Continued from EC 1.14.13.151 to EC 1.14.13.171
EC 1.14 Acting on paired donors with incorporation of molecular oxygen [continued]
EC 1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
EC 1.14.15 With a 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 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 1.14.19 With oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
EC 1.14.20 With 2-oxoglutarate as one donor, and the other dehydrogenated
EC 1.14.21 With NADH or NADPH as one donor, and the other dehydrogenated
Accepted name: unspecific monooxygenase
Reaction: RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
Other name(s): microsomal monooxygenase; xenobiotic monooxygenase; aryl-4-monooxygenase; aryl hydrocarbon hydroxylase; microsomal P-450; flavoprotein-linked monooxygenase; flavoprotein monooxygenase
Systematic name: substrate,reduced-flavoprotein:oxygen oxidoreductase (RH-hydroxylating or -epoxidizing)
Comments: A group of heme-thiolate proteins (P-450), acting on a wide range of substrates including many xenobiotics, steroids, fatty acids, vitamins and prostaglandins; reactions catalysed include hydroxylation, epoxidation, N-oxidation, sulfooxidation, N-, S- and O-dealkylations, desulfation, deamination, and reduction of azo, nitro and N-oxide groups. Together with EC 1.6.2.4 NADPH—hemoprotein reductase, it forms a system in which two reducing equivalents are supplied by NADPH. Formerly EC 1.14.1.1, EC 1.14.99.8 and EC 1.99.1.1. Some of the reactions attributed to EC 1.14.15.3 (alkane 1-monooxygenase) belong here.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9038-14-6
References:
1. Booth, J. and Boyland, E. The biochemistry of aromatic amines. 3. Enzymic hydroxylation by rat-liver microsomes. Biochem. J. 66 (1957) 73-78.
2. Fujita, T. and Mannering, G.J. Differences in soluble P-450 hemoproteins from livers of rats treated with phenobarbital and 3-methylcholanthrene. Chem.-Biol. Interact. 3 (1971) 264-265. [PMID: 5132997]
3. Haugen, D.A. and Coon, M.J. Properties of electrophoretically homogeneous phenobarbital-inducible and β-naphthoflavone-inducible forms of liver microsomal cytochrome P-450. J. Biol. Chem. 251 (1976) 7929-7939. [PMID: 187601]
4. Imaoka, S., Inoue, K. and Funae, Y. Aminopyrine metabolism by multiple forms of cytochrome P-450 from rat liver microsomes: simultaneous quantitation of four aminopyrine metabolites by high-performance liquid chromatography. Arch. Biochem. Biophys. 265 (1988) 159-170. [PMID: 3415241]
5.Johnson, E.F., Zounes, M. and Müller-Eberhard, U. Characterization of three forms of rabbit microsomal cytochrome P-450 by peptide mapping utilizing limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. Arch. Biochem. Biophys. 192 (1979) 282-289. [PMID: 434823]
6.Kupfer, D., Miranda, G.K., Navarro, J., Piccolo, D.E. and Theoharides, A.D. Effect of inducers and inhibitors of monooxygenase on the hydroxylation of prostaglandins in the guinea pig. Evidence for several monooxygenases catalyzing ω- and ω-1-hydroxylation. J. Biol. Chem. 254 (1979) 10405-10414. [PMID: 489601]
7. Lang, M.A., Gielen, J.E. and Nebert, D.W. Genetic evidence for many unique liver microsomal P-450-mediated monooxygenase activities in heterogeneic stock mice. J. Biol. Chem. 256 (1981) 12068-12075. [PMID: 7298645]
8. Lang, M.A. and Nebert, D.W. Structural gene products of the Ah locus. Evidence for many unique P-450-mediated monooxygenase activities reconstituted from 3-methylcholanthrene-treated C57BL/6N mouse liver microsomes. J. Biol. Chem. 256 (1981) 12058-12075. [PMID: ]
9. Leo, M.A., Lasker, J.M., Rauby, J.L., Kim, C.I., Black, M. and Lieber, C.S. Metabolism of retinol and retinoic acid by human liver cytochrome P450IIC8. Arch. Biochem. Biophys. 269 (1989) 305-312. [PMID: 2916844]
10. Lu, A.Y.H., Kuntzman, S.W., Jacobson, M. and Conney, A.H. Reconstituted liver microsomal enzyme system that hydroxylates drugs, other foreign compounds, and endogenous substrates. II. Role of the cytochrome P-450 and P-448 fractions in drug and steroid hydroxylations. J. Biol. Chem. 247 (1972) 1727-1734. [PMID: 4401153]
11. Mitoma, C., Posner, H.S., Reitz, H.C. and Udenfriend, S. Enzymic hydroxylation of aromatic compounds. Arch. Biochem. Biophys. 61 (1956) 431-441.
12. Mitoma, C. and Udenfriend, S. Aryl-4-hydroxylase. Methods Enzymol. 5 (1962) 816-819.
13. Napoli, J.L., Okita, R.T., Masters, B.S. and Horst, R.L. Identification of 25,26-dihydroxyvitamin D3 as a rat renal 25-hydroxyvitamin D3 metabolite. Biochemistry 20 (1981) 5865-5871. [PMID: 7295706]
14. Nebert, D.W. and Gelboin, H.V. Substrate-inducible microsomal aryl hydroxylase in mammalian cell culture. I. Assay and properties of induced enzyme. J. Biol. Chem. 243 (1968) 6242-6249. [PMID: 4387094]
15.Suhara, K., Ohashi, K., Takahashi, K. and Katagiri, M. Aromatase and nonaromatizing 10-demethylase activity of adrenal cortex mitochondrial P-450(11)β. Arch. Biochem. Biophys. 267 (1988) 31-37. [PMID: 3264134]
16.Theoharides, A.D. and Kupfer, D. Evidence for different hepatic microsomal monooxygenases catalyzing ω- and (ω-1)-hydroxylations of prostaglandins E1 and E2. Effects of inducers of monooxygenase on the kinetic constants of prostaglandin hydroxylation. J. Biol. Chem. 256 (1981) 2168-2175. [PMID: 7462235]
17. Thomas, P.E., Lu, A.Y.H., Ryan, D., West, S.B., Kawalek, J. and Levin, W. Immunochemical evidence for six forms of rat liver cytochrome P450 obtained using antibodies against purified rat liver cytochromes P450 and P448. Mol. Pharmacol. 12 (1976) 746-758. [PMID: 825720]
[EC 1.14.14.2 Deleted entry: benzopyrene 3-monooxygenase. Now included with EC 1.14.14.1 unspecific monooxygenase (EC 1.14.14.2 created 1972, deleted 1976)]
Accepted name: alkanal monooxygenase (FMN)
Reaction: an aldehyde + FMNH2 + O2 = a carboxylate + FMN + H2O + hν
Glossary: an aldehyde = R-CHO
a carboxylate = R-COO–
Other name(s): bacterial luciferase; aldehyde monooxygenase; luciferase; Vibrio fischeri luciferase; alkanal,reduced-FMN:oxygen oxidoreductase (1-hydroxylating, luminescing); alkanal,FMNH2:oxygen oxidoreductase (1-hydroxylating, luminescing)
Systematic name: alkanal,FMNH2:oxygen oxidoreductase (1-hydroxylating, luminescing)
Comments: The reaction sequence involves incorporation of a molecule of oxygen into reduced FMN, and subsequent reaction with the aldehyde to form an activated FMN.H2O complex, which breaks down with emission of light. The enzyme is highly specific for reduced FMN, and for long-chain aliphatic aldehydes with eight carbons or more.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9014-00-0
References:
1. Hastings, J.W. Bacterial bioluminescence light emission in the mixed function oxidation of reduced flavin and fatty aldehyde. Crit. Rev. Biochem. 5 (1978) 163-184. [PMID: 363350]
2. Hastings, J.W. and Nealson, K.H. Bacterial bioluminescence. Annu. Rev. Microbiol. 31 (1977) 549-595. [PMID: 199107]
3. Hastings, J.W. and Presswood, R.P. Bacterial luciferase: FMNH2-aldehyde oxidase. Methods Enzymol. 53 (1978) 558-570. [PMID: 309549]
4. Nealson, K.H. and Hastings, J.W. Bacterial bioluminescence: its control and ecological significance. Microbiol. Rev. 43 (1979) 496-518. [PMID: 396467]
5. Suzuki, K., Kaidoh, T., Katagiri, M. and Tsuchiya, T. O2 incorporation into a long-chain fatty-acid during bacterial luminescence. Biochim. Biophys. Acta 722 (1983) 297-301.
[EC 1.14.14.4 Deleted entry: choline monooxygenase. Identical to EC 1.14.15.7 (EC 1.14.14.4 created 2000, deleted 2002)]
Accepted name: alkanesulfonate monooxygenase
Reaction: an alkanesulfonate + FMNH2 + O2 = an aldehyde + FMN + sulfite + H2O
Glossary: an alkanesulfonate = R-CH2-SO3-
an aldehyde = R-CHO
Other name(s): SsuD; sulfate starvation-induced protein 6; alkanesulfonate,reduced-FMN:oxygen oxidoreductase
Systematic name: alkanesulfonate,FMNH2:oxygen oxidoreductase
Comments: The enzyme from Escherichia coli catalyses the desulfonation of a wide range of aliphatic sulfonates (unsubstituted C1- to C14-sulfonates as well as substituted C2-sulfonates). Does not desulfonate taurine (2-aminoethanesulfonate) or aromatic sulfonates. Does not use FMN as a bound cofactor. Instead, it uses reduced FMN (i.e., FMNH2) as a substrate. FMNH2 is provided by SsuE, the associated FMN reductase (EC 1.5.1.29).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 256383-67-2
References:
1. Eichhorn, E., van der Ploeg, J.R. and Leisinger, T. Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli. J. Biol. Chem. 274 (1999) 26639-26646. [PMID: 10480865]
[EC 1.14.14.6 Transferred entry: methanesulfonate monooxygenase. Now EC 1.14.13.111, methanesulfonate monooxygenase. Formerly thought to involve FMNH2 but now shown to use NADH. (EC 1.14.14.6 created 2009, deleted 2010)]
Accepted name: tryptophan 7-halogenase
Reaction: tryptophan + FADH2 + Cl- + O2 + H+ = 7-chloro-L-tryptophan + FAD + 2 H2O
Other name(s): PrnA; RebH
Systematic name: L-tryptophan:FADH2 oxidoreductase (7-halogenating)
Comments: In Lechevalieria aerocolonigenes the enzyme catalyses the initial step in the biosynthesis of rebeccamycin [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Dong, C., Kotzsch, A., Dorward, M., van Pee, K.H. and Naismith, J.H. Crystallization and X-ray diffraction of a halogenating enzyme, tryptophan 7-halogenase, from Pseudomonas fluorescens. Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 1438-1440. [PMID: 15272170]
2. Yeh, E., Garneau, S. and Walsh, C.T. Robust in vitro activity of RebF and RebH, a two-component reductase/halogenase, generating 7-chlorotryptophan during rebeccamycin biosynthesis. Proc. Natl. Acad. Sci. USA 102 (2005) 3960-3965. [PMID: 15743914]
3. Bitto, E., Huang, Y., Bingman, C.A., Singh, S., Thorson, J.S. and Phillips Jr., G.N. The structure of flavin-dependent tryptophan 7-halogenase RebH. Proteins Struct. Funct. Genet. 70 (2008) 289-293.
Accepted name: anthranilate 3-monooxygenase (FAD)
Reaction: anthranilate + FADH2 + O2 = 3-hydroxyanthranilate + FAD + H2O
Glossary: anthranilate = 2-aminobenzoate
Other name(s): anthranilate 3-hydroxylase; anthranilate hydroxylase
Systematic name: anthranilate,FAD:oxygen oxidoreductase (3-hydroxylating)
Comments: This enzyme, isolated from the bacterium Geobacillus thermodenitrificans, participates in the pathway of tryptophan degradation. The enzyme is part of a system that also includes a bifunctional riboflavin kinase/FMN adenylyltransferase and an FAD reductase, which ensures ample supply of FAD to the monooxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Liu, X., Dong, Y., Li, X., Ren, Y., Li, Y., Wang, W., Wang, L. and Feng, L. Characterization of the anthranilate degradation pathway in Geobacillus thermodenitrificans NG80-2. Microbiology 156 (2010) 589-595. [PMID: 19942660]
Accepted name: 4-hydroxyphenylacetate 3-monooxygenase
Reaction: 4-hydroxyphenylacetate + FADH2 + O2 = 3,4-dihydroxyphenylacetate + FAD + H2O
Other name(s): p-hydroxyphenylacetate 3-hydroxylase; 4-hydroxyphenylacetic acid-3-hydroxylase; p-hydroxyphenylacetate hydroxylase (FAD); 4 HPA 3-hydroxylase; p-hydroxyphenylacetate 3-hydroxylase (FAD); HpaB
Systematic name: 4-hydroxyphenylacetate,FAD:oxygen oxidoreductase (3-hydroxylating)
Comments: The enzyme from Escherichia coli attacks a broad spectrum of phenolic compounds. The enzyme uses FADH2 as a substrate rather than a cofactor [4]. FADH2 is provided by EC 1.5.1.36, flavin reductase (NADH) [5,6].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number:
References:
1. Adachi, K., Takeda, Y., Senoh, S. and Kita, H. Metabolism of p-hydroxyphenylacetic acid in Pseudomonas ovalis. Biochim. Biophys. Acta 93 (1964) 483-493. [PMID: 14263147]
2. Prieto, M.A., Perez-Aranda, A. and Garcia, J.L. Characterization of an Escherichia coli aromatic hydroxylase with a broad substrate range. J. Bacteriol. 175 (1993) 2162-2167. [PMID: 8458860]
3. Prieto, M.A. and Garcia, J.L. Molecular characterization of 4-hydroxyphenylacetate 3-hydroxylase of Escherichia coli. A two-protein component enzyme. J. Biol. Chem. 269 (1994) 22823-22829. [PMID: 8077235]
4. Xun, L. and Sandvik, E.R. Characterization of 4-hydroxyphenylacetate 3-hydroxylase (HpaB) of Escherichia coli as a reduced flavin adenine dinucleotide-utilizing monooxygenase. Appl. Environ. Microbiol. 66 (2000) 481-486. [PMID: 10653707]
5. Galan, B., Diaz, E., Prieto, M.A. and Garcia, J.L. Functional analysis of the small component of the 4-hydroxyphenylacetate 3-monooxygenase of Escherichia coli W: a prototype of a new Flavin:NAD(P)H reductase subfamily. J. Bacteriol. 182 (2000) 627-636. [PMID: 10633095]
6. Louie, T.M., Xie, X.S. and Xun, L. Coordinated production and utilization of FADH2 by NAD(P)H-flavin oxidoreductase and 4-hydroxyphenylacetate 3-monooxygenase. Biochemistry 42 (2003) 7509-7517. [PMID: 12809507]
Accepted name: nitrilotriacetate monooxygenase
Reaction: nitrilotriacetate + FMNH2 + H+ + O2 = iminodiacetate + glyoxylate + FMN + H2O
Systematic name: nitrilotriacetate,FMNH2:oxygen oxidoreductase (glyoxylate-forming)
Comments: Requires Mg2+. The enzyme from Aminobacter aminovorans (previously Chelatobacter heintzii) is part of a two component system that also includes EC 1.5.1.42 (FMN reductase), which provides reduced flavin mononucleotide for this enzyme.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number:
References:
1. Uetz, T., Schneider, R., Snozzi, M. and Egli, T. Purification and characterization of a two-component monooxygenase that hydroxylates nitrilotriacetate from "Chelatobacter" strain ATCC 29600. J. Bacteriol. 174 (1992) 1179-1188. [PMID: 1735711]
2. Knobel, H.R., Egli, T. and van der Meer, J.R. Cloning and characterization of the genes encoding nitrilotriacetate monooxygenase of Chelatobacter heintzii ATCC 29600. J. Bacteriol. 178 (1996) 6123-6132. [PMID: 8892809]
3. Xu, Y., Mortimer, M.W., Fisher, T.S., Kahn, M.L., Brockman, F.J. and Xun, L. Cloning, sequencing, and analysis of a gene cluster from Chelatobacter heintzii ATCC 29600 encoding nitrilotriacetate monooxygenase and NADH:flavin mononucleotide oxidoreductase. J. Bacteriol. 179 (1997) 1112-1116. [PMID: 9023192]
Accepted name: styrene monooxygenase
Reaction: styrene + FADH2 + O2 = (S)-2-phenyloxirane + FAD + H2O
Other name(s): StyA; SMO; NSMOA
Systematic name: styrene,FADH2:oxygen oxidoreductase
Comments: The enzyme catalyses the first step in the aerobic styrene degradation pathway. It forms a two-component system with a reductase (StyB) that utilizes NADH to reduce flavin-adenine dinucleotide, which is then transferred to the oxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Otto, K., Hofstetter, K., Rothlisberger, M., Witholt, B. and Schmid, A. Biochemical characterization of StyAB from Pseudomonas sp. strain VLB120 as a two-component flavin-diffusible monooxygenase. J. Bacteriol. 186 (2004) 5292-5302. [PMID: 15292130]
2. Tischler, D., Kermer, R., Groning, J.A., Kaschabek, S.R., van Berkel, W.J. and Schlomann, M. StyA1 and StyA2B from Rhodococcus opacus 1CP: a multifunctional styrene monooxygenase system. J. Bacteriol. 192 (2010) 5220-5227. [PMID: 20675468]
Accepted name: 3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione monooxygenase
Reaction: 3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione + FMNH2 + O2 = 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione + FMN + H2O
Other name(s): HsaA
Systematic name: 3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione,FMNH2:oxygen oxidoreductase
Comments: This bacterial enzyme participates in the degradation of several steroids, including cholesterol and testosterone. It can use either FADH or FMNH2 as flavin cofactor. The enzyme forms a two-component system with a reductase (HsaB) that utilizes NADH to reduce the flavin, which is then transferred to the oxygenase subunit.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number:
References:
1. Dresen, C., Lin, L.Y., D'Angelo, I., Tocheva, E.I., Strynadka, N. and Eltis, L.D. A flavin-dependent monooxygenase from Mycobacterium tuberculosis involved in cholesterol catabolism. J. Biol. Chem. 285 (2010) 22264-22275. [PMID: 20448045]
Accepted name: 4-(L-γ-glutamylamino)butanoyl-[BtrI acyl-carrier protein] monooxygenase
Reaction: 4-(L-γ-glutamylamino)butanoyl-[BtrI acyl-carrier protein] + FMNH2 + O2 = 4-(L-γ-glutamylamino)-(2S)-2-hydroxybutanoyl-[BtrI acyl-carrier protein] + FMN + H2O
Other name(s): btrO (gene name); 4-(L-γ-glutamylamino)butanoyl-[BtrI acyl-carrier protein],FMNH:oxygen oxidoreductase (2-hydroxylating)
Systematic name: 4-(L-γ-glutamylamino)butanoyl-[BtrI acyl-carrier protein],FMNH2:oxygen oxidoreductase (2-hydroxylating)
Comments: Catalyses a step in the biosynthesis of the side chain of the aminoglycoside antibiotics of the butirosin family. FMNH2 is used as a free cofactor. Forms a complex with a dedicated NAD(P)H:FMN oxidoreductase. The enzyme is not able to hydroxylate free substrates, activation by the acyl-carrier protein is mandatory. Octanoyl-S-[BtrI acyl-carrier protein] is also accepted.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Li, Y., Llewellyn, N.M., Giri, R., Huang, F. and Spencer, J.B. Biosynthesis of the unique amino acid side chain of butirosin: possible protective-group chemistry in an acyl carrier protein-mediated pathway. Chem. Biol. 12 (2005) 665-675. [PMID: 15975512]
Accepted name: camphor 5-monooxygenase
Reaction: (+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
For diagram of reaction click here.
Other name(s): camphor 5-exo-methylene hydroxylase; 2-bornanone 5-exo-hydroxylase; bornanone 5-exo-hydroxylase; camphor 5-exo-hydroxylase; camphor 5-exohydroxylase; camphor hydroxylase; d-camphor monooxygenase; methylene hydroxylase; methylene monooxygenase; D-camphor-exo-hydroxylase; camphor methylene hydroxylase
Systematic name: (+)-camphor,reduced putidaredoxin:oxygen oxidoreductase (5-hydroxylating)
Comments: A heme-thiolate protein (P-450). Also acts on (–)-camphor and 1,2-campholide, forming 5-exo-hydroxy-1,2-campholide.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9030-82-4
References:
1. Hedegaard, J. and Gunsalus, I.C. Mixed function oxidation. IV. An induced methylene hydroxylase in camphor oxidation. J. Biol. Chem. 240 (1965) 4038-4043. [PMID: 4378858]
2. Tyson, C.A., Lipscomb, J.D. and Gunsalus, I.C. The role of putidaredoxin and P450cam in methylene hydroxylation. J. Biol. Chem. 247 (1972) 5777-5784. [PMID: 4341491]
[EC 1.14.15.2 Transferred entry: camphor 1,2-monooxygenase. Now EC 1.14.13.162, 2,5-diketocamphane 1,2-monooxygenase. (EC 1.14.15.2 created 1972, deleted 2012)]
Accepted name: alkane 1-monooxygenase
Reaction: octane + reduced rubredoxin + O2 = 1-octanol + oxidized rubredoxin + H2O
Other name(s): alkane 1-hydroxylase; ω-hydroxylase; fatty acid ω-hydroxylase; alkane monooxygenase; 1-hydroxylase; alkane hydroxylase
Systematic name: alkane,reduced-rubredoxin:oxygen 1-oxidoreductase
Comments: Some enzymes in this group are heme-thiolate proteins (P-450). Also hydroxylates fatty acids in the ω-position.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9059-16-9
References:
1. Cardini, G. and Jurtshuk, P. The enzymatic hydroxylation of n-octane by Corynebacterium sp. strain 7E1C. J. Biol. Chem. 245 (1970) 2789-2796. [PMID: 4317878]
2. McKenna, E.J. and Coon, M.J. Enzymatic ω-oxidation. IV. Purification and properties of the ω-hydroxylase of Pseudomonas oleovorans. J. Biol. Chem. 245 (1970) 3882-3889. [PMID: 4395379]
3. Peterson, J.A., Kusunose, M., Kusunose, E. and Coon, M.J. Enzymatic ω-oxidation. II. Function of rubredoxin as the electron carrier in ω-hydroxylation. J. Biol. Chem. 242 (1967) 4334-4340. [PMID: 4294330]
Accepted name: steroid 11β-monooxygenase
Reaction: a steroid + reduced adrenodoxin + O2 = an 11β-hydroxysteroid + oxidized adrenodoxin + H2O
Other name(s): steroid 11β-hydroxylase; steroid 11β/18-hydroxylase
Systematic name: steroid,reduced-adrenal-ferredoxin:oxygen oxidoreductase (11β-hydroxylating)
Comments: A heme-thiolate protein (P-450). Also hydroxylates steroids at the 18-position, and converts 18-hydroxycorticosterone into aldosterone. Formerly EC 1.14.1.6 and EC 1.99.1.7.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9029-66-7
References:
1. Grant, J.K. and Brownie, A.C. The role of fumarate and TPN in steroid enzymic 11β-hydroxylation. Biochim. Biophys. Acta 18 (1955) 433-434.
2. Hayano, M. and Dorfman, R.I. On the mechanism of the C-11β-hydroxylation of steroids. J. Biol. Chem. 211 (1954) 227-235.
3. Tomkins, G.M., Michael, P.J. and Curran, J.F. Studies on the nature of steroid 11-β hydroxylation. Biochim. Biophys. Acta 23 (1957) 655-656.
4. Yanagibashi, K., Haniu, M., Shively, J.E., Shen, W.H. and Hall, P. The synthesis of aldosterone by the adrenal cortex. Two zones (fasciculata and glomerulosa) possess one enzyme for 11β-, 18-hydroxylation, and aldehyde synthesis. J. Biol. Chem. 261 (1986) 3556-3562. [PMID: 3485096]
5. Zuidweg, M.H.J. Hydroxylation of Reichstein's compound S with cell-free preparations from Curvularia lunata. Biochim. Biophys. Acta 152 (1968) 144-158. [PMID: 4967077]
Accepted name: corticosterone 18-monooxygenase
Reaction: corticosterone + reduced adrenodoxin + O2 = 18-hydroxycorticosterone + oxidized adrenodoxin + H2O
Other name(s): corticosterone 18-hydroxylase; corticosterone methyl oxidase; corticosterone,reduced-adrenal-ferredoxin:oxygen oxidoreductase (18-hydroxylating
Systematic name: corticosterone,reduced-adrenodoxin:oxygen oxidoreductase (18-hydroxylating)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37256-75-0
References:
1. Raman, P.B., Sharma, D.C. and Dorfman, R.I. Studies on aldosterone biosynthesis in vitro. Biochemistry 5 (1966) 1795.
Accepted name: cholesterol monooxygenase (side-chain-cleaving)
Reaction: cholesterol + 6 reduced adrenodoxin + 3 O2 = pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 H2O (overall reaction)
(1a) cholesterol + 2 reduced adrenodoxin + O2 = (22R)-22-hydroxycholesterol + 2 oxidized adrenodoxin + H2O
(1b) (22R)-22-hydroxycholesterol + 2 reduced adrenodoxin + O2 = (20R,22R)-20,22-dihydroxycholesterol + 2 oxidized adrenodoxin + H2O
(1c) (20R,22R)-20,22-dihydroxy-cholesterol + 2 reduced adrenodoxin + O2 = pregnenolone + 4-methylpentanal + 2 oxidized adrenodoxin + 2 H2O
Other name(s): cholesterol desmolase; cytochrome P-450scc; C27-side chain cleavage enzyme; cholesterol 20-22-desmolase; cholesterol C20-22 desmolase; cholesterol side-chain cleavage enzyme; cholesterol side-chain-cleaving enzyme; steroid 20-22 desmolase; steroid 20-22-lyase; CYP11A1 (gene name); cholesterol,reduced-adrenal-ferredoxin:oxygen oxidoreductase (side-chain-cleaving)
Systematic name: cholesterol,reduced-adrenodoxin:oxygen oxidoreductase (side-chain-cleaving)
Comments: A heme-thiolate protein (cytochrome P-450). The reaction proceeds in three stages, with two hydroxylations at C-22 and C-20 preceding scission of the side-chain between carbons 20 and 22. The initial source of the electrons is NADPH, which transfers the electrons to the adrenodoxin via EC 1.18.1.6, adrenodoxin-NADP+ reductase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37292-81-2, 440354-98-3
References:
1. Burstein, S., Middleditch, B.S. and Gut, M. Mass spectrometric study of the enzymatic conversion of cholesterol to (22R)-22-hydroxycholesterol, (20R,22R)-20,22-dihydroxycholesterol, and pregnenolone, and of (22R)-22-hydroxycholesterol to the lgycol and pregnenolone in bovine adrenocortical preparations. Mode of oxygen incorporation. J. Biol. Chem. 250 (1975) 9028-9037. [PMID: 1238395]
2. Hanukoglu, I., Spitsberg, V., Bumpus, J.A., Dus, K.M. and Jefcoate, C.R. Adrenal mitochondrial cytochrome P-450scc. Cholesterol and adrenodoxin interactions at equilibrium and during turnover. J. Biol. Chem. 256 (1981) 4321-4328. [PMID: 7217084]
3. Hanukoglu, I. and Hanukoglu, Z. Stoichiometry of mitochondrial cytochromes P-450, adrenodoxin and adrenodoxin reductase in adrenal cortex and corpus luteum. Implications for membrane organization and gene regulation. Eur. J. Biochem. 157 (1986) 27-31. [PMID: 3011431]
4. Strushkevich, N., MacKenzie, F., Cherkesova, T., Grabovec, I., Usanov, S. and Park, H.W. Structural basis for pregnenolone biosynthesis by the mitochondrial monooxygenase system. Proc. Natl. Acad. Sci. USA 108 (2011) 10139-10143. [PMID: 21636783]
5. Mast, N., Annalora, A.J., Lodowski, D.T., Palczewski, K., Stout, C.D. and Pikuleva, I.A. Structural basis for three-step sequential catalysis by the cholesterol side chain cleavage enzyme CYP11A1. J. Biol. Chem. 286 (2011) 5607-5613. [PMID: 21159775]
Accepted name: choline monooxygenase
Reaction: choline + O2 + 2 reduced ferredoxin + 2 H+ = betaine aldehyde hydrate + H2O + 2 oxidized ferredoxin
Glossary: betaine = glycine betaine = N,N,N-trimethylammonioacetate
betaine aldehyde = N,N,N-trimethyl-2-oxoethylammonium
choline = (2-hydroxyethyl)trimethylammonium
Systematic name: choline,reduced-ferredoxin:oxygen oxidoreductase
Comments: The spinach enzyme, which is located in the chloroplast, contains a Rieske-type [2Fe-2S] cluster, and probably also a mononuclear Fe centre. Requires Mg2+. Catalyses the first step of glycine betaine synthesis. In many bacteria, plants and animals, betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. Different enzymes are involved in the first reaction. In plants, the reaction is catalysed by this enzyme whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase) [7]. The enzyme involved in the second step, EC 1.2.1.8 (betaine-aldehyde dehydrogenase), appears to be the same in plants, animals and bacteria. In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 118390-76-4
References:
1. Brouquisse, R., Weigel, P., Rhodes, D., Yocum, C.F. and Hanson, A.D. Evidence for a ferredoxin-dependent choline monooxygenase from spinach chloroplast stroma. Plant Physiol. 90 (1989) 322-329. [PMID: 16666757]
2. Burnet, M., Lafontaine, P.J. and Hanson, A.D. Assay, purification, and partial characterization of choline monooxygenase from spinach. Plant Physiol. 108 (1995) 581-588. [PMID: 12228495]
3. Rathinasabapathi, B., Burnet, M., Russell, B.L., Gage, D.A., Liao, P., Nye, G.J., Scott, P., Golbeck, J.H. and Hanson, A.D. Choline monooxygenase, an unusual iron-sulfur enzyme catalyzing the first step of glycine betaine synthesis in plants: Prosthetic group characterization and cDNA cloning. Proc. Natl. Acad. Sci. USA 94 (1997) 3454-3458. [PMID: 9096415]
4. Russell, B.L., Rathinasabapathi, B. and Hanson, A.D. Osmotic stress induces expression of choline monooxygenase in sugar beet and amaranth. Plant Physiol. 116 (1998) 859-865. [PMID: 9489025]
5. Nuccio, M.L., Russell, B.L., Nolte, K.D., Rathinasabapathi, B., Gage, D.A. and Hanson, A.D. Glycine betaine synthesis in transgenic tobacco expressing choline monooxygenase is limited by the endogenous choline supply. Plant J. 16 (1998) 101-110.
6. Nuccio, M.L., Russell, B.L., Nolte, K.D., Rathinasabapathi, B., Gage, D.A. and Hanson, A.D. The endogenous choline supply limits glycine betaine synthesis in transgenic tobacco expressing choline. Plant J. 16 (1998) 487-496. [PMID: 9881168]
7. Waditee, R., Tanaka, Y., Aoki, K., Hibino, T., Jikuya, H., Takano, J., Takabe, T. and Takabe, T. Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica. J. Biol. Chem. 278 (2003) 4932-4942. [PMID: 12466265]
Accepted name: steroid 15β-monooxygenase
Reaction: progesterone + reduced ferredoxin + O2 = 15β-hydroxyprogesterone + oxidized ferredoxin + H2O
Other name(s): cytochrome P-450meg; cytochrome P450meg; steroid 15β-hydroxylase; CYP106A2; BmCYP106A2
Systematic name: progesterone,reduced-ferredoxin:oxygen oxidoreductase (15β-hydroxylating)
Comments: The enzyme from Bacillus megaterium hydroxylates a variety of 3-oxo-Δ4-steroids in position 15β. Ring A-reduced, aromatic, and 3β-hydroxy-Δ4-steroids do not serve as substrates [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Berg, A., Ingelman-Sundberg, M. and Gustafsson, J.A. Purification and characterization of cytochrome P-450meg. J. Biol. Chem. 254 (1979) 5264-5271. [PMID: 109432]
2. Berg, A., Gustafsson, J.A. and Ingelman-Sundberg, M. Characterization of a cytochrome P-450-dependent steroid hydroxylase system present in Bacillus megaterium. J. Biol. Chem. 251 (1976) 2831-2838. [PMID: 177422]
3. Lisurek, M., Kang, M.J., Hartmann, R.W. and Bernhardt, R. Identification of monohydroxy progesterones produced by CYP106A2 using comparative HPLC and electrospray ionisation collision-induced dissociation mass spectrometry. Biochem. Biophys. Res. Commun. 319 (2004) 677-682. [PMID: 15178459]
4. Goni, G., Zollner, A., Lisurek, M., Velazquez-Campoy, A., Pinto, S., Gomez-Moreno, C., Hannemann, F., Bernhardt, R. and Medina, M. Cyanobacterial electron carrier proteins as electron donors to CYP106A2 from Bacillus megaterium ATCC 13368. Biochim. Biophys. Acta 1794 (2009) 1635-1642. [PMID: 19635596]
5. Lisurek, M., Simgen, B., Antes, I. and Bernhardt, R. Theoretical and experimental evaluation of a CYP106A2 low homology model and production of mutants with changed activity and selectivity of hydroxylation. Chembiochem 9 (2008) 1439-1449. [PMID: 18481342]
Accepted name: spheroidene monooxygenase
Reaction: (1) spheroidene + reduced ferredoxin + O2 = spheroiden-2-one + oxidized ferredoxin + H2O
(2) spirilloxantin + reduced ferredoxin + O2 = 2-oxospirilloxanthin + oxidized ferredoxin + H2O
(3) 2'-oxospirilloxanthin + reduced ferredoxin + O2 = 2,2'-dioxospirilloxanthin + oxidized ferredoxin + H2O
For diagram of reaction click here or click here.
Glossary: spheroidene = 1-methoxy-3,4-didehydro-1,2,7',8'-tetrahydro-ψ,ψ-carotene
Other name(s): CrtA; acyclic carotenoid 2-ketolase; spirilloxantin monooxygenase; 2-oxo-spirilloxanthin monooxygenase
Systematic name: spheroidene,reduced-ferredoxin:oxygen oxidoreductase (spheroiden-2-one-forming)
Comments: The enzyme is involved in spheroidenone biosynthesis and in 2,2'-dioxospirilloxanthin biosynthesis. The enzyme from Rhodobacter sphaeroides contains heme at its active site [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Lee, P.C., Holtzapple, E. and Schmidt-Dannert, C. Novel activity of Rhodobacter sphaeroides spheroidene monooxygenase CrtA expressed in Escherichia coli. Appl. Environ. Microbiol. 76 (2010) 7328-7331. [PMID: 20851979]
2. Gerjets, T., Steiger, S. and Sandmann, G. Catalytic properties of the expressed acyclic carotenoid 2-ketolases from Rhodobacter capsulatus and Rubrivivax gelatinosus. Biochim. Biophys. Acta 1791 (2009) 125-131. [PMID: 19136077]
Accepted name: (+)-camphor 6-endo-hydroxylase
Reaction: (+)-camphor + reduced putidaredoxin + O2 = (+)-6-endo-hydroxycamphor + oxidized putidaredoxin + H2O
For diagram of reaction click here.
Other name(s): P450camr
Systematic name: (+)-camphor,reduced putidaredoxin:oxygen oxidoreductase (6-endo-hydroxylating)
Comments: A cytochrome P-450 monooxygenase from the bacterium Rhodococcus sp. NCIMB 9784.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Grogan, G., Roberts, G.A., Parsons, S., Turner, N.J. and Flitsch, S.L. P450camr, a cytochrome P450 catalysing the stereospecific 6-endo-hydroxylation of (1R)-(+)-camphor. Appl. Microbiol. Biotechnol. 59 (2002) 449-454. [PMID: 12172608]
Accepted name: pentalenic acid synthase
Reaction: 1-deoxypentalenate + reduced ferredoxin + O2 = pentalenate + oxidized ferredoxin + H2O
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
pentalenate = (1R,3aR,5aS,6R,8aS)-6-hydroxy-1,7,7-trimethyl-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene-4-carboxylate
Other name(s): CYP105D7; sav7469 (gene name)
Systematic name: 1-deoxypentalenate,reduced ferredoxin:O2 oxidoreductase
Comments: A heme-thiolate enzyme (P-450). Isolated from the bacterium Streptomyces avermitilis. The product, pentalenate, is a co-metabolite from pentalenolactone biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Takamatsu, S., Xu, L.H., Fushinobu, S., Shoun, H., Komatsu, M., Cane, D.E. and Ikeda, H. Pentalenic acid is a shunt metabolite in the biosynthesis of the pentalenolactone family of metabolites: hydroxylation of 1-deoxypentalenic acid mediated by CYP105D7 (SAV_7469) of Streptomyces avermitilis. J. Antibiot. (Tokyo) 64 (2011) 65-71. [PMID: 21081950]
Accepted name: pimeloyl-[acyl-carrier protein] synthase
Reaction: a long-chain acyl-[acyl-carrier protein] + 2 reduced flavodoxin + 3 O2 = pimeloyl-[acyl-carrier protein] + an n-alkanal + 2 oxidized flavodoxin + 3 H2O (overall reaction)
(1a) a long-chain acyl-[acyl-carrier protein] + reduced flavodoxin + O2 = a (7S)-7-hydroxy-long-chain-acyl-[acyl-carrier protein] + oxidized flavodoxin + H2O
(1b) a (7S)-7-hydroxy-long-chain-acyl-[acyl-carrier protein] + reduced flavodoxin + O2 = a (7R,8R)-7,8-dihydroxy-long-chain-acyl-[acyl-carrier protein] + oxidized flavodoxin + H2O
(1c) a (7R,8R)-7,8-dihydroxy-long-chain-acyl-[acyl-carrier protein] + reduced flavodoxin + O2 = a 7-oxoheptanoyl-[acyl-carrier protein] + an n-alkanal + oxidized flavodoxin + 2 H2O
(1d) a 7-oxoheptanoyl-[acyl-carrier protein] + oxidized flavodoxin + H2O = a pimeloyl-[acyl-carrier protein] + reduced flavodoxin + H+
Glossary: palmitoyl-[acyl-carrier protein] = hexadecanoyl-[acyl-carrier protein]
pimeloyl-[acyl-carrier protein] = 7-hydroxy-7-oxoheptanoyl-[acyl-carrier protein]
Other name(s): bioI (gene name); P450BioI; CYP107H1
Systematic name: acyl-[acyl-carrier protein],reduced-flavodoxin:oxygen oxidoreductase (pimeloyl-[acyl-carrier protein] forming)
Comments: A heme-thiolate protein (P-450). The enzyme catalyses an oxidative C-C bond cleavage of long-chain acyl-[acyl-carrier protein]s of various lengths to generate pimeloyl-[acyl-carrier protein], an intermediate in the biosynthesis of biotin. The preferred substrate of the enzyme from the bacterium Bacillus subtilis is palmitoyl-[acyl-carrier protein] which then gives heptanal as the alkanal. The mechanism is similar to EC 1.14.15.6, cholesterol monooxygenase (side-chain-cleaving), followed by a hydroxylation step, which may occur spontaneously [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Stok, J.E. and De Voss, J. Expression, purification, and characterization of BioI: a carbon-carbon bond cleaving cytochrome P450 involved in biotin biosynthesis in Bacillus subtilis. Arch. Biochem. Biophys. 384 (2000) 351-360. [PMID: 11368323]
2. Cryle, M.J. and De Voss, J.J. Carbon-carbon bond cleavage by cytochrome p450(BioI)(CYP107H1). Chem. Commun. (Camb.) (2004) 86-87. [PMID: 14737344]
3. Cryle, M.J. and Schlichting, I. Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI) ACP complex. Proc. Natl. Acad. Sci. USA 105 (2008) 15696-15701. [PMID: 18838690]
4. Cryle, M.J. Selectivity in a barren landscape: the P450(BioI)-ACP complex. Biochem. Soc. Trans. 38 (2010) 934-939. [PMID: 20658980]
Accepted name: phenylalanine 4-monooxygenase
Reaction: L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin
For diagram click here and here also for mechanism.
Other name(s): phenylalaninase; phenylalanine 4-hydroxylase; phenylalanine hydroxylase
Systematic name: L-phenylalanine,tetrahydrobiopterin:oxygen oxidoreductase (4-hydroxylating)
Comments: The active centre contains mononuclear iron(II). The reaction involves an arene oxide that rearranges to give the phenolic hydroxy group. This results in the hydrogen at C-4 migrating to C-3 and in part being retained. This process is known as the NIH-shift. The 4a-hydroxytetrahydrobiopterin formed can dehydrate to 6,7-dihydrobiopterin, both spontaneously and by the action of EC 4.2.1.96, 4a-hydroxytetrahydrobiopterin dehydratase. The 6,7-dihydrobiopterin can be enzymically reduced back to tetrahydrobiopterin, by EC 1.5.1.34, 6,7-dihydropteridine reductase, or slowly rearranges into the more stable compound 7,8-dihydrobiopterin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-73-6
References:
1. Guroff, G. and Rhoads, C.A. Phenylalanine hydroxylation by Pseudomonas species (ATCC 11299a). Nature of the cofactor. J. Biol. Chem. 244 (1969) 142-146. [PMID: 5773277]
2. Kaufman, S. Studies on the mechanism of the enzymic conversion of phenylalanine to tyrosine. J. Biol. Chem. 234 (1959) 2677-2682.
3. Mitoma, C. Studies on partially purified phenylalanine hydroxylase. Arch. Biochem. Biophys. 60 (1956) 476-484.
4. Udenfriend, S. and Cooper, J.R. The enzymic conversion of phenylalanine to tyrosine. J. Biol. Chem. 194 (1952) 503-511.
5. Carr, R.T., Balasubramanian, S., Hawkins, P.C. and Benkovic, S.J. Mechanism of metal-independent hydroxylation by Chromobacterium violaceum phenylalanine hydroxylase. Biochemistry 34 (1995) 7525-7532. [PMID: 7779797]
6. Andersen, O.A., Flatmark, T. and Hough, E. High resolution crystal structures of the catalytic domain of human phenylalanine hydroxylase in its catalytically active Fe(II) form and binary complex with tetrahydrobiopterin. J. Mol. Biol. 314 (2001) 266-278. [PMID: 11718561]
7. Erlandsen, H., Kim, J.Y., Patch, M.G., Han, A., Volner, A., Abu-Omar, M.M. and Stevens, R.C. Structural comparison of bacterial and human iron-dependent phenylalanine hydroxylases: similar fold, different stability and reaction rates. J. Mol. Biol. 320 (2002) 645-661. [PMID: 12096915]
Accepted name: tyrosine 3-monooxygenase
Reaction: L-tyrosine + tetrahydrobiopterin + O2 = L-dopa + 4a-hydroxytetrahydrobiopterin
For diagram click here and here.
Glossary: L-dopa = 3,4-dihydroxy-L-phenylalanine
Other name(s): L-tyrosine hydroxylase; tyrosine 3-hydroxylase; tyrosine hydroxylase
Systematic name: L-tyrosine,tetrahydrobiopterin:oxygen oxidoreductase (3-hydroxylating)
Comments: The active centre contains mononuclear iron(II). The enzyme is activated by phosphorylation, catalysed by EC 2.7.11.27, [acetyl-CoA caboxylase]kinase. The 4a-hydroxytetrahydrobiopterin formed can dehydrate to 6,7-dihydrobiopterin, both spontaneously and by the action of EC 4.2.1.96, 4a-hydroxytetrahydrobiopterin dehydratase. The 6,7-dihydrobiopterin can be enzymically reduced back to tetrahydrobiopterin, by EC 1.5.1.34 (6,7-dihydropteridine reductase), or slowly rearranges into the more stable compound 7,8-dihydrobiopterin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9036-22-0
References:
1. El Mestikawy, S., Glowinski, J. and Hamon, M. Tyrosine hydroxylase activation in depolarized dopaminergic terminals -involvement of Ca2+-dependent phosphorylation. Nature (Lond.) 302 (1983) 830-832. [PMID: 6133218]
2. Ikeda, M., Levitt, M. and Udenfriend, S. Phenylalanine as substrate and inhibitor of tyrosine hydroxylase. Arch. Biochem. Biophys. 120 (1967) 420-427. [PMID: 6033458]
3. Nagatsu, T., Levitt, M. and Udenfriend, S. Tyrosine hydroxylase. The initial step in norepinephrine biosynthesis. J. Biol. Chem. 239 (1964) 2910-2917.
4. Pigeon, D., Drissi-Daoudi, R., Gros, F. and Thibault, J. Copurification of tyrosine-hydroxylase from rat pheochromocytoma, with a protein-kinase activity. C.R. Acad. Sci. Paris, Ser. 3, 302 (1986) 435-438. [PMID: 2872947]
5. Goodwill, K.E., Sabatier, C., Marks, C., Raag, R., Fitzpatrick, P.F. and Stevens, R.C. Crystal structure of tyrosine hydroxylase at 2.3 Å and its implications for inherited neurodegenerative diseases. Nat. Struct. Biol. 4 (1997) 578-585. [PMID: 9228951]
Accepted name: anthranilate 3-monooxygenase
Reaction: anthranilate + tetrahydrobiopterin + O2 = 3-hydroxyanthranilate + dihydrobiopterin + H2O
Other name(s): anthranilate 3-hydroxylase; anthranilate hydroxylase; anthranilic hydroxylase; anthranilic acid hydroxylase
Systematic name: anthranilate,tetrahydrobiopterin:oxygen oxidoreductase (3-hydroxylating)
Comments: Requires Fe2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37256-79-4
References:
1. Jequier, E., Robinson, B.S., Lovenberg, W. and Sjoerdsma, A. Further studies on tryptophan hydroxylase in rat brainstem and beef pineal. Biochem. Pharmacol. 18 (1969) 1071-1081. [PMID: 5789774]
2. Nair, P.M. and Vaidyanathan, C.S. Anthranilic acid hydroxylase from Tecoma stans. Biochim. Biophys. Acta 110 (1965) 521-531.
Accepted name: tryptophan 5-monooxygenase
Reaction: L-tryptophan + tetrahydrobiopterin + O2 = 5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin
For diagram click here.
Other name(s): L-tryptophan hydroxylase; indoleacetic acid-5-hydroxylase; tryptophan 5-hydroxylase; tryptophan hydroxylase
Systematic name: L-tryptophan,tetrahydrobiopterin:oxygen oxidoreductase (5-hydroxylating)
Comments: The active centre contains mononuclear iron(II). The enzyme is activated by phosphorylation, catalysed by a Ca2+-activated protein kinase. The 4a-hydroxytetrahydrobiopterin formed can dehydrate to 6,7-dihydrobiopterin, both spontaneously and by the action of EC 4.2.1.96, 4a-hydroxytetrahydrobiopterin dehydratase. The 6,7-dihydrobiopterin can be enzymically reduced back to tetrahydrobiopterin, by EC 1.5.1.34 (6,7-dihydropteridine reductase), or slowly rearranges into the more stable compound 7,8-dihydrobiopterin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9037-21-2
References:
1. Friedman, P.A., Kappelman, A.H. and Kaufman, S. Partial purification and characterization of tryptophan hydroxylase from rabbit hindbrain. J. Biol. Chem. 247 (1972) 4165-4173. [PMID: 4402511]
2. Hamon, M., Bourgoin, S., Artaud, F. and Glowinski, J. The role of intraneuronal 5-HT and of tryptophan hydroxylase activation in the control of 5-HT synthesis in rat brain slices incubated in K+-enriched medium. J. Neurochem. 33 (1979) 1031-1042. [PMID: 315449]
3. Ichiyama, A., Nakamura, S., Nishizuka, Y. and Hayaishi, O. Enzymic studies on the biosynthesis of serotonin in mammalian brain. J. Biol. Chem. 245 (1970) 1699-1709. [PMID: 5309585]
4. Jequier, E., Robinson, B.S., Lovenberg, W. and Sjoerdsma, A. Further studies on tryptophan hydroxylase in rat brainstem and beef pineal. Biochem. Pharmacol. 18 (1969) 1071-1081. [PMID: 5789774]
5. Wang, L., Erlandsen, H., Haavik, J., Knappskog, P.M. and Stevens, R.C. Three-dimensional structure of human tryptophan hydroxylase and its implications for the biosynthesis of the neurotransmitters serotonin and melatonin. Biochemistry 41 (2002) 12569-12574. [PMID: 12379098]
Accepted name: alkylglycerol monooxygenase
Reaction: 1-alkyl-sn-glycerol + tetrahydrobiopterin + O2 = 1-O-alkyl-sn-glycerol + dihydrobiopterin + H2O
Other name(s): glyceryl-ether monooxygenase; glyceryl-ether cleaving enzyme; alkylglycerol monooxygenase; glyceryl ether oxygenase; glyceryl etherase; O-alkylglycerol monooxygenase
Systematic name: 1-alkyl-sn-glycerol,tetrahydrobiopterin:oxygen oxidoreductase
Comments: The enzyme cleaves alkylglycerols, but does not cleave alkenylglycerols (plasmalogens). Requires reduced glutathione and phospholipids for full activity. The product spontaneously breaks down to form a fatty aldehyde and glycerol.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37256-82-9
References:
1. Ishibashi, T. and Imai, Y. Solubilization and partial characterization of alkylglycerol monooxygenase from rat liver microsomes. Eur. J. Biochem. 132 (1983) 23-27. [PMID: 6840084]
2. Pfleger, E.C., Piantadosi, C. and Snyder, F. The biocleavage of isomeric glyceryl ethers by soluble liver enzymes in a variety of species. Biochim. Biophys. Acta 144 (1967) 633-648. [PMID: 4383918]
3. Snyder, F., Malone, B. and Piantadosi, C. Tetrahydropteridine-dependent cleavage enzyme for O-alkyl lipids: substrate specificity. Biochim. Biophys. Acta 316 (1973) 259-265. [PMID: 4355017]
4. Soodsma, J.F., Piantadosi, C. and Snyder, F. Partial characterization of the alkylglycerol cleavage enzyme system of rat liver. J. Biol. Chem. 247 (1972) 3923-3929. [PMID: 4402391]
5. Tietz, A., Lindberg, M. and Kennedy, E.P. A new pteridine-requiring enzyme system for the oxidation of glyceryl ethers. J. Biol. Chem. 239 (1964) 4081-4090. [PMID: 14247652]
6. Taguchi, H. and Armarego, W.L. Glyceryl-ether monooxygenase [EC 1.14.16.5]. A microsomal enzyme of ether lipid metabolism. Med. Res. Rev. 18 (1998) 43-89. [PMID: 9436181]
Accepted name: mandelate 4-monooxygenase
Reaction: (S)-2-hydroxy-2-phenylacetate + tetrahydrobiopterin + O2 = (S)-4-hydroxymandelate + dihydrobiopterin + H2O
Glossary: (S)-4-hydroxymandelate = (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate
Other name(s): L-mandelate 4-hydroxylase; mandelic acid 4-hydroxylase
Systematic name: (S)-2-hydroxy-2-phenylacetate,tetrahydrobiopterin:oxygen oxidoreductase (4-hydroxylating)
Comments: Requires Fe2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 39459-82-0
References:
1. Bhat, S.G. and Vaidyanathan, C.S. Purifications and properties of L-mandelate-4-hydroxylase from Pseudomonas convexa. Arch. Biochem. Biophys. 176 (1976) 314-323. [PMID: 9909]
Accepted name: dopamine β-monooxygenase
Reaction: dopamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O
For diagram click here.
Glossary: dopamine = 4-(2-aminoethyl)benzene-1,2-diol
Other name(s): dopamine β-hydroxylase; MDBH (membrane-associated dopamine β-monooxygenase); SDBH (soluble dopamine β-monooxygenase); dopamine-B-hydroxylase; oxygenase, dopamine β-mono-; 3,4-dihydroxyphenethylamine β-oxidase; 4-(2-aminoethyl)pyrocatechol β-oxidase; dopa β-hydroxylase; dopamine β-oxidase; dopamine hydroxylase; phenylamine β-hydroxylase; (3,4-dihydroxyphenethylamine)β-mono-oxygenase; DβM
Systematic name: 3,4-dihydroxyphenethylamine,ascorbate:oxygen oxidoreductase (β-hydroxylating)
Comments: A copper protein. Stimulated by fumarate. Formerly EC 1.14.2.1.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9013-38-1
References:
1. Friedman, S. and Kaufman, S. 3,4-Dihydroxyphenylethylamine β-hydroxylase. Physical properties, copper content, and role of copper in the catalytic activity. J. Biol. Chem. 240 (1965) 4763-4773. [PMID: 5846992]
2. Levin, E.Y., Levenberg, B. and Kaufman, S. The enzymatic conversion of 3,4-dihydroxyphenylethylamine to norepinephrine. J. Biol. Chem. 235 (1960) 2080-2086.
[EC 1.14.17.2 Deleted entry: 4-coumarate 3-monooxygenase. Now included with EC 1.14.18.1 monophenol monooxygenase (EC 1.14.17.2 created 1972, deleted 1984)]
Accepted name: peptidylglycine monooxygenase
Reaction: peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
Other name(s): peptidylglycine 2-hydroxylase; peptidyl α-amidating enzyme; peptide-α-amide synthetase; synthase, peptide α-amide; peptide α-amidating enzyme; peptide α-amide synthase; peptidylglycine α-hydroxylase; peptidylglycine α-amidating monooxygenase; PAM-A; PAM-B; PAM
Systematic name: peptidylglycine,ascorbate:oxygen oxidoreductase (2-hydroxylating)
Comments: A copper protein. Peptidylglycines with a neutral amino acid residue in the penultimate position are the best substrates for the enzyme. The product is unstable and dismutates to glyoxylate and the corresponding desglycine peptide amide, a reaction catalysed by EC 4.3.2.5 peptidylamidoglycolate lyase. Involved in the final step of biosynthesis of α-melanotropin and related biologically active peptides.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 90597-47-0
References:
1. Bradbury, A.F., Finnie, M.D.A. and Smyth, D.G. Mechanism of C-terminal amide formation by pituitary enzymes. Nature (Lond.) 298 (1982) 686-688. [PMID: 7099265]
2. Bradbury, A.F. and Smyth, D.G. Enzyme-catalysed peptide amidation. Isolation of a stable intermediate formed by reaction of the amidating enzyme with an imino acid. Eur. J. Biochem. 169 (1987) 579-584. [PMID: 3691506]
3. Glembotski, C.G.Further characterization of the peptidyl α-amidating enzyme in rat anterior pituitary secretory granules. Arch. Biochem. Biophys. 241 (1985) 673-683. [PMID: 2994573]
4. Katopodis, A.G., Ping, D. and May, S.W. A novel enzyme from bovine neurointermediate pituitary catalyzes dealkylation of α-hydroxyglycine derivatives, thereby functioning sequentially with peptidylglycine α-amidating monooxygenase in peptide amidation. Biochemistry 29 (1990) 6115-6120. [PMID: 2207061]
5.Murthy, A.S.N., Keutmann, H.T. and Eipper, B.A. Further characterization of peptidylglycine α-amidating monooxygenase from bovine neurointermediate pituitary. Mol. Endocrinol. 1 (1987) 290-299. [PMID: 3453894]
6.Murthy, A.S.N., Mains, R.E. and Eipper, B.A. Purification and characterization of peptidylglycine α-amidating monooxygenase from bovine neurointermediate pituitary. J.Biol. Chem. 261 (1986) 1815-1822. [PMID: 3944110]
Accepted name: aminocyclopropanecarboxylate oxidase
Reaction: 1-aminocyclopropane-1-carboxylate + ascorbate + O2 = ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
For diagram click here.
Other name(s): ACC oxidase; ethylene-forming enzyme
Systematic name: 1-aminocyclopropane-1-carboxylate oxygenase (ethylene-forming)
Comments: A nonheme iron enzyme. Requires CO2 for activity. In the enzyme from plants, the ethylene has signalling functions such as stimulation of fruit-ripening.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 98668-53-2
References:
1. Zhang, Z.H., Schofield, C.J., Baldwin, J.E., Thomas, P. and John, P. Expression, purification and characterization of 1-aminocyclopropane-1-carboxylate oxidase from tomato in Escherichia coli. Biochem. J. 307 (1995) 77-85. [PMID: 7717997]
2. Zhang, Z.H., Barlow, J.N., Baldwin, J.E. and Schofield, C.J. Metal-catalyzed oxidation and mutagenesis studies on the iron(II) binding site of 1-aminocyclopropane-1-carboxylate oxidase. Biochemistry 36 (1997) 15999-16007. [PMID: 9398335]
3. Pirrung, M.C. Ethylene biosynthesis from 1-aminocyclopropanecarboxylic acid. Acc. Chem. Res. 32 (1999) 711-718.
4. Charng, Y., Chou, S.J., Jiaang, W.T., Chen, S.T. and Yang, S.F. The catalytic mechanism of 1-aminocyclopropane-1-carboxylic acid oxidase. Arch. Biochem. Biophys. 385 (2001) 179-185. [PMID: 11361015]
5. Thrower, J.S., Blalock, R. and Klinman, J.P. Steady-state kinetics of substrate binding and iron release in tomato ACC oxidase. Biochemistry 40 (2001) 9717-9724. [PMID: 11583172]
Accepted name: tyrosinase
Reaction: (1) L-tyrosine + O2 = dopaquinone + H2O (overall reaction)
(1a) L-tyrosine + ½ O2 = L-dopa
(1b) L-dopa + ½ O2 = dopaquinone + H2O
(2) 2 L-dopa + O2 = 2 dopaquinone + 2 H2O
For diagram of reaction click here.
Other name(s): monophenol monooxygenase; phenolase; monophenol oxidase; cresolase; monophenolase; tyrosine-dopa oxidase; monophenol monooxidase; monophenol dihydroxyphenylalanine:oxygen oxidoreductase; N-acetyl-6-hydroxytryptophan oxidase; monophenol, dihydroxy-L-phenylalanine oxygen oxidoreductase; o-diphenol:O2 oxidoreductase; phenol oxidase
Systematic name: L-tyrosine,L-dopa:oxygen oxidoreductase
Comments: A type III copper protein found in a broad variety of bacteria, fungi, plants, insects, crustaceans, and mammals, which is involved in the synthesis of betalains and melanin. The enzyme, which is activated upon binding molecular oxygen, can catalyse both a monophenolase reaction cycle (reaction 1) or a diphenolase reaction cycle (reaction 2). During the monophenolase cycle, one of the bound oxygen atoms is transferred to a monophenol (such as L-tyrosine), generating an o-diphoenol intermediate, which is subsequently oxidized to an o-quinone and released, along with a water molecule. The enzyme remains in an inactive deoxy state, and is restored to the active oxy state by the binding of a new oxygen molecule. During the diphenolase cycle the enzyme binds an external diphenol molecule (such as L-dopa) and oxidizes it to an o-quinone that is released along with a water molecule, leaving the enzyme in the intermediate met state. The enzyme then binds a second diphenol molecule and repeats the process, ending in a deoxy state [7]. The second reaction is identical to that catalysed by the related enzyme catechol oxidase (EC 1.10.3.1). However, the latter can not catalyse the hydroxylation or monooxygenation of monophenols.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9002-10-2
References:
1. Dawson, C.R. and Tarpley, W.B. The copper oxidases. In: Sumner, J.B. and Myrbäck, K. (Eds), The Enzymes, 1st edn, vol. 2, Academic Press, New York, 1951, pp. 454-498.
2. Patil, S.S. and Zucker, M. Potato phenolases. Purification and properties. J. Biol. Chem. 240 (1965) 3938-3943. [PMID: 5842066]
3. Pomerantz, S.H. Separation, purification, and properties of two tyrosinases from hamster melanoma. J. Biol. Chem. 238 (1963) 2351-2357. [PMID: 13972077]
4. Robb, D.A. `Tyrosinase. In: Lontie, R. (Ed.), Copper Proteins and Copper Enzymes, vol. 2, CRC Press, Boca Raton, FL, 1984, pp. 207-240.
5. Sanchez-Ferrer, A., Rodriguez-Lopez, J.N., Garcia-Canovas, F. and Garcia-Carmona, F. Tyrosinase: a comprehensive review of its mechanism. Biochim. Biophys. Acta 1247 (1995) 1-11. [PMID: 7873577]
6. Steiner, U., Schliemann, W. and Strack, D. Assay for tyrosine hydroxylation activity of tyrosinase from betalain-forming plants and cell cultures. Anal. Biochem. 238 (1996) 72-75. [PMID: 8660589]
7. Rolff, M., Schottenheim, J., Decker, H. and Tuczek, F. Copper-O2 reactivity of tyrosinase models towards external monophenolic substrates: molecular mechanism and comparison with the enzyme. Chem Soc Rev 40 (2011) 4077-4098. [PMID: 21416076]
Accepted name: CMP-N-acetylneuraminate monooxygenase
Reaction: CMP-N-acetylneuraminate + 2 ferrocytochrome b5 + O2 + 2 H+ = CMP-N-glycoloylneuraminate + 2 ferricytochrome b5 + H2O
Other name(s): CMP-N-acetylneuraminic acid hydroxylase; CMP-Neu5Ac hydroxylase; cytidine monophosphoacetylneuraminate monooxygenase; N-acetylneuraminic monooxygenase; cytidine-5'-monophosphate-N-acetylneuraminic acid hydroxylase
Systematic name: CMP-N-acetylneuraminate,ferrocytochrome-b5:oxygen oxidoreductase (N-acetyl-hydroxylating)
Comments: This enzyme contains both a Rieske-type [2Fe-2S] cluster and a second iron site. The ferricytochrome b5 produced is reduced by NADH and cytochrome-b5 reductase (EC 1.6.2.2). The enzyme can be activated by Fe2+ or Fe3+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 116036-67-0
References:
1. Shaw, L. and Schauer, R. The biosynthesis of N-glycoloylneuraminic acid occurs by hydroxylation of the CMP-glycoside of N-acetylneuraminic acid. Biol. Chem. Hoppe-Seyler 369 (1988) 477-486. [PMID: 3202954]
2. Kozutsumi, Y., Kawano, T., Yamakawa, T. and Suzuki, A. Participation of cytochrome b5 in CMP-N-acetylneuraminic acid hydroxylation in mouse liver cytosol. J. Biochem. (Tokyo) 109 (1990) 704-706.[PMID: 1964451]
3. Schneckenburger, P., Shaw, L. and Schauer, R. Purification, characterization and reconstitution of CMP-N-acetylneuraminate hydroxylase from mouse liver. Glycoconj. J. 11 (1994) 194-203. [PMID: 7841794]
4. Kawano, T., Koyama, S., Takematsu, H., Kozutsumi, Y., Kawasaki, H., Kawashima, S., Kawasaki, T. and Suzuki, A. Molecular cloning of cytidine monophospho-N-acetylneuraminic acid hydroxylase. Regulation of species- and tissue-specific expression of N-glycolylneuraminic acid. J. Biol. Chem. 270 (1995) 16458-16463. [PMID: 7608218]
5. Schlenzka, W., Shaw, L., Kelm, S., Schmidt, C.L., Bill, E., Trautwein, A.X., Lottspeich, F. and Schauer, R. CMP-N-acetylneuraminic acid hydroxylase: the first cytosolic Rieske iron-sulphur protein to be described in Eukarya. FEBS Lett. 385 (1996) 197-200. [PMID: 8647250]
Accepted name: methane monooxygenase (particulate)
Reaction: methane + quinol + O2 = methanol + quinone + H2O
Systematic name: methane,quinol:oxygen oxidoreductase
Comments: Contains copper. It is membrane-bound, in contrast to the soluble methane monooxygenase (EC 1.14.13.25).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Shiemke, A.K., Cook, S.A., Miley, T. and Singleton, P. Detergent solubilization of membrane-bound methane monooxygenase requires plastoquinol analogs as electron donors. Arch. Biochem. Biophys. 321 (1995) 421-428. [PMID: 7646068]
2. Basu, P., Katterle, B., Andersson, K.K. and Dalton, H. The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein. Biochem. J. 369 (2003) 417-427. [PMID: 12379148]
3. Kitmitto, A., Myronova, N., Basu, P. and Dalton, H. Characterization and structural analysis of an active particulate methane monooxygenase trimer from Methylococcus capsulatus (Bath). Biochemistry 44 (2005) 10954-10965. [PMID: 16101279]
4. Balasubramanian, R. and Rosenzweig, A.C. Structural and mechanistic insights into methane oxidation by particulate methane monooxygenase. Acc. Chem. Res. 40 (2007) 573-580. [PMID: 17444606]
Accepted name: stearoyl-CoA 9-desaturase
Reaction: stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Other name(s): δ9-desaturase; acyl-CoA desaturase; fatty acid desaturase; stearoyl-CoA, hydrogen-donor:oxygen oxidoreductase
Systematic name: stearoyl-CoA,ferrocytochrome-b5:oxygen oxidoreductase (9,10-dehydrogenating)
Comments: An iron protein. The rat liver enzyme is an enzyme system involving cytochrome b5 and EC 1.6.2.2, cytochrome-b5 reductase. The ferricytochrome b5 produced is reduced by NADH and cytochrome-b5 reductase (EC 1.6.2.2).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9014-34-0
References:
1. Fulco, A.J. and Bloch, K. Cofactor requirements for the formation of δ9-unsaturated fatty acids in Mycobacterium phlei. J. Biol. Chem. 239 (1964) 993-997. [PMID: 14167617]
2. Oshino, N., Imai, Y. and Sato, R. Electron-transfer mechanism associated with fatty acid desaturation catalyzed by liver microsomes. Biochim. Biophys. Acta 128 (1966) 13-27. [PMID: 4382040]
3. Oshino, N., Imai, Y. and Sato, R. A function of cytochrome b5 in fatty acid desaturation by rat liver microsomes. J. Biochem. (Tokyo) 69 (1971) 155-167. [PMID: 5543646]
4. Strittmatter, P., Sputz, L., Corcoran, D., Rogers, M.J., Setlow, B. and Redline, R. Purification and properties of rat liver microsomal stearyl coenzyme A desaturase. Proc. Natl. Acad. Sci. USA 71 (1974) 4565-4569. [PMID: 4373719]
Accepted name: acyl-[acyl-carrier-protein] desaturase
Reaction: a stearoyl-[acyl-carrier protein] + reduced acceptor + O2 = an oleoyl-[acyl-carrier protein] + acceptor + 2 H2O
Other name(s): stearyl acyl carrier protein desaturase; stearyl-ACP desaturase; acyl-[acyl-carrier-protein], hydrogen-donor:oxygen oxidoreductase
Systematic name: acyl-[acyl-carrier protein], hydrogen-donor:oxygen oxidoreductase
Comments: The enzyme from safflower is specific for stearoyl-[acyl-carrier protein]; that from Euglena acts on derivatives of a number of long-chain fatty acids. Requires ferredoxin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37256-86-3
References:
1. Jaworski, J.G. and Stumpf, P.K. Fat metabolism in higher plants. Properties of a soluble stearyl-acyl carrier protein desaturase from maturing Carthamus tinctorius. Arch. Biochem. Biophys. 162 (1974) 158-165. [PMID: 4831331]
2. Nagai, J. and Bloch, K. Enzymatic desaturation of stearyl acyl carrier protein. J. Biol. Chem. 243 (1968) 4626-4633. [PMID: 4300868]
Accepted name: linoleoyl-CoA desaturase
Reaction: linoleoyl-CoA + AH2 + O2 = γ-linolenoyl-CoA + A + 2 H2O
Other name(s):δ6-desaturase; δ6-fatty acyl-CoA desaturase; δ6-acyl CoA desaturase; fatty acid δ6-desaturase; fatty acid 6-desaturase; linoleate desaturase; linoleic desaturase; linoleic acid desaturase; linoleoyl CoA desaturase; linoleoyl-coenzyme A desaturase; long-chain fatty acid δ6-desaturase
Systematic name: linoleoyl-CoA,hydrogen-donor:oxygen oxidoreductase
Comments: An iron protein. The rat liver enzyme is an enzyme system involving cytochrome b5 and EC 1.6.2.2, cytochrome- b5 reductase. Formerly EC 1.14.99.25.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9082-66-0
References:
1. Okayasu, T., Nagao, M., Ishibashi, T. and Imai, Y. Purification and partial characterization of linoleoyl-CoA desaturase from rat liver microsomes. Arch. Biochem. Biophys. 206 (1981) 21-28. [PMID: 7212717]
Accepted name: Δ8-fatty-acid desaturase
Reaction: phytosphinganine + reduced acceptor + O2 = Δ8-phytosphingenine + acceptor + 2 H2O
Glossary: phytosphinganine = (4R)-4-hydroxysphinganine
Other name(s): Δ8-sphingolipid desaturase; EFD1; BoDES8; SLD; Δ8 fatty acid desaturase; Δ8-desaturase
Systematic name: phytosphinganine,hydrogen donor:oxygen Δ8-oxidoreductase
Comments: This enzyme, which has been found mainly in plants, introduces a double bond at Δ8 of C18 and C20 fatty acids [2]. The enzyme from the marine microalga Euglena gracilis requires a double bond to be present at Δ11 and is most active with 20:3 Δ11,14,17 and 20:2 Δ11,14 as substrates, although it can also desaturate 20:1 Δ11 [1]. The Δ8-desaturation pathway represents an alternate pathway for the synthesis of the polyunsaturated fatty acids arachidonate (C20:4 Δ5,14) and eicosapentaenoate (C20:5 Δ5,17) in organisms lacking a Δ6-desaturase [1]. The enzyme from the sunflower Helianthus annuus and from the herb Borago officinalis comprises a C-terminal desaturase domain and an N-terminal cytochrome-b5 domain [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Wallis, J.G. and Browse, J. The Δ8-desaturase of Euglena gracilis: an alternate pathway for synthesis of 20-carbon polyunsaturated fatty acids. Arch. Biochem. Biophys. 365 (1999) 307-316. [PMID: 10328826]
2. Sperling, P., Libisch, B., Zähringer, U., Napier, J.A. and Heinz, E. Functional identification of a Δ8-sphingolipid desaturase from Borago officinalis. Arch. Biochem. Biophys. 388 (2001) 293-298. [PMID: 11368168]
3. Takakuwa, N., Kinoshita, M., Oda, Y. and Ohnishi, M. Isolation and characterization of the genes encoding Δ8-sphingolipid desaturase from Saccharomyces kluyveri and Kluyveromyces lactis. Curr. Microbiol. 45 (2002) 459-461. [PMID: 12402089]
4. Beckmann, C., Rattke, J., Oldham, N.J., Sperling, P., Heinz, E. and Boland, W. Characterization of a Δ8-sphingolipid desaturase from higher plants: a stereochemical and mechanistic study on the origin of E,Z isomers. Angew. Chem. Int. Ed. Engl. 41 (2002) 2298-2300. [PMID: 12203571]
Accepted name: Δ11-fatty-acid desaturase
Reaction: acyl-CoA + reduced acceptor + O2 = Δ11-acyl-CoA + acceptor + 2 H2O
Other name(s): Δ11 desaturase; fatty acid Δ11-desaturase; TpDESN; Cro-PG; Δ11 fatty acid desaturase; Z/E11-desaturase; Δ11-palmitoyl-CoA desaturase
Systematic name: acyl-CoA,hydrogen donor:oxygen Δ11-oxidoreductase
Comments: In common with front-end desaturases involved in the synthesis of polyunsaturated fatty acids (PUFAs), this membrane-bound enzyme has a cytochrome b5-like domain at the N-terminus and contains three histidine boxes that are critical for desaturase activity [1]. The enzyme from the marine microalga Thalassiosira pseudonana specifically desaturates palmitic acid 16:0 to 16:1Δ11 [1] whereas that from the leafroller moth Choristoneura rosaceana desaturates myristic acid 14:0 to 14:1Δ11 [2]. 16:1Δ11 represents an important precursor for pheromone synthesis in insect cells, although its function in microalgae is currently unknown [1]. The enzyme from the Egyptian cotton leafworm Spodoptera littoralis has a preference for palmitoyl-CoA as substrate and for NADH rather than NADPH as reduced acceptor [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Tonon, T., Harvey, D., Qing, R., Li, Y., Larson, T.R. and Graham, I.A. Identification of a fatty acid Δ11-desaturase from the microalga Thalassiosira pseudonana. FEBS Lett. 563 (2004) 28-34. [PMID: 15063718]
2. Hao, G., O'Connor, M., Liu, W. and Roelofs, W.L. Characterization of Z/E11- and Z9-desaturases from the obliquebanded leafroller moth, Choristoneura rosaceana. J. Insect Sci. 2:26 (2002) 1-7.
3. Rodriguez, F., Hallahan, D.L., Pickett, J.A. and Camps, F. Characterization of the Δ11-palmitoyl-CoA-desaturase from Spodoptera littoralis (Lepidoptera:Noctuidae). Insect Biochem. Mol. Biol. 22 (1992) 143-148.
Accepted name: Δ12-fatty-acid desaturase
Reaction: acyl-CoA + reduced acceptor + O2 = Δ12-acyl-CoA + acceptor + 2 H2O
Glossary: oleoyl-CoA = cis-octadec-9-enoyl-CoA = (9Z)-octadec-9-enoyl-CoA = 18:1 cis-9 = 18:1(n-9)
linoleoyl-CoA = cis,cis-octadeca-9,12-dienoyl-CoA = (9Z,12Z)-octadeca-9,12-dienoyl-CoA = 18:2(n-6)
Other name(s): Δ12 fatty acid desaturase; Δ12(ω6)-desaturase; oleoyl-CoA Δ12 desaturase; Δ12 desaturase; Δ12-desaturase
Systematic name: acyl-CoA,hydrogen donor:oxygen Δ12-oxidoreductase
Comments: In the yeast Lipomyces starkeyi [3] and in the American cockroach [1], this microsomal enzyme converts oleoyl-CoA into linoleoyl-CoA. In the moths Cadra cautella and Spodoptera, the enzyme converts (Z)-tetradec-9-enoic acid into (9Z,12E)-tetradeca-9,12-dienoic acid, which is reduced and acetylated to form the acetate ester pheromone [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Borgeson, C.E., de Renobales, M. and Blomquist, G.J. Characterization of the Δ12 desaturase in the American cockroach, Periplaneta americana: the nature of the substrate. Biochim. Biophys. Acta 1047 (1990) 135-140. [PMID: 2248971]
2. Jurenka, R.A. Biosynthetic pathway for producing the sex pheromone component (Z,E)-9,12-tetradecadienyl acetate in moths involves a Δ12 desaturase. Cell. Mol. Life Sci. 53 (1997) 501-505. [PMID: 9230926]
3. Lomascolo, A., Dubreucq, E. and Galzy, P. Study of the Δ12-desaturase system of Lipomyces starkeyi. Lipids 31 (1996) 253-259. [PMID: 8900454]
4. Tocher, D.R., Leaver, M.J. and Hodgson, P.A. Recent advances in the biochemistry and molecular biology of fatty acyl desaturases. Prog. Lipid Res. 37 (1998) 73-117. [PMID: 9829122]
Accepted name: (S)-2-hydroxypropylphosphonic acid epoxidase
Reaction: (S)-2-hydroxypropylphosphonate + 2 NADH + O2 = (1R,2S)-epoxypropylphosphonate + 2 H2O + 2 NAD+
Glossary: (1R,2S)-epoxypropylphosphonate = fosfomycin
Other name(s): HPP epoxidase; HppE; 2-hydroxypropylphosphonic acid epoxidase; Fom4; (S)-2-hydroxypropylphosphonate epoxidase
Systematic name: (S)-2-hydroxypropylphosphonate,NADH:oxygen epoxidase
Comments: Contains one non-heme iron centre per monomer [1,5]. FMN is required to mediate the transfer of reducing equivalents from NADH to the active site iron [1]. This is the last enzyme in the biosynthetic pathway of fosfomycin, a broad-spectrum antibiotic produced by certain Streptomyces species.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Munos, J.W., Moon, S.J., Mansoorabadi, S.O., Chang, W., Hong, L., Yan, F., Liu, A. and Liu, H.W. Purification and characterization of the epoxidase catalyzing the formation of fosfomycin from Pseudomonas syringae. Biochemistry 47 (2008) 8726-8735. [PMID: 18656958]
2. Yan, F., Moon, S.J., Liu, P., Zhao, Z., Lipscomb, J.D., Liu, A. and Liu, H.W. Determination of the substrate binding mode to the active site iron of (S)-2-hydroxypropylphosphonic acid epoxidase using 17O-enriched substrates and substrate analogues. Biochemistry 46 (2007) 12628-12638. [PMID: 17927218]
3. Hidaka, T., Goda, M., Kuzuyama, T., Takei, N., Hidaka, M. and Seto, H. Cloning and nucleotide sequence of fosfomycin biosynthetic genes of Streptomyces wedmorensis. Mol. Gen. Genet. 249 (1995) 274-280. [PMID: 7500951]
4. Liu, P., Mehn, M.P., Yan, F., Zhao, Z., Que, L., Jr. and Liu, H.W. Oxygenase activity in the self-hydroxylation of (S)-2-hydroxypropylphosphonic acid epoxidase involved in fosfomycin biosynthesis. J. Am. Chem. Soc. 126 (2004) 10306-10312. [PMID: 15315444]
5. Higgins, L.J., Yan, F., Liu, P., Liu, H.W. and Drennan, C.L. Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme. Nature 437 (2005) 838-844. [PMID: 16015285]
Accepted name: deacetoxycephalosporin-C synthase
Reaction: penicillin N + 2-oxoglutarate + O2 = deacetoxycephalosporin C + succinate + CO2 + H2O
For diagram click here.
Other names: DAOCS; penicillin N expandase; DAOC synthase
Systematic name: penicillin-N,2-oxoglutarate:oxygen oxidoreductase (ring-expanding)
Comments: Forms part of the penicillin biosynthesis pathway (for pathway, click here).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 85746-10-7
References:
1. Cantwell, C., Beckmann, R., Whiteman, P., Queener, S.W. and Abraham, E.P. Isolation of deacetoxycephalosporin-c from fermentation broths of Penicillium chrysogenum transformants - construction of a new fungal biosynthetic-pathway. Proc. R. Soc. Lond. B Biol. Sci. 248 (1992) 283-289. [PMID: 1354366]
2. Lee, H.J., Lloyd, M.D., Harlos, K., Clifton, I.J., Baldwin, J.E. and Schofield, C.J. Kinetic and crystallographic studies on deacetoxycephalosporin C synthase (DAOCS). J. Mol. Biol. 308 (2001) 937-948. [PMID: 11352583]
3. Yeh, W.K., Ghag, S.K. and Queener, S.W. Enzymes for epimerization of isopenicillin N, ring expansion of penicillin N, and 3'-hydroxylation of deacetoxycephalosporin C. Function, evolution, refolding, and enzyme engineering. Ann. N.Y. Acad. Sci. 672 (1992) 396-408.
4. Valegård, K., van Scheltinga, A.C.T., Lloyd, M.D., Hara, T., Ramaswamy, S., Perrakis, A., Thompson, A., Lee, H.-J., Baldwin, J.E., Schofield, C.J., Hajdu, J. and Andersson, I. Structure of a cephalosporin synthase. Nature 394 (1998) 805-809. [PMID: 9723623]
5. Dotzlaf, J.E. and Yeh, W.K. Purification and properties of deacetoxycephalosporin C synthase from recombinant Escherichia coli and its comparison with the native enzyme purified from Streptomyces clavuligerus. J. Biol. Chem. 264 (1989) 10219-10227. [PMID: 2656705]
Accepted name: 2,4-dihydroxy-1,4-benzoxazin-3-one-glucoside dioxygenase
Reaction: (2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside + 2-oxoglutarate + O2 = (2R)-4,7-dihydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside + succinate + CO2 + H2O
For diagram of reaction click here.
Glossary: (2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside = DIBOA β-D-glucoside
(2R)-4,7-dihydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside = TRIBOA β-D-glucoside
Other name(s): BX6 (gene name); DIBOA-Glc dioxygenase
Systematic name: (2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside:oxygen oxidoreductase (7-hydroxylating)
Comments: The enzyme is involved in the biosynthesis of protective and allelophatic benzoxazinoids in some plants, most commonly from the family of Poaceae (grasses).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Jonczyk, R., Schmidt, H., Osterrieder, A., Fiesselmann, A., Schullehner, K., Haslbeck, M., Sicker, D., Hofmann, D., Yalpani, N., Simmons, C., Frey, M. and Gierl, A. Elucidation of the final reactions of DIMBOA-glucoside biosynthesis in maize: characterization of Bx6 and Bx7. Plant Physiol. 146 (2008) 1053-1063. [PMID: 18192444]
Accepted name: (S)-stylopine synthase
Reaction: (S)-cheilanthifoline + NADPH + H+ + O2 = (S)-stylopine + NADP+ + 2 H2O
For diagram click here.
Other name(s): (S)-cheilanthifoline oxidase (methylenedioxy-bridge-forming)
Systematic name: (S)-cheilanthifoline,NADPH:oxygen oxidoreductase (methylenedioxy-bridge-forming)
Comments: A heme-thiolate enzyme (P-450) catalysing an oxidative reaction that does not incorporate oxygen into the product. Forms the second methylenedioxy bridge of the protoberberine alkaloid stylopine from oxidative ring closure of adjacent phenolic and methoxy groups of cheilanthifoline.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 138791-29-4
References:
1. Bauer, W. and Zenk, M.H. Two methylenedioxy bridge-forming cytochrome P-450 dependent enzymes are involved in (S)-stylopine biosynthesis. Phytochemistry 30 (1991) 2953-2961.
Accepted name: (S)-cheilanthifoline synthase
Reaction: (S)-scoulerine + NADPH + H+ + O2 = (S)-cheilanthifoline + NADP+ + 2 H2O
For diagram click here.
Other name(s): (S)-scoulerine oxidase (methylenedioxy-bridge-forming)
Systematic name: (S)-scoulerine,NADPH:oxygen oxidoreductase (methylenedioxy-bridge-forming)
Comments: A heme-thiolate enzyme (P-450) catalysing an oxidative reaction that does not incorporate oxygen into the product. Forms the methylenedioxy bridge of the protoberberine alkaloid cheilanthifoline from oxidative ring closure of adjacent phenolic and methoxy groups of scoulerine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 138791-27-2
References:
1. Bauer, W. and Zenk, M.H. Two methylenedioxy bridge-forming cytochrome P-450 dependent enzymes are involved in (S)-stylopine biosynthesis. Phytochemistry 30 (1991) 2953-2961.
Accepted name: berbamunine synthase
Reaction: (S)-N-methylcoclaurine + (R)-N-methylcoclaurine + NADPH + H+ + O2 = berbamunine + NADP+ + 2 H2O
For diagram click here.
Other name(s): (S)-N-methylcoclaurine oxidase (C-O phenol-coupling)
Systematic name: (S)-N-methylcoclaurine,NADPH:oxygen oxidoreductase (C-O phenol-coupling)
Comments: A heme-thiolate enzyme (P-450). Forms the bisbenzylisoquinoline alkaloid berbamunine by phenol oxidation of N-methylcoclaurine without the incorporation of oxygen into the product. Reaction of two molecules of (R)-N-methylcoclaurine gives the dimer guattagaumerine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 144941-42-4
References:
1. Stadler, R. and Zenk, M.H. The purification and characterization of a unique cytochrome P-450 enzyme from Berberis stolifera plant cell cultures. J. Biol. Chem. 268 (1993) 823-831. [PMID: 8380416]
Accepted name: salutaridine synthase
Reaction: (R)-reticuline + NADPH + H+ + O2 = salutaridine + NADP+ + 2 H2O
For diagram click here.
Other name(s): (R)-reticuline oxidase (C-C phenol-coupling)
Systematic name: (R)-reticuline,NADPH:oxygen oxidoreductase (C-C phenol-coupling)
Comments: A heme-thiolate enzyme (P-450). Forms the morphinan alkaloid salutaridine by intramolecular phenol oxidation of reticuline without the incorporation of oxygen into the product.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 149433-84-1
References:
1. Gerady, R. and Zenk, M.H. Formation of salutaridine from (R)-reticuline by a membrane-bound cytochrome P-450 enzyme from Papaver somniferum. Phytochemistry 32 (1993) 79-86.
Accepted name: (S)-canadine synthase
Reaction: (S)-tetrahydrocolumbamine + NADPH + H+ + O2 = (S)-canadine + NADP+ + 2 H2O
For diagram click here.
Other name(s): (S)-tetrahydroberberine synthase; (S)-tetrahydrocolumbamine oxidase (methylenedioxy-bridge-forming)
Systematic name: (S)-tetrahydrocolumbamine,NADPH:oxygen oxidoreductase (methylenedioxy-bridge-forming)
Comments: A heme-thiolate enzyme (P-450) catalysing an oxidative reaction that does not incorporate oxygen into the product. Oxidation of the methoxyphenol group of the alkaloid tetrahydrocolumbamine results in the formation of the methylenedioxy bridge of canadine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 114308-22-4
References:
1. Rueffer, M. and Zenk, M.H. Canadine synthase from Thalictrum tuberosum cell cultures catalyses the formation of the methylenedioxy bridge in berberine synthesis. Phytochemistry 36 (1994) 1219-1223.
Accepted name: lathosterol oxidase
Reaction: 5α-cholest-7-en-3β-ol + NAD(P)H + H+ + O2 = cholesta-5,7-dien-3β-ol + NAD(P)+ + 2 H2O
For diagram click here.
Glossary: lathosterol = 5α-cholest-7-en-3β-ol
7-dehydrocholesterol = cholesta-5,7-dien-3β-ol
Other name(s): Δ7-sterol Δ5-dehydrogenase; Δ7-sterol 5-desaturase; Δ7-sterol-C5(6)-desaturase; 5-DES
Systematic name: 5α-cholest-7-en-3β-ol, NAD(P)H:oxygen 5-oxidoreductase
Comments: This enzyme catalyses the introduction of a C5 double bond into the B ring of Δ7-sterols to yield the corresponding Δ5,7-sterols in mammals, yeast and plants [4]. Forms part of the plant sterol biosynthesis pathway.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37255-37-1
References:
1. Dempsey, M.E., Seaton, J.D., Schroepfer, G.J. and Trockman, R.W. The intermediary role of Δ5,7-cholestadien-3β-ol in cholesterol biosynthesis. J. Biol. Chem. 239 (1964) 1381-1387. [PMID: 14189869]
2. Nishino, H., Nakaya, J., Nishi, S., Kurosawa, T. and Ishibashi, T. Temperature-induced differential kinetic properties between an initial burst and the following steady state in membrane-bound enzymes: studies on lathosterol 5-desaturase. Arch. Biochem. Biophys. 339 (1997) 298-304. [PMID: 9056262]
3. Taton, M. and Rahier, A. Plant sterol biosynthesis: identification and characterization of higher plant Δ7-sterol C5(6)-desaturase. Arch. Biochem. Biophys. 325 (1996) 279-288. [PMID: 8561508]
4. Taton, M., Husselstein, T., Benveniste, P. and Rahier, A. Role of highly conserved residues in the reaction catalyzed by recombinant Δ7-sterol-C5(6)-desaturase studied by site-directed mutagenesis. Biochemistry 39 (2000) 701-711. [PMID: 10651635]
Accepted name: biflaviolin synthase
Reaction: (1) 2 flaviolin + NADPH + H+ + O2 = 3,3'-biflaviolin + NADP+ + 2 H2O
(2) 2 flaviolin + NADPH + H+ + O2 = 3,8'-biflaviolin + NADP+ + 2 H2O
Glossary: flaviolin = 4,5,7-trihydroxynaphthalene-1,2-dione
3,3'-biflaviolin = 3,3',6,6',8,8'-hexahydroxy-2,2'-binaphthalene-1,1',4,4'-tetraone
3,8'-biflaviolin = 2,3',4,6',7,8'-hexahydroxy-1,2'-binaphthalene-1',4',5,8-tetraone
Other name(s): CYP158A2; CYP 158A2; cytochrome P450 158A2
Systematic name: flaviolin,NADPH:oxygen oxidoreductase
Comments: This cytochrome-P450 enzyme, from the soil-dwelling bacterium Streptomyces coelicolor A3(2), catalyses a phenol oxidation C-C coupling reaction, which results in the polymerization of flaviolin to form biflaviolin or triflaviolin without the incorporation of oxygen into the product [1,3]. The products are highly conjugated pigments that protect the bacterium from the deleterious effects of UV irradiation [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Zhao, B., Guengerich, F.P., Bellamine, A., Lamb, D.C., Izumikawa, M., Lei, L., Podust, L.M., Sundaramoorthy, M., Kalaitzis, J.A., Reddy, L.M., Kelly, S.L., Moore, B.S., Stec, D., Voehler, M., Falck, J.R., Shimada, T. and Waterman, M.R. Binding of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450 158A2. J. Biol. Chem. 280 (2005) 11599-11607. [PMID: 15659395]
2. Zhao, B., Guengerich, F.P., Voehler, M. and Waterman, M.R. Role of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer. J. Biol. Chem. 280 (2005) 42188-42197. [PMID: 16239228]
3. Zhao, B., Lamb, D.C., Lei, L., Kelly, S.L., Yuan, H., Hachey, D.L. and Waterman, M.R. Different binding modes of two flaviolin substrate molecules in cytochrome P450 158A1 (CYP158A1) compared to CYP158A2. Biochemistry 46 (2007) 8725-8733. [PMID: 17614370]
Accepted name: pseudobaptigenin synthase
Reaction: (1) calycosin + NADPH + H+ + O2 = pseudobaptigenin + NADP+ + 2 H2O
(2) pratensein + NADPH + H+ + O2 = 5-hydroxypseudobaptigenin + NADP+ + 2 H2O
Glossary: calycosin = 3'-hydroxyformononetin
pratensein = 3'-hydroxybiochanin A
Systematic name: calycosin,NADPH:oxygen oxidoreductase (methylenedioxy-bridge-forming)
Comments: A heme-thiolate enzyme (P450) catalysing an oxidative reaction that does not incorporate oxygen into the product. Catalyses a step in the biosynthesis of (–)-maackiain, the main pterocarpan phytoalexin in chickpea (Cicer arietinum).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Clemens S., Barz W. Cytochrome P450-dependent methylenedioxy bridge formation in Cicer arietinum. Phytochemistry 41 (1996) 457-460.