7-dihydro-6-(1H-indol-3-yl)-2-[(S)-1-methylpropyl]-3-oxoimidazo[1,2-a]pyrazin-8-yl}propyl)guanidine
Other name(s): Cypridina-type luciferase; luciferase (Cypridina luciferin); Cypridina luciferase
Systematic name: Cypridina-luciferin:oxygen 2-oxidoreductase (decarboxylating)
Comments: Cypridina is a bioluminescent crustacea. The luciferins (and presumably the luciferases, since they cross-react) of some luminous fish (e.g. Apogon, Parapriacanthus, Porichthys) are apparently similar. The enzyme may be assayed by measurement of light emission.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 61969-99-1
References:
1. Cormier, M.J., Crane, J.M.,Jr. and Nakano, Y Evidence for the identity of the luminescent systems of Porichthys porosissimus (fish) and Cypridina hilgendorfii (crustacean). Biochem. Biophys. Res. Commun. 29 (1967) 747-752. [PMID: 5624784]
2. Karpetsky, T.P. and White, E.H. The synthesis of Cypridina etioluciferamine and the proof of the structure of Cypridina luciferin. Tetrahedron 29 (1973) 3761-3773.
3. Kishi, Y., Goto, T., Hirata, Y., Shiromura, O. and Johnson, F.H. Cypridina bioluminescence. I. Structure of Cypridina luciferin. Tetrahedron Lett. (1966) 3427-3436.
4. Tsuji, F.I., Lynch, R.V. and Stevens, C.L. Some properties of luciferase from the bioluminescent crustacean, Cypridina hilgendorfii. Biochemistry 13 (1974) 5204-5209. [PMID: 4433517]
Accepted name: Photinus-luciferin 4-monooxygenase (ATP-hydrolysing)
Reaction: Photinus luciferin + O2 + ATP = oxidized Photinus luciferin + CO2 + AMP + diphosphate + hν
For diagram click here.
Glossary: Photinus-luciferin = (S)-4,5-dihydro-2-(6-hydroxy-1,3-benzothiazol-2-yl)thiazole-4-carboxylic acid
Other name(s): firefly luciferase; luciferase (firefly luciferin); Photinus luciferin 4-monooxygenase (adenosine triphosphate-hydrolyzing); firefly luciferin luciferase; Photinus pyralis luciferase
Systematic name: Photinus-luciferin:oxygen 4-oxidoreductase (decarboxylating, ATP-hydrolysing)
Comments: Photinus (firefly) is a bioluminescent insect. The first step in the reaction is the formation of an acid anhydride between the carboxylic group and AMP, with the release of diphosphate. The enzyme may be assayed by measurement of light emission.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 61970-00-1
References:
1. Hopkins, T.A., Seliger, H.H., White, E.H. and Cass, M.W. The chemiluminescence of firefly luciferin. A model for the bioluminescent reaction and identification of the product excited state. J. Am. Chem. Soc. 89 (1967) 7148-7150. [PMID: 6064360]
2. White, E.H., McCapra, F., Field, G.F. and McElroy, W.D. The structure and synthesis of firefly luciferin. J. Am. Chem. Soc. 83 (1961) 2402-2403.
3. White, E.H., Rapaport, E., Hopkins, T.A. and Seliger, H.H. Chemi- and bioluminescence of firefly luciferin. J. Am. Chem. Soc. 91 (1969) 2178-2180. [PMID: 5784183]
Accepted name: Watasenia-luciferin 2-monooxygenase
Reaction: Watasenia luciferin + O2 = oxidized Watasenia luciferin + CO2 + hν
For diagram click here.
Glossary: Watasenia-luciferin = 8-benzyl-6-(4-sulfooxyphenyl)-2-(4-sulfooxybenzyl)imidazo[1,2-a]pyrazin-3(7H)-one
Other name(s): Watasenia-type luciferase
Systematic name: Watasenia-luciferin:oxygen 2-oxidoreductase (decarboxylating)
Comments: The enzyme from the luminous squid Watasenia may be assayed by measurement of light emission.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Inoue, S., Kakoi, H. and Goto, T. Squid bioluminescence. III. Isolation and structure of Watasenia luciferin. Tetrahedron Lett. (1976) 2971-2974.
Accepted name: phenylalanine 2-monooxygenase
Reaction: L-phenylalanine + O2 = 2-phenylacetamide + CO2 + H2O
Other name(s): L-phenylalanine oxidase (deaminating and decarboxylating); phenylalanine (deaminating, decarboxylating)oxidase
Systematic name: L-phenylalanine:oxygen 2-oxidoreductase (decarboxylating)
Comments: The reaction shown above is about 80% of the reaction catalysed; the remaining 20% is:
L-phenylalanine + O2 + H2O = 3-phenylpyruvic acid + ammonia + H2O2
a reaction similar to that of EC 1.4.3.2, L-amino-acid oxidase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 190396-37-3
References:
1. Koyama, H. Purification and characterization of a novel L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501. J. Biochem. (Tokyo) 92 (1982) 1235-1240. [PMID: 7174643]
2. Koyama, H. Oxidation and oxygenation of L-amino acids catalyzed by a L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501. J. Biochem. (Tokyo) 96 (1984) 421-427. [PMID: 6501250]
3. Koyama, H. A simple and rapid enzymatic determination of L-phenylalanine with a novel L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501. Clin. Chim. Acta 1361 (1984) 131-136. [PMID: 6692570]
4. Koyama, H. and Suzuki, H. Spectral and kinetic studies on Pseudomonas L-phenylalanine oxidase (deaminating and decarboxylating). J. Biochem. (Tokyo) 100 (1986) 859-866. [PMID: 3818566]
[EC 1.13.12.10 Deleted entry: lysine 6-monooxygenase. reaction covered by EC 1.14.13.59, L-lysine 6-monooxygenase (NADPH) (EC 1.13.12.10 created 1989, modified 1999, deleted 2001)]
[EC 1.13.12.11 Deleted entry: methylphenyltetrahydropyridine N-monooxygenase. The activity is due to EC 1.14.13.8, flavin-containing monooxygenase. (EC 1.13.12.11 created 1992, deleted 2006)]
[EC 1.13.12.12 Transferred entry: apo-β-carotenoid-14',13'-dioxygenase. The enzyme was misclassified and has been transferred to EC 1.13.11.67, 8-apo-β-carotenoid 14',13'-cleaving dioxygenase (EC 1.13.12.12 created 2000, modified 2001, deleted 2012)]
Accepted name: Oplophorus-luciferin 2-monooxygenase
Reaction: Oplophorus luciferin + O2 = oxidized Oplophorus luciferin + CO2 + hν
For diagram click here.
Glossary: Oplophorus luciferin = 8-benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one
Other name(s): Oplophorus luciferase
Systematic name: Oplophorus-luciferin:oxygen 2-oxidoreductase (decarboxylating)
Comments: The luciferase from the deep sea shrimp Oplophorus gracilorostris is a complex composed of more than one protein. The enzyme's specificity is quite broad, with both coelenterazine and bisdeoxycoelenterazine being good substrates.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Shimomura, O., Masugi, T., Johnson, F.H. and Haneda, Y. Properties and reaction mechanism of the bioluminescence system of the deep-sea shrimp Oplophorus gracilorostris. Biochemistry 17 (1978) 994-998. [PMID: 629957]
2. Inouye, S., Watanabe, K., Nakamura, H., Shimomura, O. Secretional luciferase of the luminous shrimp Oplophorus gracilirostris: cDNA cloning of a novel imidazopyrazinone luciferase. FEBS Lett. 481 (2000) 19-25. [PMID: 10984608]
[EC 1.13.12.14 Transferred entry: chlorophyllide-a oxygenase. Now EC 1.14.13.122, chlorophyllide-a oxygenase (EC 1.13.12.14 created 2006, deleted 2011)]
Accepted name: 3,4-dihydroxyphenylalanine oxidative deaminase
Reaction: 2 L-dopa + O2 = 2 3,4-dihydroxyphenylpyruvate + 2 NH3
Glossary: L-dopa = 3,4-dihydroxy-L-phenylalanine
Other name(s): 3,4-dihydroxy-L-phenylalanine: oxidative deaminase; oxidative deaminase; DOPA oxidative deaminase; DOPAODA
Systematic name: 3,4-dihydroxy-L-phenylalanine:oxygen oxidoreductase (deaminating)
Comments: This enzyme is one of the three enzymes involved in L-dopa (3,4-dihydroxyphenylalanine) catabolism in the non-oxygenic phototrophic bacterium Rubrivivax benzoatilyticus OU5 (and not Rhodobacter sphaeroides OU5 as had been thought [1]), the other two being EC 4.3.1.22 (dihydroxyphenylalanine reductive deaminase) and EC 2.6.1.49 (3,4-dihydroxyphenylalanine transaminase). In addition to L-dopa, the enzyme can also use L-tyrosine, L-phenylalanine, L-tryptophan and glutamate as substrate, but more slowly. The enzyme is inhibited by NADH and 2-oxoglutarate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Ranjith, N.K., Ramana, Ch.V. and Sasikala, Ch. Purification and characterization of 3,4-dihydroxyphenylalanine oxidative deaminase from Rhodobacter sphaeroides OU5. Can. J. Microbiol. 54 (2008) 829-834.
Accepted name: nitronate monooxygenase
Reaction: ethylnitronate + O2 = acetaldehyde + nitrite + other products
Other name(s): NMO; 2-nitropropane dioxygenase (incorrect)
Systematic name: nitronate:oxygen 2-oxidoreductase (nitrite-forming)
Comments: Previously classified as 2-nitropropane dioxygenase (EC 1.13.11.32), but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Neither hydrogen peroxide nor superoxide were detected during enzyme turnover. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Francis, K., Russell, B. and Gadda, G. Involvement of a flavosemiquinone in the enzymatic oxidation of nitroalkanes catalyzed by 2-nitropropane dioxygenase. J. Biol. Chem. 280 (2005) 5195-5204. [PMID: 15582992]
2. Ha, J.Y., Min, J.Y., Lee, S.K., Kim, H.S., Kim do, J., Kim, K.H., Lee, H.H., Kim, H.K., Yoon, H.J. and Suh, S.W. Crystal structure of 2-nitropropane dioxygenase complexed with FMN and substrate. Identification of the catalytic base. J. Biol. Chem. 281 (2006) 18660-18667. [PMID: 16682407]
3. Gadda, G. and Francis, K. Nitronate monooxygenase, a model for anionic flavin semiquinone intermediates in oxidative catalysis. Arch. Biochem. Biophys. 493 (2010) 53-61. [PMID: 19577534]
4. Francis, K. and Gadda, G. Kinetic evidence for an anion binding pocket in the active site of nitronate monooxygenase. Bioorg. Chem. 37 (2009) 167-172. [PMID: 19683782]
Accepted name: dichloroarcyriaflavin A synthase
Reaction: dichlorochromopyrrolate + 4 O2 + 4 NADH + 4 H+ = dichloroarcyriaflavin A + 2 CO2 + 6 H2O + 4 NAD+
For diagram of reaction click here
Glossary: dichloro-arcyriaflavin A = rebeccamycin aglycone
Systematic name: dichlorochromopyrrolate,NADH:oxygen 2,5-oxidoreductase (dichloroarcyriaflavin A-forming)
Comments: The conversion of dichlorochromopyrrolate to dichloroarcyriaflavin A is a complex process that involves two enzyme components. RebP is an NAD-dependent cytochrome P450 oxygenase that performs an aryl-aryl bond formation yielding the six-ring indolocarbazole scaffold [1]. Along with RebC, a flavin-dependent hydroxylase, it also catalyses the oxidative decarboxylation of both carboxyl groups. The presence of RebC ensures that the only product is the rebeccamycin aglycone dichloroarcyriaflavin A [2]. The enzymes are similar, but not identical, to StaP and StaC, which are involved in the synthesis of staurosporine [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Makino, M., Sugimoto, H., Shiro, Y., Asamizu, S., Onaka, H. and Nagano, S. Crystal structures and catalytic mechanism of cytochrome P450 StaP that produces the indolocarbazole skeleton. Proc. Natl. Acad. Sci. USA 104:1159 (2007). [PMID: 17606921]
2. Howard-Jones, A.R. and Walsh, C.T. Staurosporine and rebeccamycin aglycones are assembled by the oxidative action of StaP, StaC, and RebC on chromopyrrolic acid. J. Am. Chem. Soc. 128:1228 (2006). [PMID: 16967980]
3. Sanchez, C., Zhu, L., Brana, A.F., Salas, A.P., Rohr, J., Mendez, C. and Salas, J.A. Combinatorial biosynthesis of antitumor indolocarbazole compounds. Proc. Natl. Acad. Sci. USA 102:461 (2005). [PMID: 15625109]
Accepted name: dinoflagellate luciferase
Reaction: dinoflagellate luciferin + O2 = oxidized dinoflagellate luciferin + H2O + hν
For diagram of reaction, click here
Glossary: dinoflagellate luciferin = (1S,2S,3S)-1-carboxy-3-(2-carboxyethyl)-12-ethyl-2,8,13,18-tetramethyl-17-vinyl-1,2,3,21-tetrahydro-5,7-ethanobilene-a-19(16H),52-dione
Other name(s): (dinoflagellate luciferin) luciferase; Gonyaulax luciferase
Systematic name: dinoflagellate-luciferin:oxygen 132-oxidoreductase
Comments: A luciferase from dinoflagelates such as Gonyaulax polyedra, Lingulodinium polyedrum, Noctiluca scintillans, and Pyrocystis lunula. It is a single protein with three luciferase domains. The luciferin is strongly bound by a luciferin binding protein above a pH of 7.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Dunlap, J.C. and Hastings, J.W. The biological clock in Gonyaulax controls luciferase activity by regulating turnover. J. Biol. Chem. 256 (1981) 10509-10518. [PMID: 7197271]
2. Morse, D., Pappenheimer, A.M., Jr. and Hastings, J.W. Role of a luciferin-binding protein in the circadian bioluminescent reaction of Gonyaulax polyedra. J. Biol. Chem. 264 (1989) 11822-11826. [PMID: 2745419]
3. Bae, Y.M. and Hastings, J.W. Cloning, sequencing and expression of dinoflagellate luciferase DNA from a marine alga, Gonyaulax polyedra. Biochim. Biophys. Acta 1219 (1994) 449-456. [PMID: 7918642]
4. Li, L. Gonyaulax luciferase: gene structure, protein expression, and purification from recombinant sources. Methods Enzymol. 305 (2000) 249-258. [PMID: 10812605]
5. Morse, D. and Mittag, M. Dinoflagellate luciferin-binding protein. Methods Enzymol. 305 (2000) 258-276. [PMID: 10812606]
6. Schultz, L.W., Liu, L., Cegielski, M. and Hastings, J.W. Crystal structure of a pH-regulated luciferase catalyzing the bioluminescent oxidation of an open tetrapyrrole. Proc. Natl. Acad. Sci. USA 102 (2005) 1378-1383. [PMID: 15665092]
EC 1.13.12.19
Accepted name: 2-oxuglutarate dioxygenase (ethylene-forming)
Reaction: 2-oxoglutarate + O2 = ethylene + 3 CO2 + H2O
Other name(s): ethylene-forming enzyme; EFE
Systematic name: 2-oxuglutarate:oxygen oxidoreductase (decarboxylating, ethylene-forming)
Comments: This is one of two simultaneous reactions catalysed by the enzyme, which is responsible for ethylene production in bacteria of the Pseudomonas syringae group. In the other reaction [EC 1.14.11.34, 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming)] the enzyme catalyses the mono-oxygenation of both 2-oxoglutarate and L-arginine, forming succinate, carbon dioxide and L-hydroxyarginine, which is subsequently cleaved into guanidine and (S)-1-pyrroline-5-carboxylate. The enzymes catalyse two cycles of the ethylene-forming reaction for each cycle of the succinate-forming reaction, so that the stoichiometry of the products ethylene and succinate is 2:1.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Nagahama, K., Ogawa, T., Fujii, T., Tazaki, M., Tanase, S., Morino, Y. and Fukuda, H. Purification and properties of an ethylene-forming enzyme from Pseudomonas syringae pv. phaseolicola PK2. J. Gen. Microbiol. 137 (1991) 2281-2286. [PMID: 1770346]
2. Fukuda, H., Ogawa, T., Tazaki, M., Nagahama, K., Fujii, T., Tanase, S. and Morino, Y. Two reactions are simultaneously catalyzed by a single enzyme: the arginine-dependent simultaneous formation of two products, ethylene and succinate, from 2-oxoglutarate by an enzyme from Pseudomonas syringae. Biochem. Biophys. Res. Commun. 188 (1992) 483-489. [PMID: 1445291]
3. Fukuda, H., Ogawa, T., Ishihara, K., Fujii, T., Nagahama, K., Omata, T., Inoue, Y., Tanase, S. and Morino, Y. Molecular cloning in Escherichia coli, expression, and nucleotide sequence of the gene for the ethylene-forming enzyme of Pseudomonas syringae pv. phaseolicola PK2. Biochem. Biophys. Res. Commun. 188 (1992) 826-832. [PMID: 1445325]
EC 1.13.12.20
Accepted name: noranthrone monooxygenase
Reaction: norsolorinic acid anthrone + O2 = norsolorinic acid + H2O
For diagram of reaction click here.
Glossary: norsolorinic acid anthrone = noranthrone = 2-hexanoyl-1,3,6,8-tetrahydroxyanthracen-9(10H)-one
Other name(s): norsolorinate anthrone oxidase
Systematic name: norsolorinic acid anthrone:oxygen 9-oxidoreductase (norsolorinic acid-forming)
Comments: Involved in the synthesis of aflatoxins in the fungus Aspergillus parasiticus.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Ehrlich, K.C., Li, P., Scharfenstein, L. and Chang, P.K. HypC, the anthrone oxidase involved in aflatoxin biosynthesis. Appl. Environ. Microbiol. 76 (2010) 3374-3377. [PMID: 20348292]
norsolorinate = 2-hexanoyl-1,3,6,8-tetrahydroxy-9,10-anthraquinone
EC 1.13.99 miscellaneousContents
EC 1.13.99.1 inositol oxygenase
EC 1.13.99.2 now EC 1.14.12.10
EC 1.13.99.3 tryptophan 2'-dioxygenase
EC 1.13.99.4 now EC 1.14.12.9
EC 1.13.99.5 now EC 1.13.11.47
Accepted name: inositol oxygenase
Reaction: myo-inositol + O2 = D-glucuronate + H2O
For diagram click here.
Other name(s): meso-inositol oxygenase; myo-inositol oxygenase; MOO
Systematic name: myo-inositol:oxygen oxidoreductase
Comments: An iron protein. Formerly EC 1.13.1.11 and EC 1.99.2.6.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-59-8
References:
1. Charalampous, F.C. Biochemical studies on inositol. V. Purification and properties of the enzyme that cleaves inositol to D-glucuronic acid. J. Biol. Chem. 234 (1959) 220-227.
2. Reddy, C.C., Swan, J.S. and Hamilton, G.A. myo-Inositol oxygenase from hog kidney. I. Purification and characterization of the oxygenase and of an enzyme complex containing the oxygenase and D-glucuronate reductase. J. Biol. Chem. 256 (1981) 8510-8518. [PMID: 7263666]
3. Arner, R.J., Prabhu, K.S., Thompson, J.T., Hildenbrandt, G.R., Liken, A.D. and Reddy, C.C. myo-Inositol oxygenase: molecular cloning and expression of a unique enzyme that oxidizes myo-inositol and D-chiro-inositol. Biochem. J. 360 (2001) 313-320. [PMID: 11716759]
[EC 1.13.99.2 Transferred entry: benzoate 1,2-dioxygenase - now EC 1.14.12.10 benzoate 1,2-dioxygenase (EC 1.13.99.2 created 1972, deleted 1992)]
Accepted name: tryptophan 2'-dioxygenase
Reaction: L-tryptophan + O2 = (indol-3-yl)glycolaldehyde + CO2 + NH3
Other name(s): indole-3-alkane α-hydroxylase; tryptophan side-chain α,β-oxidase; tryptophan side chain oxidase II; tryptophan side-chain oxidase; TSO; indolyl-3-alkan α-hydroxylase; tryptophan side chain oxidase type I; TSO I ; TSO II; tryptophan side chain oxidase
Systematic name: L-tryptophan:oxygen 2'-oxidoreductase (side-chain-cleaving)
Comments: A hemoprotein. Acts on a number of indolyl-3-alkane derivatives, oxidizing the 3-side-chain in the 2'-position. Best substrates were L-tryptophan and 5-hydroxy-L-tryptophan.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 64295-81-4
References:
1. Roberts, J. and Rosenfeld, H.J. Isolation, crystallization, and properties of indolyl-3-alkane α-hydroxylase. A novel tryptophan-metabolizing enzyme. J. Biol. Chem. 252 (1977) 2640-2647. [PMID: 15994]
2. Takai, K., Ushiro, H., Noda, Y., Narumiya, S., Tokuyama, T. and Hayaishi, O. Crystalline hemoprotein from Pseudomonas that catalyzes oxidation of side chain of tryptophan and other indole derivatives. J. Biol. Chem. 252 (1977) 2648-2656. [PMID: 15995]
[EC 1.13.99.4 Transferred entry: 4-chlorophenylacetate 3,4-dioxygenase - now EC 1.14.12.9 4-chlorophenylacetate 3,4-dioxygenase (EC 1.13.99.4 created 1989, deleted 1992)]
[EC 1.13.99.5 Transferred entry: now EC 1.13.11.47, 3,4-dihydroxyquinoline 2,4-dioxygenase (EC 1.13.99.5 created 1999, deleted 2001)]
EC 1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
EC 1.14.12 With NADH or NADPH as one donor, and incorporation of two atoms of oxygen into one donor
EC 1.14.13 With NAD or NADH as one donor, and incorporation of one atom of oxygen
EC 1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
EC 1.14.15 With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen
EC 1.14.16 With reduced pteridine as one donor, and incorporation of one atom of oxygen
EC 1.14.17 With reduced ascorbate as one donor, and incorporation of one atom of oxygen
EC 1.14.18 With another compound as one donor, and incorporation of one atom of oxygen
EC 1.14.99 Miscellaneous
Accepted name: γ-butyrobetaine dioxygenase
Reaction: 4-trimethylammoniobutanoate + 2-oxoglutarate + O2 = 3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2
Other name(s): α-butyrobetaine hydroxylase; γ-butyrobetaine hydroxylase; butyrobetaine hydroxylase
Systematic name: 4-trimethylammoniobutanoate,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Comments: Requires Fe2+ and ascorbate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9045-31-2
References:
1. Lindstedt, G. and Lindstedt, S. Cofactor requirements of γ-butyrobetaine hydroxylase from rat liver. J. Biol. Chem. 245 (1970) 4178-4186. [PMID: 4396068]
Accepted name: procollagen-proline dioxygenase
Reaction: procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2
For diagram click here.
Other name(s): protocollagen hydroxylase; proline hydroxylase; proline,2-oxoglutarate 4-dioxygenase; collagen proline hydroxylase; hydroxylase, collagen proline; peptidyl proline hydroxylase; proline protocollagen hydroxylase; proline, 2-oxoglutarate dioxygenase; prolyl hydroxylase; prolylprotocollagen dioxygenase; prolylprotocollagen hydroxylase; protocollagen proline 4-hydroxylase; protocollagen proline dioxygenase; protocollagen proline hydroxylase; protocollagen prolyl hydroxylase; prolyl 4-hydroxylase; prolyl-glycyl-peptide, 2-oxoglutarate:oxygen oxidoreductase, 4-hydroxylating; procollagen-proline 4-dioxygenase
Systematic name: procollagen-L-proline,2-oxoglutarate:oxygen oxidoreductase (4-hydroxylating)
Comments: Requires Fe2+ and ascorbate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9028-06-2
References:
1. Berg, R.A. and Prockop, D.J. Affinity column purification of protocollagen proline hydroxylase from chick embryos and further characterization of the enzyme. J. Biol. Chem. 248 (1973) 1175-1182. [PMID: 4346946]
2. Hutton, J.J., Jr., Tappel, A.L. and Udenfriend, S. Cofactor and substrate requirements of collagen proline hydroxylase. Arch. Biochem. Biophys. 118 (1967) 231-240.
3. Kivirikko, K.I., Kishida, Y., Sakakibara, S. and Prockop, J. Hydroxylation of (X-Pro-Gly)n by protocollagen proline hydroxylase. Effect of chain length, helical conformation and amino acid sequence in the substrate. Biochim. Biophys. Acta 271 (1972) 347-356. [PMID: 5046811]
4. Kivirikko, K.I. and Prockop, D.J. Purification and partial characterization of the enzyme for the hydroxylation of proline in protocollogen. Arch. Biochem. Biophys. 118 (1967) 611-618.
Accepted name: pyrimidine-deoxynucleoside 2'-dioxygenase
Reaction: 2'-deoxyuridine + 2-oxoglutarate + O2 = uridine + succinate + CO2
Other name(s): deoxyuridine 2'-dioxygenase; deoxyuridine 2'-hydroxylase; pyrimidine deoxyribonucleoside 2'-hydroxylase; thymidine 2'-dioxygenase; thymidine 2'-hydroxylase; thymidine 2-oxoglutarate dioxygenase; thymidine dioxygenase
Systematic name: 2'-deoxyuridine,2-oxoglutarate:oxygen oxidoreductase (2'-hydroxylating)
Comments: Requires Fe(II) and ascorbate. Also acts on thymidine. cf. EC 1.14.11.10, pyrimidine-deoxynucleoside 1'-dioxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9076-89-5
References:
1. Bankel, L., Lindstedt, G. and Lindstedt, S. Thymidine 2'-hydroxylation in Neurospora crassa. J. Biol. Chem. 247 (1972) 6128-6134. [PMID: 4265566]
2. Stubbe, J. Identification of two α-ketoglutarate-dependent dioxygenases in extracts of Rhodotorula glutinis catalyzing deoxyuridine hydroxylation. J. Biol. Chem. 260 (1985) 9972-9975. [PMID: 4040518]
3. Warn-Cramer, B.J., Macrander, L.A. and Abbott, M.T. Markedly different ascorbate dependencies of the sequential α-ketoglutarate dioxygenase reactions catalyzed by an essentially homogeneous thymine 7-hydroxylase from Rhodotorula glutinis. J. Biol. Chem. 258 (1983) 10551-10557. [PMID: 6684117]
Accepted name: procollagen-lysine 5-dioxygenase
Reaction: L-lysine-[procollagen] + 2-oxoglutarate + O2 = (2S,5R)- 5-hydroxy-L-lysine-[procollagen] + succinate + CO2
Other name(s): lysine hydroxylase; lysine,2-oxoglutarate 5-dioxygenase; protocollagen lysine dioxygenase; collagen lysine hydroxylase; lysine-2-oxoglutarate dioxygenase; lysyl hydroxylase; lysylprotocollagen dioxygenase; protocollagen lysyl hydroxylase; peptidyl-lysine, 2-oxoglutarate: oxygen oxidoreductase; peptidyllysine, 2-oxoglutarate:oxygen 5-oxidoreductase; protocollagen lysine hydroxylase
Systematic name: L-lysine-[procollagen],2-oxoglutarate:oxygen oxidoreductase (5-hydroxylating)
Comments: Requires Fe2+ and ascorbate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9059-25-0
References:
1. Hausmann, E. Cofactor requirements for the enzymatic hydroxylation of lysine in a polypeptide precursor of collagen. Biochim. Biophys. Acta 133 (1967) 591-598. [PMID: 6033801]
2. Rhoads, R.E. and Udenfriend, S. Decarboxylation of α-ketoglutarate coupled to collagen proline hydroxylase. Proc. Natl. Acad. Sci. USA 60 (1968) 1473-1478.
[EC 1.14.11.5 Deleted entry: 5-hydroxymethyluracil,2-oxoglutarate dioxygenase. Now included with EC 1.14.11.6 thymine dioxygenase (EC 1.14.11.5 created 1972, deleted 1976)]
Accepted name: thymine dioxygenase
Reaction: thymine + 2-oxoglutarate + O2 = 5-hydroxymethyluracil + succinate + CO2
Other name(s): thymine 7-hydroxylase; 5-hydroxy-methyluracil dioxygenase; 5-hydroxymethyluracil oxygenase
Systematic name: thymine,2-oxoglutarate:oxygen oxidoreductase (7-hydroxylating)
Comments: Requires Fe2+ and ascorbate. Also acts on 5-hydroxymethyluracil to oxidize its -CH2OH group first to -CHO and then to -COOH.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37256-67-0
References:
1. Bankel, L., Holme, E., Lindstedt, G. and Lindstedt, S. Oxygenases involved in thymine and thymidine metabolism in Neurospora crassa. FEBS Lett. 21 (1972) 135-138.
2. Liu, C.-K., Hsu, C.-A. and Abbott, M.T. Catalysis of three sequential dioxygenase reactions by thymine 7-hydroxylase. Arch. Biochem. Biophys. 159 (1973) 180-187. [PMID: 4274083]
3. Warn-Cramer, B.J., Macrander, L.A. and Abbott, M.T. Markedly different ascorbate dependencies of the sequential α-ketoglutarate dioxygenase reactions catalyzed by an essentially homogeneous thymine 7-hydroxylase from Rhodotorula glutinis. J. Biol. Chem. 258 (1983) 10551-10557. [PMID: 6684117]
Accepted name: procollagen-proline 3-dioxygenase
Reaction: procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2
For diagram click here.
Other name(s): proline,2-oxoglutarate 3-dioxygenase; prolyl 3-hydroxylase; protocollagen proline 3-hydroxylase; prolyl-4-hydroxyprolyl-glycyl-peptide, 2-oxoglutarate: oxygen oxidoreductase, 3-hydroxylating
Systematic name: procollagen-L-proline,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Comments: Requires Fe2+ and ascorbate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 63551-75-7
References:
1. Risteli, J., Tryggvason, K. and Kivirikko, K.I. Prolyl 3-hydroxylase: partial characterization of the enzyme from rat kidney cortex. Eur. J. Biochem. 73 (1977) 485-492. [PMID: 191255]
2. Risteli, J., Tryggvason, K. and Kivirikko, K.I. A rapid assay for prolyl 3-hydroxylase activity. Anal. Biochem. 84 (1978) 423-431. [PMID: 204218]
Accepted name: trimethyllysine dioxygenase
Reaction: N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2 = 3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
Other name(s): trimethyllysine α-ketoglutarate dioxygenase; TML-α-ketoglutarate dioxygenase; TML hydroxylase
Systematic name: N6,N6,N6-trimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Comments: Requires Fe2+ and ascorbate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 74622-49-4
References:
1. Hulse, J.D., Ellis, S.R. and Henderson, L.M. Carnitine biosynthesis. β-Hydroxylation of trimethyllysine by an α-ketoglutarate-dependent mitochondrial dioxygenase. J. Biol. Chem. 253 (1978) 1654-1659. [PMID: 627563]
Accepted name: flavanone 3-dioxygenase
Reaction: a flavanone + 2-oxoglutarate + O2 = a dihydroflavonol + succinate + CO2
See diagram for reaction in aromadendrin or taxifolin biosynthesis.
Other name(s): naringenin 3-hydroxylase; flavanone 3-hydroxylase; flavanone 3β-hydroxylase; flavanone synthase I; (2S)-flavanone 3-hydroxylase; naringenin,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Systematic name: flavanone,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Comments: Requires Fe2+ and ascorbate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 75991-43-4
References: (if your browser cannot recognise unicode the author is Lukacin with a hacek over the c)
1. Forkmann, G., Heller, W. and Grisebach, H. Anthocyanin biosynthesis in flowers of Matthiola incana flavanone 3- and flavonoid 3'-hydroxylases. Z. Naturforsch. C: Biosci. 35 (1980) 691-695.
2. Wellmann, F., Matern, U. and Lukačin, R. Significance of C-terminal sequence elements for Petunia flavanone 3β-hydroxylase activity. FEBS Lett. 561 (2004) 149-154. [PMID: 15013767]
Accepted name: pyrimidine-deoxynucleoside 1'-dioxygenase
Reaction: 2'-deoxyuridine + 2-oxoglutarate + O2 = uracil + 2-deoxyribonolactone + succinate + CO2
Other name(s): deoxyuridine-uridine 1'-dioxygenase
Systematic name: 2'-deoxyuridine,2-oxoglutarate:oxygen oxidoreductase (1'-hydroxylating)
Comments: Requires Fe(II) and ascorbate. cf. EC 1.14.11.3, pyrimidine-deoxynucleoside 2'-dioxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 98865-52-2
References:
1. Stubbe, J. Identification of two α-ketoglutarate-dependent dioxygenases in extracts of Rhodotorula glutinis catalyzing deoxyuridine hydroxylation. J. Biol. Chem. 260 (1985) 9972-9975. [PMID: 4040518]
Accepted name: hyoscyamine (6S)-dioxygenase
Reaction: L-hyoscyamine + 2-oxoglutarate + O2 = (6S)-hydroxyhyoscyamine + succinate + CO2
For diagram of reaction, click here.
Other name(s): hyoscyamine 6β-hydroxylase; hyoscyamine 6β-dioxygenase; hyoscyamine 6-hydroxylase
Systematic name: L-hyoscyamine,2-oxoglutarate:oxygen oxidoreductase [(6S)-hydroxylating]
Comments: Requires Fe2+ and ascorbate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 103865-33-4
References:
1. Hashimoto, T. and Yamada, Y. Hyoscyamine 6β-hydroxylase, a 2-oxoglutarate-dependent dioxygenase, in alkaloid-producing root cultures. Plant Physiol. 81 (1986) 619-625.
Accepted name: gibberellin-44 dioxygenase
Reaction: gibberellin 44 + 2-oxoglutarate + O2 = gibberellin 19 + succinate + CO2
For reaction pathway click here.
Other name(s): oxygenase, gibberellin A44 oxidase; (gibberellin-44), 2-oxoglutarate:oxygen oxidoreductase
Systematic name: (gibberellin-44),2-oxoglutarate:oxygen oxidoreductase
Comments: Requires Fe2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 112198-85-3
References:
1. Gilmour, S.J., Bleecker, A.B. and Zeevaart, J.A.D. Partial-purification of gibberellin oxidases from spinach leaves. Plant Physiol. 85 (1987) 87-90.
Accepted name: gibberellin 2β-dioxygenase
Reaction: gibberellin 1 + 2-oxoglutarate + O2 = 2β-hydroxygibberellin 1 + succinate + CO2
For reaction pathway click here.
Other name(s): gibberellin 2β-hydroxylase
Systematic name: (gibberellin-1),2-oxoglutarate:oxygen oxidoreductase (2β-hydroxylating)
Comments: Also acts on a number of other gibberellins.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 85713-20-8
References:
1. Smith, V.A. and MacMillan, J. The partial-purification and characterization of gibberellin 2β-hydroxylases from seeds of Pisum sativum. Planta 167 (1986) 9-18.
Accepted name: 6β-hydroxyhyoscyamine epoxidase
Reaction: (6S)-6β-hydroxyhyoscyamine + 2-oxoglutarate + O2 = scopolamine + succinate + CO2 + H2O
For diagram of reaction, click here.
Glossary: scopolamine = hyoscine
Other name(s): hydroxyhyoscyamine dioxygenase; (6S)-6-hydroxyhyoscyamine,2-oxoglutarate oxidoreductase (epoxide-forming)
Systematic name: (6S)-6β-hydroxyhyoscyamine,2-oxoglutarate:oxygen oxidoreductase (epoxide-forming)
Comments: Requires Fe2+ and ascorbate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 121479-53-6
References:
1. Hashimoto, T., Kohno, J. and Yamada, Y. 6β-Hydroxyhyoscyamine epoxidase from cultured roots of Hyoscyamus niger. Phytochemistry 28 (1989) 1077-1082.
Accepted name: gibberellin 3β-dioxygenase
Reaction: gibberellin 20 + 2-oxoglutarate + O2 = gibberellin 1 + succinate + CO2
For reaction pathway click here.
Other name(s): gibberellin 3β-hydroxylase; (gibberrellin-20),2-oxoglutarate: oxygen oxidoreductase (3β-hydroxylating)
Systematic name: (gibberellin-20),2-oxoglutarate:oxygen oxidoreductase (3β-hydroxylating)
Comments: Requires Fe2+ and ascorbate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 120860-89-1
References:
1. Kwak, S.-S., Kamiya, Y., Sakurai, A., Takahishi, N. and Graebe, J.E. Partial-purification and characterization of gibberellin 3β-hydroxylase from immature seeds of Phaseolus vulgaris L. Plant Cell Physiol. 29 (1988) 935-943.
Accepted name: peptide-aspartate β-dioxygenase
Reaction: peptide-L-aspartate + 2-oxoglutarate + O2 = peptide-3-hydroxy-L-aspartate + succinate + CO2
Other name(s): aspartate β-hydroxylase; aspartylpeptide β-dioxygenase
Systematic name: peptide-L-aspartate,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Comments: Requires Fe2+. Some vitamin K-dependent coagulation factors, as well as synthetic peptides based on the structure of the first epidermal growth factor domain of human coagulation factor IX or X, can act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 122544-66-5
References:
1. Gronke, R.S., Welsch, D.J., VanDusen, W.J., Garsky, V.M., Sardana, M.K., Stern, A.M. and Friedman, P.A. Partial purification and characterization of bovine liver aspartyl β-hydroxylase. J. Biol. Chem. 265 (1990) 8558-8565. [PMID: 2187868]
Accepted name: taurine dioxygenase
Reaction: taurine + 2-oxoglutarate + O2 = sulfite + aminoacetaldehyde + succinate + CO2
Other name(s) 2-aminoethanesulfonate dioxygenase; α-ketoglutarate-dependent taurine dioxygenase
Systematic name: taurine, 2-oxoglutarate::oxygen oxidoreductase (sulfite-forming)
Comments: Requires FeII. The enzyme from Escherichia coli also acts on pentanesulfonate, 3-(N-morpholino)propanesulfonate and 2-(1,3-dioxoisoindolin-2-yl)ethanesulfonate, but at lower rates.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 197809-75-9
References:
1. Eichhorn, E., Van Der Poeg, J.R., Kertesz, M.A. and Leisinger, T. Characterization of α-ketoglutarate-dependent taurine dioxygenase from Escherichia coli. J.Biol. Chem. 272 (1997) 23031-23036. [PMID: 9287300]
Accepted name: phytanoyl-CoA dioxygenase
Reaction: phytanoyl-CoA + 2-oxoglutarate + O2 = 2-hydroxyphytanoyl-CoA + succinate + CO2
Glossary entries
phytanate: 3,7,11,15-tetramethylhexadecanoate
Other name(s): phytanoyl-CoA hydroxylase
Systematic name: phytanoyl-CoA, 2-oxoglutarate:oxygen oxidoreductase (2-hydroxylating)
Comments: Part of the peroxisomal phytanic acid α-oxidation pathway. Requires Fe2+ and ascorbate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 185402-46-4
References:
1. Jansen, G.A., Mihalik, S.J., Watkins, P.A., Jakobs, C., Moser, H.W. and Wanders, R.J.A. Characterization of phytanoyl-CoA hydroxylase in human liver and activity measurements in patients with peroxisomal disorders. Clin. Chim. Acta 271 (1998) 203-211. [PMID: 9565335]
2. Jansen, G.A., Mihalik, S.J., Watkins, P.A., Moser, H.W., Jakobs, C., Denis, S. and Wanders, R.J.A. Phytanoyl-CoA hydroxylase is present in human liver, located in peroxisomes, and deficient in Zellweger syndrome: direct, unequivocal evidence for the new, revised pathway of phytanic acid α-oxidation in humans. Biochem. Biophys. Res. Commun. 229 (1996) 205-210. [PMID: 8954107]
3. Jansen, G.A., Ofman, R., Ferdinandusse, S., Ijlst, L., Muijsers, A.O., Skjeldal, O.H., Stokke, O., Jakobs, C., Besley, G.T.N., Wraith, J.E. and Wanders, R.J.A. Refsum disease is caused by mutations in the phytanoyl-CoA hydroxylase gene. Nat. Genet. 17 (1997) 190-193. [PMID: 9326940]
4. Mihalik, S.J., Rainville, A.M. and Watkins, P.A. Phytanic acid α-oxidation in rat liver peroxisomes. Production of α-hydroxyphytanoyl-CoA and formate is enhanced by dioxygenase cofactors. Eur. J. Biochem. 232 (1995) 545-551.
5. Mihalik, S.J., Morrell, J.C., Kim, D., Sacksteder, K.A., Watkins, P.A. and Gould, S.J. Identification of PAHX, a Refsum disease gene. Nat. Genet. 17 (1997) 185-189. [PMID: 9326939]
Accepted name: leucocyanidin oxygenase
Reaction: leucocyanidin + 2-oxoglutarate + O2 = cis- and trans-dihydroquercetins + succinate + CO2 + 2 H2O
For diagram click here
Other name(s): anthocyanidin synthase
Systematic name: leucocyanidin,2-oxoglutarate:oxygen oxidoreductase
Comments: The enzyme requires Fe(II) and ascorbate. It is involved in the pathway by which many flowering plants make anthocyanin (glycosylated anthocyandin) flower pigments. The intermediates are transformed into cis- and trans-dihydroquercetin [2], which the enzyme can also oxidize to quercetin. Acidification of the products gives anthocyanidin [1], which, however, may not be a natural precursor of the anthocyanins.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 180984-01-4
References:
1. Saito, K., Kobayashi, M., Gong, Z., Tanaka, Y. and Yamazaki, M. Direct evidence for anthocyanidin synthase as a 2-oxoglutarate-dependent oxygenase: molecular cloning and functional expression of cDNA from a red forma of Perilla frutescens. Plant J. 17 (1999) 181-190. [PMID: 10074715]
2. Turnbull, J.J., Sobey, W.J., Aplin, R.T., Hassan, A., Firmin, J.L., Schofield, C.J. and Prescott, A.G. Are anthocyanidins the immediate products of anthocyanidin synthase? Chem. Commun. (2000) 2473-2474.
Accepted name: deacetoxyvindoline 4-hydroxylase
Reaction: deacetoxyvindoline + 2-oxoglutarate + O2 = deacetylvindoline + succinate + CO2
For reaction pathway click here.
Other name(s): desacetoxyvindoline 4-hydroxylase; desacetyoxyvindoline-17-hydroxylase; D17H; desacetoxyvindoline,2-oxoglutarate:oxygen oxidoreductase (4β-hydroxylating)
Systematic name: deacetoxyvindoline,2-oxoglutarate:oxygen oxidoreductase (4β-hydroxylating)
Comments: Requires Fe2+ and ascorbate. Also acts on 3-hydroxy-16-methoxy-2,3-dihydrotabersonine and to a lesser extent on 16-methoxy-2,3-dihydrotabersonine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 132084-83-4
References:
1. De Carolis, E., Chan, F., Balsevich, J. and De Luca, V. Isolation and characterization of a 2-oxoglutarate dependent dioxygenase involved in the 2nd-to-last step in vindoline biosynthesis Plant Physiol. 94 (1990) 1323-1329.
2. De Carolis, E. and De Luca, V. Purification, characterization, and kinetic analysis of a 2-oxoglutarate-dependent dioxygenase involved in vindoline biosynthesis from Catharanthus roseus. J. Biol. Chem. 268 (1993) 5504-5511. [PMID: 8449913]
3. Vazquez-Flota, F.A. and De Luca, V. Developmental and light regulation of desacetoxyvindoline 4-hydroxylase in Catharanthus roseus (L.) G. Don. Evidence of a multilevel regulatory mechanism. Plant Physiol. 117 (1998) 1351-1361. [PMID: 9701591]
Accepted name: clavaminate synthase
Reaction: (1) deoxyamidinoproclavaminate + 2-oxoglutarate + O2 = amidinoproclavaminate + succinate + CO2
(2) proclavaminate + 2-oxoglutarate + O2 = dihydroclavaminate + succinate + CO2 + H2O
(3) dihydroclavaminate + 2-oxoglutarate + O2 = clavaminate + succinate + CO2 + H2O
For diagram click here.
Other name(s): clavaminate synthase 2; clavaminic acid synthase
Systematic name: deoxyamidinoproclavaminate,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Comments: Contains nonheme iron. Catalyses three separate oxidative reactions in the pathway for the biosythesis of the β-lactamase inhibitor clavulanate in Streptomyces clavuligerus. The first step (hydroxylation) is separated from the latter two (oxidative cyclization and desaturation) by the action of EC 3.5.3.22, proclavaminate amidinohydrolase. The three reactions are all catalysed at the same nonheme iron site.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 122799-56-8
References:
1. Salowe, S.P., Krol, W.J., Iwatareuyl, D. and Townsend, C.A. Elucidation of the order of oxidations and identification of an intermediate in the multistep clavaminate synthase reaction. Biochemistry 30 (1991) 2281-2292. [PMID: 1998687]
2. Zhou, J., Gunsior, M., Bachmann, B.O., Townsend, C.A. and Solomon, E.I. Substrate binding to the α-ketoglutarate-dependent non-heme iron enzyme clavaminate synthase 2: Coupling mechanism of oxidative decarboxylation and hydroxylation. J. Am. Chem. Soc. 120 (1998) 13539-13540.
3. Zhang, Z.H., Ren, J.S., Stammers, D.K., Baldwin, J.E., Harlos, K. and Schofield, C.J. Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase. Nat. Struct. Biol. 7 (2000) 127-133. [PMID: 10655615]
4. Zhou, J., Kelly, W.L., Bachmann, B.O., Gunsior, M., Townsend, C.A. and Solomon, E.I. Spectroscopic studies of substrate interactions with clavaminate synthase 2, a multifunctional α-KG-dependent non-heme iron enzyme: Correlation with mechanisms and reactivities. J. Am. Chem. Soc. 123 (2001) 7388-7398.
5. Townsend, C.A. New reactions in clavulanic acid biosynthesis. Curr. Opin. Chem. Biol. 6 (2002) 583-589. [PMID: 12413541]
Accepted name: flavone synthase
Reaction: a flavanone + 2-oxoglutarate + O2 = a flavone + succinate + CO2 + H2O
See diagram for reaction in apigenin or luteolin biosynthesis.
Other Name(s): flavone synthase I; FNS I
Systematic name: flavanone,2-oxoglutarate:oxygen oxidoreductase (dehydrating)
Comments: Requires ascorbate for full activity and Fe2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 138263-98-6
References: (if your browser cannot recognise unicode the author is Lukacin with a hacek over the c)
1. Martens, S., Forkmann, G., Matern, U. and Lukačin, R. Cloning of parsley flavone synthase I. Phytochemistry 58 (2001) 43-46. [PMID: 11524111]
2. Lukačin, R., Matern, U., Junghanns, K.T., Heskamp, M.L., Britsch, L., Forkmann, G. and Martens, S. Purification and antigenicity of flavone synthase I from irradiated parsley cells. Arch. Biochem. Biophys. 393 (2001) 177-183. [PMID: 11516175]
3. Martens, S., Forkmann, G., Britsch, L., Wellmann, F., Matern, U. and Lukačin, R. Divergent evolution of flavonoid 2-oxoglutarate-dependent dioxygenases in parsley. FEBS Lett. 544 (2003) 93-98. [PMID: 12782296]
Accepted name: flavonol synthase
Reaction: a dihydroflavonol + 2-oxoglutarate + O2 = a flavonol + succinate + CO2 + H2O
See diagram for reaction in quercetin or kaempferol or myricetin biosynthesis.
Other Name(s): flavonoid 2-oxoglutarate-dependent dioxygenase; FLS
Systematic name: dihydroflavonol,2-oxoglutarate:oxygen oxidoreductase
Comments: In addition to the desaturation of (2R,3R)-dihydroflavonols to flavonols, the enzyme from the satsuma Citrus unshiu also has a non-specific activity that trans-hydroxylates the flavanones (2S)-naringenin and the unnatural (2R)-naringenin at C-3 to kaempferol and (2R,3R)-dihydrokaempferol, respectively [2]. Requires Fe2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 146359-76-4
References: (if your browser cannot recognise unicode the author is Lukacin with a hacek over the c)
1. Wellmann, F., Lukačin, R., Moriguchi, T., Britsch, L., Schiltz, E. and Matern, U. Functional expression and mutational analysis of flavonol synthase from Citrus unshiu. Eur. J. Biochem. 269 (2002) 4134-4142. [PMID: 12180990]
2. Lukačin, R., Wellmann, F., Britsch, L., Martens, S. and Matern, U. Flavonol synthase from Citrus unshiu is a bifunctional dioxygenase. Phytochemistry 62 (2003) 287-292. [PMID: 12620339]
3. Martens, S., Forkmann, G., Britsch, L., Wellmann, F., Matern, U. and Lukačin, R. Divergent evolution of flavonoid 2-oxoglutarate-dependent dioxygenases in parsley. FEBS Lett. 544 (2003) 93-98. [PMID: 12782296]
4. Turnbull, J.J., Nakajima, J., Welford, R.W., Yamazaki, M., Saito, K. and Schofield, C.J. Mechanistic studies on three 2-oxoglutarate-dependent oxygenases of flavonoid biosynthesis: anthocyanidin synthase, flavonol synthase, and flavanone 3β-hydroxylase. J. Biol. Chem. 279 (2004) 1206-1216. [PMID: 14570878]
Accepted name: 2'-deoxymugineic-acid 2'-dioxygenase
Reaction: 2'-deoxymugineic acid + 2-oxoglutarate + O2 = mugineic acid + succinate + CO2
For diagram click here.
Other name(s): IDS3
Systematic name: 2'-deoxymugineic acid,2-oxoglutarate:oxygen oxidoreductase (2-hydroxylating)
Comments: Requires iron(II). It is also likely that this enzyme can catalyse the hydroxylation of 3-epihydroxy-2'-deoxymugineic acid to form 3-epihydroxymugineic acid.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 133758-62-0
References:
1. Nakanishi, H., Yamaguchi, H., Sasakuma, T., Nishizawa, N.K. and Mori, S. Two dioxygenase genes, Ids3 and Ids2, from Hordeum vulgare are involved in the biosynthesis of mugineic acid family phytosiderophores. Plant Mol. Biol. 44 (2000) 199-207. [PMID: 11117263]
2. Kobayashi, T., Nakanishi, H., Takahashi, M., Kawasaki, S., Nishizawa, N.K. and Mori, S. In vivo evidence that Ids3 from Hordeum vulgare encodes a dioxygenase that converts 2'-deoxymugineic acid to mugineic acid in transgenic rice. Planta 212 (2001) 864-871. [PMID: 11346963]
Accepted name: mugineic-acid 3-dioxygenase
Reaction: (1) mugineic acid + 2-oxoglutarate + O2 = 3-epihydroxymugineic acid + succinate + CO2
(2) 2'-deoxymugineic acid + 2-oxoglutarate + O2 = 3-epihydroxy-2'-deoxymugineic acid + succinate + CO2
For diagram click here.
Other name(s): IDS2
Systematic name: mugineic acid,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Comments: Requires iron(II).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Nakanishi, H., Yamaguchi, H., Sasakuma, T., Nishizawa, N.K. and Mori, S. Two dioxygenase genes, Ids3 and Ids2, from Hordeum vulgare are involved in the biosynthesis of mugineic acid family phytosiderophores. Plant Mol. Biol. 44 (2000) 199-207. [PMID: 11117263]
2. Okumura, N., Nishizawa, N.K., Umehara, Y., Ohata, T., Nakanishi, H., Yamaguchi, T., Chino, M. and Mori. S. A dioxygenase gene (Ids2) expressed under iron deficiency conditions in the roots of Hordeum vulgare. Plant Mol. Biol. 25 (1994) 705-719. [PMID: 8061321]
Accepted name: deacetoxycephalosporin-C hydroxylase
Reaction: deacetoxycephalosporin C + 2-oxoglutarate + O2 = deacetylcephalosporin C + succinate + CO2
For diagram click here.
Other name(s): deacetylcephalosporin C synthase; 3'-methylcephem hydroxylase; DACS; DAOC hydroxylase; deacetoxycephalosporin C hydroxylase
Systematic name: deacetoxycephalosporin-C,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Comments: Requires iron(II). The enzyme can also use 3-exomethylenecephalosporin C as a substrate to form deacetoxycephalosporin C, although more slowly [2]. In Acremonium chrysogenum, the enzyme forms part of a bifunctional protein along with EC 1.14.20.1, deactoxycephalosporin-C synthase. It is a separate enzyme in Streptomyces clavuligerus.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 69772-89-0
References:
1. Dotzlaf, J.E. and Yeh, W.K. Copurification and characterization of deacetoxycephalosporin C synthetase/hydroxylase from Cephalosporium acremonium. J. Bacteriol. 169 (1987) 1611-1618. [PMID: 3558321]
2. Baker, B.J., Dotzlaf, J.E. and Yeh, W.K. Deacetoxycephalosporin C hydroxylase of Streptomyces clavuligerus. Purification, characterization, bifunctionality, and evolutionary implication. J. Biol. Chem. 266 (1991) 5087-5093. [PMID: 2002049]
3. Coque, J.J., Enguita, F.J., Cardoza, R.E., Martin, J.F. and Liras, P. Characterization of the cefF gene of Nocardia lactamdurans encoding a 3'-methylcephem hydroxylase different from the 7-cephem hydroxylase. Appl. Microbiol. Biotechnol. 44 (1996) 605-609. [PMID: 8703431]
4. Ghag, S.K., Brems, D.N., Hassell, T.C. and Yeh, W.K. Refolding and purification of Cephalosporium acremonium deacetoxycephalosporin C synthetase/hydroxylase from granules of recombinant Escherichia coli. Biotechnol. Appl. Biochem. 24 (1996) 109-119. [PMID: 8865604]
5. Lloyd, M.D., Lipscomb, S.J., Hewitson, K.S., Hensgens, C.M., Baldwin, J.E. and Schofield, C.J. Controlling the substrate selectivity of deacetoxycephalosporin/deacetylcephalosporin C synthase. J. Biol. Chem. 279 (2004) 15420-15426. [PMID: 14734549]
6. Wu, X.B., Fan, K.Q., Wang, Q.H. and Yang, K.Q. C-terminus mutations of Acremonium chrysogenum deacetoxy/deacetylcephalosporin C synthase with improved activity toward penicillin analogs. FEMS Microbiol. Lett. 246 (2005) 103-110. [PMID: 15869968]
7. Martín, J.F., Gutiérrez, S., Fernández, F.J., Velasco, J., Fierro, F., Marcos, A.T. and Kosalkova, K. Expression of genes and processing of enzymes for the biosynthesis of penicillins and cephalosporins. Antonie Van Leeuwenhoek 65 (1994) 227-43. [PMID: 7847890]
Accepted name: [histone-H3]-lysine-36 demethylase
Reaction: protein N6,N6-dimethyl-L-lysine + 2 2-oxoglutarate + 2 O2 = protein L-lysine + 2 succinate + 2 formaldehyde + 2 CO2 (overall reaction)
(1a) protein-N6,N6-dimethyl-L-lysine + 2-oxoglutarate + O2 = protein-N6-methyl-L-lysine + succinate + formaldehyde + CO2
(1b) protein-N6-methyl-L-lysine + 2-oxoglutarate + O2 = protein-L-lysine + succinate + formaldehyde + CO2
Other name(s): JHDM1A; JmjC domain-containing histone demethylase 1A; H3-K36-specific demethylase; histone-lysine (H3-K36) demethylase; histone demethylase; protein-6-N,6-N-dimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase
Systematic name: protein-N6,N6-dimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase
Comments: Requires iron(II). Of the seven potential methylation sites in histones H3 (K4, K9, K27, K36, K79) and H4 (K20, R3) from HeLa cells, the enzyme is specific for Lys-36. Lysine residues exist in three methylation states (mono-, di- and trimethylated). The enzyme preferentially demethylates the dimethyl form of Lys-36 (K36me2), which is its natural substrate, to form the monomethyl and unmethylated forms of Lys-36. It can also demethylate the monomethyl- but not the trimethyl form of Lys-36.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Tsukada, Y., Fang, J., Erdjument-Bromage, H., Warren, M.E., Borchers, C.H., Tempst, P. and Zhang, Y. Histone demethylation by a family of JmjC domain-containing proteins. Nature 439 (2006) 811-816. [PMID: 16362057]
Accepted name: proline 3-hydroxylase
Reaction: L-proline + 2-oxoglutarate + O2 = cis-3-hydroxy-L-proline + succinate + CO2
For diagram click here.
Other name(s): P-3-H
Systematic name: L-proline,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Comments: Requires iron(II) for activity. Unlike the proline hydroxylases involved in collagen biosynthesis [EC 1.14.11.2 (procollagen-proline dioxygenase) and EC 1.14.11.7 (procollagen-proline 3-dioxygenase)], this enzyme does not require ascorbate for activity although it does increase the activity of the enzyme [2]. The enzyme is specific for L-proline as D-proline, trans-4-hydroxy-L-proline, cis-4-hydroxy-L-proline and 3,4-dehydro-DL-proline are not substrates [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 162995-24-6
References:
1. Mori, H., Shibasaki, T., Uozaki, Y., Ochiai, K. and Ozaki, A. Detection of novel proline 3-hydroxylase activities in Streptomyces and Bacillus spp. by regio- and stereospecific hydroxylation of L-proline. Appl. Environ. Microbiol. 62 (1996) 1903-1907. [PMID: 16535329]
2. Mori, H., Shibasaki, T., Yano, K. and Ozaki, A. Purification and cloning of a proline 3-hydroxylase, a novel enzyme which hydroxylates free L-proline to cis-3-hydroxy-L-proline. J. Bacteriol. 179 (1997) 5677-5683. [PMID: 9294421]
3. Clifton, I.J., Hsueh, L.C., Baldwin, J.E., Harlos, K. and Schofield, C.J. Structure of proline 3-hydroxylase. Evolution of the family of 2-oxoglutarate dependent oxygenases. Eur. J. Biochem. 268 (2001) 6625-6636. [PMID: 11737217]
Accepted name: hypoxia-inducible factor-proline dioxygenase
Reaction: hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 = hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
Other name(s): HIF hydroxylase
Systematic name: hypoxia-inducible factor-L-proline, 2-oxoglutarate:oxygen oxidoreductase (4-hydroxylating)
Comments: Contains iron, and requires ascorbate. Specifically hydroxylates a proline residue in HIF-α, the α subunit of the transcriptional regulator HIF (hypoxia-inducible factor), which targets HIF for proteasomal destruction. The requirement of oxygen for the hydroxylation reaction enables animals to respond to hypoxia.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Jaakkola, P., Mole, D.R., Tian, Y.M., Wilson, M.I., Gielbert, J., Gaskell, S.J., Kriegsheim Av, Hebestreit, H.F., Mukherji, M., Schofield, C.J., Maxwell, P.H., Pugh, C.W. and Ratcliffe, P.J. Targeting of HIF-α to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation. Science 292 (2001) 468-472. [PMID: 11292861]
2. Ivan, M., Kondo, K., Yang, H., Kim, W., Valiando, J., Ohh, M., Salic, A., Asara, J.M., Lane, W.S. and Kaelin , W.G., Jr. HIFα targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing. Science 292 (2001) 464-468. [PMID: 11292862]
3. Bruick, R.K. and McKnight, S.L. A conserved family of prolyl-4-hydroxylases that modify HIF. Science 294 (2001) 1337-1340. [PMID: 11598268]
4. Epstein, A.C., Gleadle, J.M., McNeill, L.A., Hewitson, K.S., O'Rourke, J., Mole, D.R., Mukherji, M., Metzen, E., Wilson, M.I., Dhanda, A., Tian, Y.M., Masson, N., Hamilton, D.L., Jaakkola, P., Barstead, R., Hodgkin, J., Maxwell, P.H., Pugh, C.W., Schofield, C.J. and Ratcliffe, P.J. C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 107 (2001) 43-54. [PMID: 11595184]
5. Oehme, F., Ellinghaus, P., Kolkhof, P., Smith, T.J., Ramakrishnan, S., Hutter, J., Schramm, M. and Flamme, I. Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors. Biochem. Biophys. Res. Commun. 296 (2002) 343-349. [PMID: 12163023]
6. McNeill, L.A., Hewitson, K.S., Gleadle, J.M., Horsfall, L.E., Oldham, N.J., Maxwell, P.H., Pugh, C.W., Ratcliffe, P.J. and Schofield, C.J. The use of dioxygen by HIF prolyl hydroxylase (PHD1). Bioorg. Med. Chem. Lett. 12 (2002) 1547-1550. [PMID: 12039559]
Accepted name: hypoxia-inducible factor-asparagine dioxygenase
Reaction: hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2 = hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2
Other name(s): HIF hydroxylase
Systematic name: hypoxia-inducible factor-L-asparagine, 2-oxoglutarate:oxygen oxidoreductase (4-hydroxylating)
Comments: Contains iron, and requires ascorbate. Catalyses hydroxylation of an asparagine in the C-terminal transcriptional activation domain of HIF-α, the α subunit of the transcriptional regulator HIF (hypoxia-inducible factor), which reduces its interaction with the transcriptional coactivator protein p300. The requirement of oxygen for the hydroxylation reaction enables animals to respond to hypoxia.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Mahon, P.C., Hirota, K. and Semenza, G.L. FIH-1: a novel protein that interacts with HIF-1α and VHL to mediate repression of HIF-1 transcriptional activity. Genes Dev. 15 (2001) 2675-2686. [PMID: 11641274]
2. Hewitson, K.S., McNeill, L.A., Riordan, M.V., Tian, Y.M., Bullock, A.N., Welford, R.W., Elkins, J.M., Oldham, N.J., Bhattacharya, S., Gleadle, J.M., Ratcliffe, P.J., Pugh, C.W. and Schofield, C.J. Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family. J. Biol. Chem. 277 (2002) 26351-26355. [PMID: 12042299]
4. Lando, D., Peet, D.J., Whelan, D.A., Gorman, J.J. and Whitelaw, M.L. Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch. Science 295 (2002) 858-861. [PMID: 11823643]
5. Koivunen, P., Hirsila, M., Gunzler, V., Kivirikko, K.I. and Myllyharju, J. Catalytic properties of the asparaginyl hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases. J. Biol. Chem. 279 (2004) 9899-9904. [PMID: 14701857]
6. Elkins, J.M., Hewitson, K.S., McNeill, L.A., Seibel, J.F., Schlemminger, I., Pugh, C.W., Ratcliffe, P.J. and Schofield, C.J. Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 α. J. Biol. Chem. 278 (2003) 1802-1806. [PMID: 12446723]
Accepted name: thebaine 6-O-demethylase
Reaction: thebaine + 2-oxoglutarate + O2 = neopinone + formaldehyde + succinate + CO2
Other name(s): T6ODM
Systematic name: thebaine,2-oxoglutarate:oxygen oxidoreductase (6-O-demethylating)
Comments: Requires Fe2+. Catalyses a step in morphine biosynthesis. The product neopinione spontaneously rearranges to the more stable codeinone. The enzyme also catalyses the 6-O-demethylation of oripavine to morphinone, with lower efficiency.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Hagel, J.M. and Facchini, P.J. Dioxygenases catalyze the O-demethylation steps of morphine biosynthesis in opium poppy. Nat. Chem. Biol. 6 (2010) 273-275. [PMID: 20228795]
Accepted name: codeine 3-O-demethylase
Reaction: codeine + 2-oxoglutarate + O2 = morphine + formaldehyde + succinate + CO2
Other name(s): codeine O-demethylase; CODM
Systematic name: codeine,2-oxoglutarate:oxygen oxidoreductase (3-O-demethylating)
Comments: Requires Fe2+. Catalyses a step in morphine biosynthesis. The enzyme also catalyses the 3-O-demethylation of thebaine to oripavine, with lower efficiency.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Hagel, J.M. and Facchini, P.J. Dioxygenases catalyze the O-demethylation steps of morphine biosynthesis in opium poppy. Nat. Chem. Biol. 6 (2010) 273-275. [PMID: 20228795]
Accepted name: DNA oxidative demethylase
Reaction: DNA-base-CH3 + 2-oxoglutarate + O2 = DNA-base + formaldehyde + succinate + CO2
Other name(s): alkylated DNA repair protein; α-ketoglutarate-dependent dioxygenase ABH1; alkB (gene name)
Systematic name: Methyl DNA-base, 2-oxoglutarate:oxygen oxidoreductase (formaldehyde-forming)
Comments: Contains iron; activity is slightly stimulated by ascorbate. Catalyses oxidative demethylation of the DNA base lesions N1-methyladenine, N3-methylcytosine, N1-methylguanine, and N3-methylthymine. It works better on single-stranded DNA (ssDNA) and is capable of repairing damaged bases in RNA.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Falnes, P.O., Johansen, R.F. and Seeberg, E. AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli. Nature 419 (2002) 178-182. [PMID: 12226668]
2. Yi, C., Yang, C.G. and He, C. A non-heme iron-mediated chemical demethylation in DNA and RNA. Acc. Chem. Res. 42 (2009) 519-529. [PMID: 19852088]
3. Yi, C., Jia, G., Hou, G., Dai, Q., Zhang, W., Zheng, G., Jian, X., Yang, C.G., Cui, Q. and He, C. Iron-catalysed oxidation intermediates captured in a DNA repair dioxygenase. Nature 468 (2010) 330-333. [PMID: 21068844]
EC 1.14.11.34
Accepted name: 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming)
Reaction: 2-oxoglutarate + L-arginine + O2 = succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O (overall reaction)
Other name(s): ethylene-forming enzyme; EFE
Systematic name: L-arginine,2-oxoglutarate:oxygen oxidoreductase (succinate-forming)
Comments: This is one of two simultaneous reactions catalysed by the enzyme, which is responsible for ethylene production in bacteria of the Pseudomonas syringae group. In the other reaction [EC 1.13.12.19, 2-oxoglutarate dioxygenase (ethylene-forming)] the enzyme catalyses the dioxygenation of 2-oxoglutarate forming ethylene and three molecules of carbon dioxide. The enzyme catalyses two cycles of the ethylene-forming reaction for each cycle of the succinate-forming reaction, so that the stoichiometry of the products ethylene and succinate is 2:1.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Nagahama, K., Ogawa, T., Fujii, T., Tazaki, M., Tanase, S., Morino, Y. and Fukuda, H. Purification and properties of an ethylene-forming enzyme from Pseudomonas syringae pv. phaseolicola PK2. J. Gen. Microbiol. 137 (1991) 2281-2286. [PMID: 1770346]
2. Fukuda, H., Ogawa, T., Tazaki, M., Nagahama, K., Fujii, T., Tanase, S. and Morino, Y. Two reactions are simultaneously catalyzed by a single enzyme: the arginine-dependent simultaneous formation of two products, ethylene and succinate, from 2-oxoglutarate by an enzyme from Pseudomonas syringae. Biochem. Biophys. Res. Commun. 188 (1992) 483-489. [PMID: 1445291]
3. Fukuda, H., Ogawa, T., Ishihara, K., Fujii, T., Nagahama, K., Omata, T., Inoue, Y., Tanase, S. and Morino, Y. Molecular cloning in Escherichia coli, expression, and nucleotide sequence of the gene for the ethylene-forming enzyme of Pseudomonas syringae pv. phaseolicola PK2. Biochem. Biophys. Res. Commun. 188 (1992) 826-832. [PMID: 1445325]
Accepted name: 1-deoxypentalenic acid 11β-hydroxylase
Reaction: 1-deoxypentalenate + 2-oxoglutarate + O2 = 1-deoxy-11β-hydroxypentalenate + succinate + CO2
For diagram of reaction click here.
Glossary: 1-deoxypentalenate = (1R,3aR,5aS,8aR)-1,7,7-trimethyl-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene-4-carboxylate
Other name(s): ptlH (gene name); sav2991 (gene name); pntH (gene name)
Systematic name: 1-deoxypentalenic acid,2-oxoglutarate:oxygen oxidoreductase
Comments: The enzyme requires Fe(II) and ascorbate. Isolated from the bacterium Streptomyces avermitilis. Part of the pathway for pentalenolactone biosynthesis.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. You, Z., Omura, S., Ikeda, H. and Cane, D.E. Pentalenolactone biosynthesis. Molecular cloning and assignment of biochemical function to PtlH, a non-heme iron dioxygenase of Streptomyces avermitilis. J. Am. Chem. Soc. 128 (2006) 6566-6567. [PMID: 16704250]
2. You, Z., Omura, S., Ikeda, H., Cane, D.E. and Jogl, G. Crystal structure of the non-heme iron dioxygenase PtlH in pentalenolactone biosynthesis. J. Biol. Chem. 282 (2007) 36552-36560. [PMID: 17942405]
Accepted name: pentalenolactone F synthase
Reaction: pentalenolactone D + 2 2-oxoglutarate + 2 O2 = pentalenolactone F + 2 succinate + 2 CO2 + H2O (overall reaction)
For diagram of reaction click here.
Glossary: pentalenolactone D = (1S,4aR,6aS,9aR)-1,8,8-trimethyl-2-oxo-1,2,4,4a,6a,7,8,9-octahydropentaleno[1,6a-c]pyran-5-carboxylate
Other name(s): penD (gene name); pntD (gene name); ptlD (gene name)
Systematic name: pentalenolactone-D,2-oxoglutarate:oxygen oxidoreductase
Comments: Requires Fe(II) and ascorbate. Isolated from the bacteria Streptomyces exfoliatus, Streptomyces arenae and Streptomyces avermitilis. Part of the pentalenolactone biosynthesis pathway.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Seo, M.J., Zhu, D., Endo, S., Ikeda, H. and Cane, D.E. Genome mining in Streptomyces. Elucidation of the role of Baeyer-Villiger monooxygenases and non-heme iron-dependent dehydrogenase/oxygenases in the final steps of the biosynthesis of pentalenolactone and neopentalenolactone. Biochemistry 50 (2011) 1739-1754. [PMID: 21250661]
(1a) 2-oxoglutarate + L-arginine + O2 = succinate + CO2 + L-hydroxyarginine
(1b) L-hydroxyarginine = guanidine + (S)-1-pyrroline-5-carboxylate + H2O
1-deoxy-11β-hydroxypentalenate = (1S,2R,3aR,5aS,8aR)-2-hydroxy-1,7,7-trimethyl-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene-4-carboxylate
(1a) pentalenolactone D + 2-oxoglutarate + O2 = pentalenolactone E + succinate + CO2 + H2O
(1b) pentalenolactone E + 2-oxoglutarate + O2 = pentalenolactone F + succinate + CO2
pentalenolactone E = (4aR,6aS,9aR)-8,8-dimethyl-1-methylene-2-oxo-1,2,4,4a,6a,7,8,9-octahydropentaleno[1,6a-c]pyran-5-carboxylate
pentalenolactone F = (1'R,4'aR,6'aS,9'aR)-8',8'-dimethyl-2'-oxo-4',4'a,6'a,8',9'-hexahydrospiro[oxirane-2,1'-pentaleno[1,6a-c]pyran]-5'-carboxylic acid
EC 1.14.12 With NADH or NADPH as one donor, and incorporation of two atoms of oxygen into one donor
Accepted name: anthranilate 1,2-dioxygenase (deaminating, decarboxylating)
Reaction: anthranilate + NAD(P)H + 2 H+ + O2 = catechol + CO2 + NAD(P)+ + NH3
For diagram click here.
Other name(s): anthranilate hydroxylase; anthranilic hydroxylase; anthranilic acid hydroxylase
Systematic name: anthranilate,NAD(P)H:oxygen oxidoreductase (1,2-hydroxylating, deaminating, decarboxylating)
Comments: Requires Fe2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 9059-17-0
References:
1. Kobayashi, S. and Hayaishi, O. Anthranilic acid conversion to catechol (Pseudomonas). Methods Enzymol. 17A (1970) 505-510.
2. Taniguchi, H., Hatanaka, M., Kuno, S., Hayaishi, O., Nakajima, M. and Kurihara, N. Enzymatic formation of catechol from anthranilic acid. J. Biol. Chem. 239 (1964) 2204-2211.
[EC 1.14.12.2 Transferred entry: now EC 1.14.13.35 anthranilate 3-monooxygenase (deaminating) (EC 1.14.12.2 created 1972, deleted 1990)]
Accepted name: benzene 1,2-dioxygenase
Reaction: benzene + NADH + H+ + O2 = cis-cyclohexa-3,5-diene-1,2-diol + NAD+
For diagram click here.
Other name(s): benzene hydroxylase; benzene dioxygenase
Systematic name: benzene,NADH:oxygen oxidoreductase (1,2-hydroxylating)
Comments: A system, containing a reductase which is an iron-sulfur flavoprotein (FAD), an iron-sulfur oxygenase and ferredoxin. Requires Fe2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9075-66-5
References:
1. Gibson, D.T., Koch, J.R. and Kallio, R.E. Oxidative degradation of aromatic hydrocarbons by microorganisms. I. Enzymatic formation of catechol from benzene. Biochemistry 7 (1968) 2653-2662. [PMID: 4298226]
Accepted name: 3-hydroxy-2-methylpyridinecarboxylate dioxygenase
Reaction: 3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2 = 2-(acetamidomethylene)succinate + NAD(P)+
Other name(s): methylhydroxypyridinecarboxylate oxidase; 2-methyl-3-hydroxypyridine 5-carboxylic acid dioxygenase; methylhydroxypyridine carboxylate dioxygenase; 3-hydroxy-3-methylpyridinecarboxylate dioxygenase [incorrect]
Systematic name: 3-hydroxy-2-methylpyridine-5-carboxylate,NAD(P)H:oxygen oxidoreductase (decyclizing)
Comments: A flavoprotein (FAD).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 37256-69-2
References:
1. Sparrow, L.G., Ho, P.P.K., Sundaram, T.K., Zach, D., Nyns, E.J. and Snell, E.E. The bacterial oxidation of vitamin B6. VII. Purification, properties, and mechanism of action of an oxygenase which cleaves the 3-hydroxypyridine ring. J. Biol. Chem. 244 (1969) 2590-2600. [PMID: 4306031]
Accepted name: 5-pyridoxate dioxygenase
Reaction: 3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate + NADPH + H+ + O2 = 2-(acetamidomethylene)-3-(hydroxymethyl)succinate + NADP+
Other name(s): 5-pyridoxate oxidase
Systematic name: 5-pyridoxate,NADPH:oxygen oxidoreductase (decyclizing)
Comments: A flavoprotein.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 37256-70-5
References:
1. Sparrow, L.G., Ho, P.P.K., Sundaram, T.K., Zach, D., Nyns, E.J. and Snell, E.E. The bacterial oxidation of vitamin B6. VII. Purification, properties, and mechanism of action of an oxygenase which cleaves the 3-hydroxypyridine ring. J. Biol. Chem. 244 (1969) 2590-2600. [PMID: 4306031]
[EC 1.14.12.6 Transferred entry: now EC 1.14.13.66 2-hydroxycyclohexanone 2-monooxygenase (EC 1.14.12.6 created 1978, deleted 1999)]
Accepted name: phthalate 4,5-dioxygenase
Reaction: phthalate + NADH + H+ + O2 = cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate + NAD+
For diagram click here.
Other name(s): PDO ; phthalate dioxygenase
Systematic name: phthalate,NADH:oxygen oxidoreductase (4,5-hydroxylating)
Comments: A system, containing a reductase which is an iron-sulfur flavoprotein (FMN), an iron-sulfur oxygenase, and no independent ferredoxin. Requires Fe2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 63626-44-8
References:
1. Batie, C.J., Lattaie, E. and Ballou, D.P. Purification and characterization of phthalate oxygenase and phthalate oxygenase reductase from Pseudomonas cepacia. J. Biol. Chem. 262 (1987) 1510-1518. [PMID: 3805038]
Accepted name: 4-sulfobenzoate 3,4-dioxygenase
Reaction: 4-sulfobenzoate + NADH + H+ + O2 = 3,4-dihydroxybenzoate + sulfite + NAD+
For diagram click here.
Other name(s): 4-sulfobenzoate dioxygenase; 4-sulfobenzoate 3,4-dioxygenase system
Systematic name: 4-sulfobenzoate,NADH:oxygen oxidoreductase (3,4-hydroxylating, sulfite-forming)
Comments: A system, containing a reductase which is an iron-sulfur flavoprotein (FMN), an iron-sulfur oxygenase, and no independent ferredoxin. Requires Fe2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 122933-81-7
References:
1. Locher, H.H., Leisinger, T. and Cook, A.M. 4-Sulphobenzoate 3,4-dioxygenase. Purification and properties of a desulphonative two-component enzyme system from Comamonas testosteroni T-2. Biochem. J. 274 (1991) 833-842. [PMID: 2012609]
Accepted name: 4-chlorophenylacetate 3,4-dioxygenase
Reaction: 4-chlorophenylacetate + NADH + H+ + O2 = 3,4-dihydroxyphenylacetate + chloride + NAD+
For diagram click here.
Systematic name: 4-chlorophenylacetate,NADH:oxygen oxidoreductase (3,4-hydroxylating, dechlorinating)
Comments: A system, containing a reductase and an iron-sulfur oxygenase, and no independent ferredoxin. Requires Fe2+. Also acts on 4-bromophenyl acetate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 105006-00-6
References:
1. Markus, A., Krekel, D. and Lingens, F. Purification and some properties of component A of the 4-chlorophenylacetate 3,4-dioxygenase from Pseudomonas species strain CBS. J. Biol. Chem. 261 (1986) 12883-12888. [PMID: 3745216]
Accepted name: benzoate 1,2-dioxygenase
Reaction: benzoate + NADH + H+ + O2 = (1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
For diagram click here (another example).
Other name(s): benzoate hydroxylase; benzoate hydroxylase; benzoic hydroxylase; benzoate dioxygenase; benzoate,NADH:oxygen oxidoreductase (1,2-hydroxylating, decarboxylating) [incorrect]
Systematic name: benzoate,NADH:oxygen oxidoreductase (1,2-hydroxylating)
Comments: A system, containing a reductase which is an iron-sulfur flavoprotein (FAD), and an iron-sulfur oxygenase. Requires Fe2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9059-18-1
References:
1. Yamaguchi, M. and Fujisawa, H. Characterization of NADH-cytochrome c reductase, a component of benzoate 1,2-dioxygenase system from Pseudomonas arvilla C-1. J. Biol. Chem. 253 (1978) 8848-8853. [PMID: 214433]
2. Yamaguchi, M. and Fujisawa, H. Purification and characterization of an oxygenase component in benzoate 1,2-dioxygenase system from Pseudomonas arvilla C-1. J. Biol. Chem. 255 (1980) 5058-5063. [PMID: 7372624]
3. Yamaguchi, M. and Fujisawa, H. Subunit structure of oxygenase component in benzoate-1,2-dioxygenase system from Pseudomonas arvilla C-1. J. Biol. Chem. 257 (1982) 12497-12502. [PMID: 7130163]
Accepted name: toluene dioxygenase
Reaction: toluene + NADH + H+ + O2 = (1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+
For diagram click here.
Other name(s): toluene 2,3-dioxygenase
Systematic name: toluene,NADH:oxygen oxidoreductase (1,2-hydroxylating)
Comments: A system, containing a reductase which is an iron-sulfur flavoprotein (FAD), an iron-sulfur oxygenase, and a ferredoxin. Some other aromatic compounds, including ethylbenzene, 4-xylene and some halogenated toluenes, are converted into the corresponding cis-dihydrodiols.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 120038-36-0
References:
1. Renganathan, V. Possible involvement of toluene-2,3-dioxygenase in defluorination of 3-fluoro-substituted benzenes by toluene-degrading Pseudomonas sp. strain T-12. Appl. Exp. Microbiol. 55 (1989) 330-334.
2. Subramanian, V., Liu, T.-N., Yeh, W.K. and Gibson, D.T. Toluene dioxygenase: purification of an iron-sulfur protein by affinity chromatography. Biochem. Biophys. Res. Commun. 91 (1979) 1131-1139. [PMID: 526270]
Accepted name: naphthalene 1,2-dioxygenase
Reaction: naphthalene + NADH + H+ + O2 = (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
For diagram of reaction click here and related reactions click here.
Other name(s): naphthalene dioxygenase; naphthalene oxygenase
Systematic name: naphthalene,NADH:oxygen oxidoreductase (1,2-hydroxylating)
Comments: This enzyme is a member of the ring-hydroxylating dioxygenase (RHD) family of bacterial enzymes that play a critical role in the degradation of aromatic compounds, such as polycyclic aromatic hydrocarbons [5]. This enzyme comprises a multicomponent system, containing a reductase that is an iron-sulfur flavoprotein (FAD; EC 1.18.1.3, ferredoxin—NAD+ reductase), an iron-sulfur oxygenase, and ferredoxin. Requires Fe2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9074-04-8
References:
1. Ensley, B.D. and Gibson, D.T. Naphthalene dioxygenase: purification and properties of a terminal oxygenase component. J. Bacteriol. 155 (1983) 505-511. [PMID: 6874638]
2. Jeffrey, A.M., Yeh, H.J.C., Jerina, D.M., Patel, T.R., Davey, J.F. and Gibson, D.T. Initial reactions in the oxidation of naphthalene by Pseudomonas putida. Biochemistry 14 (1975) 575-584. [PMID: 234247]
3. Kauppi, B., Lee, K., Carredano, E., Parales, R.E., Gibson, D.T., Eklund, H. and Ramaswamy, S. Structure of an aromatic-ring-hydroxylating dioxygenase - naphthalene 1,2-dioxygenase. Structure 6 (1998) 571-586. [PMID: 9634695]
4. Parales, R.E., Lee, K., Resnick, S.M., Jiang, H., Lessner, D.J. and Gibson, D.T. Substrate specificity of naphthalene dioxygenase: effect of specific amino acids at the active site of the enzyme. J. Bacteriol. 182 (2000) 1641-1649. [PMID: 10692370]
5. Jouanneau, Y., Meyer, C., Jakoncic, J., Stojanoff, V. and Gaillard, J. Characterization of a naphthalene dioxygenase endowed with an exceptionally broad substrate specificity toward polycyclic aromatic hydrocarbons. Biochemistry 45 (2006) 12380-12391. [PMID: 17014090]
Accepted name: 2-halobenzoate 1,2-dioxygenase
Reaction: a 2-halobenzoate + NADH + H+ + O2 = catechol + a halide anion + NAD+ + CO2
For diagram of reaction click here and mechanism click here.
Other name(s): 2-chlorobenzoate 1,2-dioxygenase
Systematic name: 2-halobenzoate,NADH:oxygen oxidoreductase (1,2-hydroxylating, dehalogenating, decarboxylating)
Comments: A multicomponent enzyme system composed of a dioxygenase component and an electron transfer component. The latter contains FAD. The enzyme, characterized from the bacterium Burkholderia cepacia 2CBS, has a broad substrate specificity. Substrates include 2-fluorobenzoate, 2-chlorobenzoate, 2-bromobenzoate, and 2-iodobenzoate, which are processed in this order of preference.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 125268-83-9
References:
1. Fetzner, S., Mueller, R. and Lingens, F. Degradation of 2-chlorobenzoate by Pseudomonas cepacia 2CBS. Biol. Chem. Hoppe-Seyler 370 (1989) 1173-1182. [PMID: 2610934]
2. Fetzner, S., Muller, R. and Lingens, F. Purification and some properties of 2-halobenzoate 1,2-dioxygenase, a two-component enzyme system from Pseudomonas cepacia 2CBS. J. Bacteriol. 174 (1992) 279-290. [PMID: 1370284]
3. Haak, B., Fetzner, S. and Lingens, F. Cloning, nucleotide sequence, and expression of the plasmid-encoded genes for the two-component 2-halobenzoate 1,2-dioxygenase from Pseudomonas cepacia 2CBS. J. Bacteriol. 177 (1995) 667-675. [PMID: 7530709]
Accepted name: 2-aminobenzenesulfonate 2,3-dioxygenase
Reaction: 2-aminobenzenesulfonate + NADH + H+ + O2 = 2,3-dihydroxybenzenesulfonate + NH3 + NAD+
For diagram click here.
Other name(s): 2-aminosulfobenzene 2,3-dioxygenase
Systematic name: 2-aminobenzenesulfonate,NADH:oxygen oxidoreductase (2,3-hydroxylating, ammonia-forming)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 156621-16-8
References:
1. Junker, F., Field, J.A., Bangerter, F., Ramsteiner, K., Kohler, H.-P., Joannou, C.L., Mason, J.R., Leisinger, T. and Cook, A.M. Dioxygenation and spontaneous deamination of 2-aminobenzene sulphonic acid in Alcaligenes sp. strain O-1 with subsequent meta ring cleavage and spontaneous desulphonation to 2-hydroxymuconic acid. Biochem. J. 300 (1994) 429-436. [PMID: 8002948]
2. Junker, F., Leisinger, T. and Cook, A.M. 3-Sulphocatechol dioxygenase and other dioxygenases (1.13.11.2 and 1.14.12.-) in the degradative pathways of 2-aminobenzenesulphonic, benzenesulphonic and 4-toluenesulphonic acids in Alcaligenes sp. strain O-1. J. Gen. Microbiol. 140 (1994) 1713-1722. [PMID: 8075807]
Accepted name: terephthalate 1,2-dioxygenase
Reaction: terephthalate + NADH + H+ + O2 = (1R,6S)-dihydroxycyclohexa-2,4-diene-1,4-dicarboxylate + NAD+
For diagram click here.
Other name(s): benzene-1,4-dicarboxylate 1,2-dioxygenase; 1,4-dicarboxybenzoate 1,2-dioxygenase
Systematic name: benzene-1,4-dicarboxylate,NADH:oxygen oxidoreductase (1,2-hydroxylating)
Comments: has been shown to contain a Rieske [2Fe-2S] cluster
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 162032-76-0
References:
1. Schläfli, H.R., Weiss, M.A., Leisinger, T. and Cook, A.M. Terephthalate 1,2-dioxygenase system from Comamonas testosteroni T-2; purification and some properties of the oxygenase component. J. Bacteriol. 176 (1994) 6644-6652. [PMID: 7961417]
Accepted name: 2-hydroxyquinoline 5,6-dioxygenase
Reaction: quinolin-2-ol + NADH + H+ + O2 = 2,5,6-trihydroxy-5,6-dihydroquinoline + NAD+
For diagram click here.
Other name(s): 2-oxo-1,2-dihydroquinoline 5,6-dioxygenase; quinolin-2-ol 5,6-dioxygenase; quinolin-2(1H)-one 5,6-dioxygenase
Systematic name: quinolin-2-ol,NADH:oxygen oxidoreductase (5,6-hydroxylating)
Comments: 3-Methylquinolin-2-ol, quinolin-8-ol and quinolin-2,8-diol are also substrates. Quinolin-2-ols exist largely as their quinolin-2(1H)-one tautomers
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 172399-50-7
References:
1. Schach, S.B., Tshisuaka, B., Fetzner, S. and Lingens, F. Quinoline 2-oxidoreductase and 2-oxo-1,2-dihydroquinoline 5,6-dioxygenase from Comamonas testosteroni 63. The first two enzymes in quinoline and 3-methylquinoline degradation. Eur. J. Biochem. 232 (1995) 536-544. [PMID: 7556204]
Accepted name: nitric oxide dioxygenase
Reaction: 2 nitric oxide + 2 O2 + NAD(P)H = 2 nitrate + NAD(P)+ + H+
Glossary: nitric oxide = NO
Systematic name: nitric oxide,NAD(P)H:oxygen oxidoreductase
Comments: A flavohemoglobin (FAD). It has been proposed that FAD functions as the electron carrier from NADPH to the ferric heme prosthetic group.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 214466-78-1
References:
1. Gardner, P.R., Costantino, G. and Salzman, A.L. Constitutive and adaptive detoxification of nitric oxide in Escherichia coli. Role of nitric-oxide dioxygenase in the protection of aconitase. J. Biol. Chem. 273 (1998) 26528-26533. [PMID: 9756889]
2. Gardner, P.R., Gardner, A.M., Martin, L.A. and Salzman, A.L. Nitric oxide dioxygenase: an enzymic function for flavohemoglobin. Proc. Natl. Acad. Sci. USA 95 (1998) 10378-10383. [PMID: 9724711]
Accepted name: biphenyl 2,3-dioxygenase
Reaction: biphenyl + NADH + H+ + O2 = (1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
For reaction pathway click here.
Other name(s): biphenyl dioxygenase
Systematic name: biphenyl,NADH:oxygen oxidoreductase (2,3-hydroxylating)
Comments: Requires Fe2+. The enzyme from Burkholderia fungorum LB400 (previously Pseudomonas sp.) is part of a multicomponent system composed of an NADH:ferredoxin oxidoreductase (FAD cofactor), a [2Fe-2S] Rieske-type ferredoxin, and a terminal oxygenase that contains a [2Fe-2S] Rieske-type iron-sulfur cluster and a catalytic mononuclear nonheme iron centre. Chlorine-substituted biphenyls can also act as substrates. Similar to the three-component enzyme systems EC 1.14.12.3 (benzene 1,2-dioxygenase) and EC 1.14.12.11 (toluene dioxygenase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 103289-55-0
References:
1. Haddock, J.D. and Gibson, D.T. Purification and characterization of the oxygenase component of biphenyl 2,3-dioxygenase from Pseudomonas sp. strain LB400. J. Bacteriol. 177 (1995) 5834-5839. [PMID: 7592331]
2. Haddock, J.D., Pelletier, D.A. and Gibson, D.T. Purification and properties of ferredoxinBPH, a component of biphenyl 2,3-dioxygenase of Pseudomonas sp. strain LB400. J. Indust. Microbiol. Biotechnol. 19 (1997) 355-359. [PMID: 9451832]
3. Broadus, R.M. and Haddock, J.D. Purification and characterization of the NADH:ferredoxinBPH oxidoreductase component of biphenyl 2,3-dioxygenase from Pseudomonas sp. strain LB400. Arch. Microbiol. 170 (1998) 106-112. [PMID: 9683647]
Accepted name: 3-phenylpropanoate dioxygenase
Reaction: (1) 3-phenylpropanoate + NADH + H+ + O2 = 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate + NAD+
(2) (2E)-3-phenylprop-2-enoate + NADH + H+ + O2 = (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + NAD+
For diagram of reaction, click here or click here
Glossary: (2E)-3-phenylprop-2-enoate = trans-cinnamate
(2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate = trans-2,3-dihydroxycinnamate
Other name(s): HcaA1A2CD; Hca dioxygenase; 3-phenylpropionate dioxygenase
Systematic name: 3-phenylpropanoate,NADH:oxygen oxidoreductase (2,3-hydroxylating)
Comments: This enzyme catalyses a step in the pathway of phenylpropanoid compounds degradation. It catalyses the insertion of both atoms of molecular oxygen into positions 2 and 3 of the phenyl ring of 3-phenylpropanoate or (2E)-3-phenylprop-2-enoate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number:
References:
1. Díaz, E., Ferrández, A. and García, J.L. Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12. J. Bacteriol. 180 (1998) 2915-2923. [PMID: 9603882]
2. Burlingame, R. and Chapman, P.J. Catabolism of phenylpropionic acid and its 3-hydroxy derivative by Escherichia coli. J. Bacteriol. 155 (1983) 113-121. [PMID: 6345502]
Accepted name: pheophorbide a oxygenase
Reaction: pheophorbide a + NADPH + H+ + O2 = red chlorophyll catabolite + NADP+
For diagram click here and for mechanism click here.
Glossary: red chlorophyll catabolite = RCC = (7S,8S,101R)-8-(2-carboxyethyl)-17-ethyl-19-formyl-101-(methoxycarbonyl)-3,7,13,18-tetramethyl-2-vinyl-8,23-dihydro-7H-10,12-ethanobiladiene-ab-1,102(21H)-dione
Other name(s): pheide a monooxygenase; pheide a oxygenase; PaO; PAO
Systematic name: pheophorbide-a,NADPH:oxygen oxidoreductase (biladiene-forming)
Comments: This enzyme catalyses a key reaction in chlorophyll degradation, which occurs during leaf senescence and fruit ripening in higher plants. The enzyme from Arabidopsis contains a Rieske-type iron-sulfur cluster [2] and requires reduced ferredoxin, which is generated either by NADPH through the pentose-phosphate pathway or by the action of photosystem I [4]. While still attached to this enzyme, the product is rapidly converted into primary fluorescent chlorophyll catabolite by the action of EC 1.3.1.80, red chlorophyll catabolite reductase [2,6]. Pheophorbide b acts as an inhibitor. In 18O2 labelling experiments, only the aldehyde oxygen is labelled, suggesting that the other oxygen atom may originate from H2O [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Hörtensteiner, S., Wüthrich, K.L., Matile, P., Ongania, K.H. and Kräutler, B. The key step in chlorophyll breakdown in higher plants. Cleavage of pheophorbide a macrocycle by a monooxygenase. J. Biol. Chem. 273 (1998) 15335-15339. [PMID: 9624113]
2. Pružinská, A., Tanner, G., Anders, I., Roca, M. and Hörtensteiner, S. Chlorophyll breakdown: pheophorbide a oxygenase is a Rieske-type iron-sulfur protein, encoded by the accelerated cell death 1 gene. Proc. Natl. Acad. Sci. USA 100 (2003) 15259-15264. [PMID: 14657372]
3. Chung, D.W., Pružinská, A., Hörtensteiner, S. and Ort, D.R. The role of pheophorbide a oxygenase expression and activity in the canola green seed problem. Plant Physiol. 142 (2006) 88-97. [PMID: 16844830]
4. Rodoni, S., Mühlecker, W., Anderl, M., Kräutler, B., Moser, D., Thomas, H., Matile, P. and Hörtensteiner, S. Chlorophyll breakdown in senescent chloroplasts. Cleavage of pheophorbide a in two enzymic steps. Plant Physiol. 115 (1997) 669-676. [PMID: 12223835]
5. Hörtensteiner, S. Chlorophyll degradation during senescence. Annu. Rev. Plant Biol. 57 (2006) 55-77. [PMID: 16669755]
6. Pružinská, A., Anders, I., Aubry, S., Schenk, N., Tapernoux-Lüthi, E., Müller, T., Kräutler, B. and Hörtensteiner, S. In vivo participation of red chlorophyll catabolite reductase in chlorophyll breakdown. Plant Cell 19 (2007) 369-387. [PMID: 17237353]
Note: For reference 2 and 3 an accent may not be seen. ž is z-hacek
Accepted name: benzoyl-CoA 2,3-dioxygenase
Reaction: benzoyl-CoA + NADPH + H+ + O2 = 2,3-dihydro-2,3-dihydroxybenzoyl-CoA + NADP+
Other name(s): benzoyl-CoA dioxygenase/reductase; BoxBA; BoxA/BoxB system
Systematic name: benzoyl-CoA,NADPH:oxygen oxidoreductase (2,3-hydroxylating)
Comments: The enzyme is involved in aerobic benzoate metabolism in Azoarcus evansii. BoxB functions as the oxygenase part of benzoyl-CoA oxygenase in conjunction with BoxA, the reductase component, which upon binding of benzoyl-CoA, transfers two electrons to the ring in the course of dioxygenation. BoxA is a homodimeric 46 kDa iron-sulfur-flavoprotein (FAD), BoxB is a monomeric iron-protein [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Zaar, A., Gescher, J., Eisenreich, W., Bacher, A. and Fuchs, G. New enzymes involved in aerobic benzoate metabolism in Azoarcus evansii. Mol. Microbiol. 54 (2004) 223-238. [PMID: 15458418]
2. Gescher, J., Zaar, A., Mohamed, M., Schagger, H. and Fuchs, G. Genes coding for a new pathway of aerobic benzoate metabolism in Azoarcus evansii. J. Bacteriol. 184 (2002) 6301-6315. [PMID: 12399500]
3. Mohamed, M.E., Zaar, A., Ebenau-Jehle, C. and Fuchs, G. Reinvestigation of a new type of aerobic benzoate metabolism in the proteobacterium Azoarcus evansii. J. Bacteriol. 183 (2001) 1899-1908. [PMID: 11222587]
Accepted name: carbazole 1,9a-dioxygenase
Reaction: 9H-carbazole + NAD(P)H + H+ + O2 = 2'-aminobiphenyl-2,3-diol + NAD(P)+
Other name(s): CARDO
Systematic name: 9H-carbazole,NAD(P)H:oxygen oxidoreductase (2,3-hydroxylating)
Comments: This enzyme catalyses the first reaction in the pathway of carbazole degradation. The enzyme attacks at the 1 and 9a positions of carbazle, resulting in the formation of a highly unstable hemiaminal intermediate that undergoes a spontaneous cleavage and rearomatization, resulting in 2'-aminobiphenyl-2,3-diol. In most bacteria the enzyme is a complex composed of a terminal oxygenase, a ferredoxin, and a ferredoxin reductase. The terminal oxygenase component contains a nonheme iron centre and a Rieske [2Fe-2S] iron-sulfur cluster.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number:
References:
1. Nam, J.W., Nojiri, H., Noguchi, H., Uchimura, H., Yoshida, T., Habe, H., Yamane, H. and Omori, T. Purification and characterization of carbazole 1,9a-dioxygenase, a three-component dioxygenase system of Pseudomonas resinovorans strain CA10. Appl. Environ. Microbiol. 68 (2002) 5882-5890. [PMID: 12450807]
2. Gai, Z., Wang, X., Liu, X., Tai, C., Tang, H., He, X., Wu, G., Deng, Z. and Xu, P. The genes coding for the conversion of carbazole to catechol are flanked by IS6100 elements in Sphingomonas sp. strain XLDN2-5. PLoS One 5 (2010) e10018. [PMID: 20368802]