Continued from EC 1.1.1.301 to 346
EC 1.1.2 With a cytochrome as acceptor
EC 1.1.3 With oxygen as acceptor
EC 1.1.2.6 polyvinyl alcohol dehydrogenase (cytochrome)
EC 1.1.2.7 methanol dehydrogenase (cytochrome c)
EC 1.1.2.8 alcohol dehydrogenase (cytochrome c)
Accepted name: mannitol dehydrogenase (cytochrome)
Reaction: D-mannitol + ferricytochrome c = D-fructose + ferrocytochrome c
Other name(s): polyol dehydrogenase
Systematic name: D-mannitol:ferricytochrome-c 2-oxidoreductase
Comments: Acts on polyols with a D-lyxo configuration, such as D-mannitol and D-sorbitol.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37250-78-5
References:
1 Arcus, A.C. and Edson, N.L. Polyol dehydrogenases. 2. The polyol dehydrogenases of Acetobacter suboxydans and Candida utilis. Biochem. J. 64 (1956) 385-394.
2. Cho, N.C., Kim, K. and Jhon, D.Y. Purification and characterization of polyol dehydrogenase from Gluconobacter melanogenus. Han'guk Saenghwa Hakhaochi 23 (1990) 172-178.
Accepted name: L-lactate dehydrogenase (cytochrome)
Reaction: (S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H+
Other name(s): lactic acid dehydrogenase; cytochrome b2 (flavin-free derivative of flavocytochrome b2); flavocytochrome b2; L-lactate cytochrome c reductase; L(+)-lactate:cytochrome c oxidoreductase; dehydrogenase, lactate (cytochrome); L-lactate cytochrome c oxidoreductase; lactate dehydrogenase (cytochrome); lactic cytochrome c reductase
Systematic name: (S)-lactate:ferricytochrome-c 2-oxidoreductase
Comments: Identical with cytochrome b2; a flavohemoprotein (FMN).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9078-32-4
References:
1. Appleby, C.A. and Morton, R.K. Lactic dehydrogenase and cytochrome b2 of baker's yeast. Purification and crystallization. Biochem. J. 71 (1959) 492–499. [PMID: 13638255]
2. Appleby, C.A. and Morton, R.K. Lactic dehydrogenase and cytochrome b2 of baker's yeast. Enzymic and chemical properties of the crystalline enzyme. Biochem. J. 73 (1959) 539–550. [PMID: 13793977]
3. Bach, S.G., Dixon, M. and Zerfas, L.G. Yeast lactic dehydrogenase and cytochrome b2. Biochem. J. 40 (1946) 229–239. [PMID: 16747991]
4. Nygaard, A.P. Lactate dehydrogenases of yeast. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol.7, Academic Press, New York, 1963, p. 557-565.
Accepted name: D-lactate dehydrogenase (cytochrome)
Reaction: (R)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c
Other name(s): lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(–)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(–)-lactic cytochrome c reductase
Systematic name: (R)-lactate:ferricytochrome-c 2-oxidoreductase
Comments: A flavoprotein (FAD).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37250-79-6
References:
1. Gregolin, C. and Singer, T.P. The lactate dehydrogenase of yeast. III. D-(–)-Lactate cytochrome c reductase, a zinc-flavoprotein from aerobic yeast. Biochim. Biophys. Acta 67 (1963) 201-218.
2. Gregolin, C., Singer, T.P., Kearney, E.B. and Boeri, E. The formation and enzymatic properties of the various lactic dehydrogenases of yeast. Ann. N.Y. Acad. Sci. 94 (1961) 780-797.
3. Nygaard, A.P. D(–)-Lactate cytochrome c reductase, a flavoprotein from yeast. J. Biol. Chem. 236 (1961) 920-925.
4. Nygaard, A.P. Lactate dehydrogenases of yeast. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 557-565.
Accepted name: D-lactate dehydrogenase (cytochrome c-553)
Reaction: (R)-lactate + 2 ferricytochrome c-553 = pyruvate + 2 ferrocytochrome c-553
Systematic name: (R)-lactate:ferricytochrome-c-553 2-oxidoreductase
Comments: From Desulfovibrio vulgaris.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37250-79-6
References:
1. Ogata, M., Arihara, K. and Yagi, T. D-Lactate dehydrogenase of Desulfovibrio vulgaris. J. Biochem. (Tokyo) 89 (1981) 1423-1431. [PMID: 7275946]
Accepted name: polyvinyl alcohol dehydrogenase (cytochrome)
Reaction: polyvinyl alcohol + ferricytochrome c = oxidized polyvinyl alcohol + ferrocytochrome c + H+
Other name(s): PVA dehydrogenase; PVADH
Systematic name: polyvinyl alcohol:ferricytochrome-c oxidoreductase
Comments: A quinoprotein. The enzyme is involved in bacterial polyvinyl alcohol degradation. Some Gram-negative bacteria degrade polyvinyl alcohol by importing it into the periplasmic space, where it is oxidized by polyvinyl alcohol dehydrogenase, an enzyme that is coupled to the respiratory chain via cytochrome c. The enzyme contains a pyrroloquinoline quinone cofactor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Shimao, M., Ninomiya, K., Kuno, O., Kato, N. and Sakazawa, C. Existence of a novel enzyme, pyrroloquinoline quinone-dependent polyvinyl alcohol dehydrogenase, in a bacterial symbiont, Pseudomonas sp. strain VM15C. Appl. Environ. Microbiol. 51 (1986) 268. [PMID: 3513704]
2. Shimao, M., Onishi, S., Kato, N. and Sakazawa, C. Pyrroloquinoline quinone-dependent cytochrome reduction in polyvinyl alcohol-degrading Pseudomonas sp strain VM15C. Appl. Environ. Microbiol. 55 (1989) 275-278. [PMID: 16347841]
3. Mamoto, R., Hu, X., Chiue, H., Fujioka, Y. and Kawai, F. Cloning and expression of soluble cytochrome c and its role in polyvinyl alcohol degradation by polyvinyl alcohol-utilizing Sphingopyxis sp. strain 113P3. J. Biosci. Bioeng. 105 (2008) 147-151. [PMID: 18343342]
4. Hirota-Mamoto, R., Nagai, R., Tachibana, S., Yasuda, M., Tani, A., Kimbara, K. and Kawai, F. Cloning and expression of the gene for periplasmic poly(vinyl alcohol) dehydrogenase from Sphingomonas sp. strain 113P3, a novel-type quinohaemoprotein alcohol dehydrogenase. Microbiology 152 (2006) 1941-1949. [PMID: 16804170]
5. Hu, X., Mamoto, R., Fujioka, Y., Tani, A., Kimbara, K. and Kawai, F. The pva operon is located on the megaplasmid of Sphingopyxis sp. strain 113P3 and is constitutively expressed, although expression is enhanced by PVA. Appl. Microbiol. Biotechnol. 78 (2008) 685-693. [PMID: 18214469]
6. Kawai, F. and Hu, X. Biochemistry of microbial polyvinyl alcohol degradation. Appl. Microbiol. Biotechnol. 84 (2009) 227-237. [PMID: 19590867]
Accepted name: methanol dehydrogenase (cytochrome c)
Reaction: a primary alcohol + 2 cytochrome cL = an aldehyde + 2 reduced cytochrome cL
Other name(s): methanol dehydrogenase; MDH
Systematic name: methanol:cytochrome c oxidoreductase
Comments: A periplasmic quinoprotein alcohol dehydrogenase that only occurs in methylotrophic bacteria. It uses the novel specific cytochrome cL as acceptor. Acts on a wide range of primary alcohols, including ethanol, duodecanol, chloroethanol, cinnamyl alcohol, and also formaldehyde. Activity is stimulated by ammonia or methylamine. It is usually assayed with phenazine methosulphate. Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulphide ring structure in close proximity to the PQQ. It differs from EC 1.1.2.8, alcohol dehydrogenase (cytochrome c), in having a high affinity for methanol and in having a second essential small subunit (no known function).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Anthony, C. and Zatman, L.J. The microbial oxidation of methanol. 2. The methanol-oxidizing enzyme of Pseudomonas sp. M 27. Biochem. J. 92 (1964) 614-621. [PMID: 4378696]
2. Anthony, C. and Zatman, L.J. The microbial oxidation of methanol. The prosthetic group of the alcohol dehydrogenase of Pseudomonas sp. M27: a new oxidoreductase prosthetic group. Biochem. J. 104 (1967) 960-969. [PMID: 6049934]
3. Duine, J.A., Frank, J. and Verweil, P.E.J. Structure and activity of the prosthetic group of methanol dehydrogenase. Eur. J. Biochem. 108 (1980) 187-192. [PMID: 6250827]
4. Salisbury, S.A., Forrest, H.S., Cruse, W.B.T. and Kennard, O. A novel coenzyme from bacterial primary alcohol dehydrogenases. Nature (Lond.) 280 (1979) 843-844. [PMID: 471057]
5. Cox, J.M., Day, D.J. and Anthony, C. The interaction of methanol dehydrogenase and its electron acceptor, cytochrome cL in methylotrophic bacteria . Biochim. Biophys. Acta 1119 (1992) 97-106. [PMID: 1311606]
6. Blake, C.C., Ghosh, M., Harlos, K., Avezoux, A. and Anthony, C. The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues. Nat. Struct. Biol. 1 (1994) 102-105. [PMID: 7656012]
7. Xia, Z.X., He, Y.N., Dai, W.W., White, S.A., Boyd, G.D. and Mathews, F.S. Detailed active site configuration of a new crystal form of methanol dehydrogenase from Methylophilus W3A1 at 1.9 Å resolution. Biochemistry 38 (1999) 1214-1220. [PMID: 9930981]
8. Afolabi, P.R., Mohammed, F., Amaratunga, K., Majekodunmi, O., Dales, S.L., Gill, R., Thompson, D., Cooper, J.B., Wood, S.P., Goodwin, P.M. and Anthony, C. Site-directed mutagenesis and X-ray crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome c(L). Biochemistry 40 (2001) 9799-9809. [PMID: 11502173]
9. Anthony, C. and Williams, P. The structure and mechanism of methanol dehydrogenase. Biochim. Biophys. Acta 1647 (2003) 18-23. [PMID: 12686102]
10. Williams, P.A., Coates, L., Mohammed, F., Gill, R., Erskine, P.T., Coker, A., Wood, S.P., Anthony, C. and Cooper, J.B. The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens. Acta Crystallogr. D Biol. Crystallogr. 61 (2005) 75-79. [PMID: 15608378]
Accepted name: alcohol dehydrogenase (cytochrome c)
Reaction: a primary alcohol + 2 cytochrome c = an aldehyde + 2 reduced cytochrome c
Other name(s): type I quinoprotein alcohol dehydrogenase; quinoprotein ethanol dehydrogenase
Systematic name: alcohol:cytochrome c oxidoreductase
Comments: A periplasmic PQQ-containing quinoprotein. Occurs in Pseudomonas and Rhodopseudomonas. The enzyme from Pseudomonas aeruginosa uses a specific inducible cytochrome c550 as electron acceptor. Acts on a wide range of primary and secondary alcohols, but not methanol. It has a homodimeric structure [contrasting with the heterotetrameric structure of EC 1.1.2.7, methanol dehydrogenase (cytochrome c)]. It is routinely assayed with phenazine methosulphate as electron acceptor. Activity is stimulated by ammonia or amines. Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulphide ring structure in close proximity to the PQQ.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Rupp, M. and Gorisch, H. Purification, crystallisation and characterization of quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa. Biol. Chem. Hoppe-Seyler 369 (1988) 431-439. [PMID: 3144289]
2. Toyama, H., Fujii, A., Matsushita, K., Shinagawa, E., Ameyama, M. and Adachi, O. Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols. J. Bacteriol. 177 (1995) 2442-2450. [PMID: 7730276]
3. Schobert, M. and Gorisch, H. Cytochrome c550 is an essential component of the quinoprotein ethanol oxidation system in Pseudomonas aeruginosa: cloning and sequencing of the genes encoding cytochrome c550 and an adjacent acetaldehyde dehydrogenase. Microbiology 145 (1999) 471-481. [PMID: 10075429]
4. Keitel, T., Diehl, A., Knaute, T., Stezowski, J.J., Hohne, W. and Gorisch, H. X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: basis of substrate specificity. J. Mol. Biol. 297 (2000) 961-974. [PMID: 10736230]
5. Kay, C.W., Mennenga, B., Gorisch, H. and Bittl, R. Characterisation of the PQQ cofactor radical in quinoprotein ethanol dehydrogenase of Pseudomonas aeruginosa by electron paramagnetic resonance spectroscopy. FEBS Lett. 564 (2004) 69-72. [PMID: 15094044]
6. Mennenga, B., Kay, C.W. and Gorisch, H. Quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: the unusual disulfide ring formed by adjacent cysteine residues is essential for efficient electron transfer to cytochrome c550. Arch. Microbiol. 191 (2009) 361-367. [PMID: 19224199]
[EC 1.1.3.2 Transferred entry: now EC 1.13.12.4 lactate 2-monooxygenase (EC 1.1.3.2 created 1961, deleted 1972)]
Accepted name: malate oxidase
Reaction: (S)-malate + O2 = oxaloacetate + H2O2
Other name(s): FAD-dependent malate oxidase; malic oxidase; malic dehydrogenase II
Systematic name: (S)-malate:oxygen oxidoreductase
Comments: A flavoprotein (FAD).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9028-73-3
References:
1. Cohn, D.V. The enzymatic formation of oxalacetic acid by nonpyridine nucleotide malic dehydrogenase of Micrococcus lysodeikticus. J. Biol. Chem. 233 (1958) 299-304.
2. Narindrasorasak, S., Goldie, A.H. and Sanwal, B.D. Characteristics and regulation of a phospholipid-activated malate oxidase from Escherichia coli. J. Biol. Chem. 254 (1979) 1540-1545. [PMID: 368072]
Accepted name: glucose oxidase
Reaction: β-D-glucose + O2 = D-glucono-1,5-lactone + H2O2
Other name(s): glucose oxyhydrase; corylophyline; penatin; glucose aerodehydrogenase; microcid; β-D-glucose oxidase; D-glucose oxidase; D-glucose-1-oxidase; β-D-glucose:quinone oxidoreductase; glucose oxyhydrase; deoxin-1; GOD
Systematic name: β-D-glucose:oxygen 1-oxidoreductase
Comments: A flavoprotein (FAD).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9001-37-0
References:
1. Bentley, R. Glucose oxidase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol.7, Academic Press, New York, 1963, p. 567-586.
2. Coulthard, C.E., Michaelis, R., Short, W.F., Sykes, G., Skrimshire, G.E.H., Standfast, A.F.B., Birkinshaw, J.H. and Raistick, H. Notatin: an anti-bacterial glucose-aerodehydrogenase from Penicillium notatum Westling and Penicillium resticulosum sp. nov. Biochem. J. 39 (1945) 24-36.
3. Keilin, D. and Hartree, E.F. Properties of glucose oxidase (notatin). Biochem. J. 42 (1948) 221-229.
4. Keilin, D. and Hartree, E.F. Specificity of glucose oxidase (notatin). Biochem. J. 50 (1952) 331-341.
Accepted name: hexose oxidase
Reaction: D-glucose + O2 = D-glucono-1,5-lactone + H2O2
Systematic name: D-hexose:oxygen 1-oxidoreductase
Comments: A copper glycoprotein. Also oxidizes D-galactose, D-mannose, maltose, lactose and cellobiose.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9028-75-5
References:
1. Bean, R.C. and Hassid, W.Z. Carbohydrate oxidase from a red alga Iridophycus flaccidum. J. Biol. Chem. 218 (1956) 425-436. [PMID: 13278350]
2. Bean, R.C., Porter, G.G. and Steinberg, B.M. Carbohydrate metabolism of citrus fruit. II. Oxidation of sugars by an aerodehydrogenase from young orange fruit. J. Biol. Chem. 236 (1961) 1235-1240. [PMID: 13688220]
3. Sullivan, J.D. and Ikawa, M. Purification and characterization of hexose oxidase from the red alga Chondrus crispus. Biochim. Biophys. Acta 309 (1973) 11-22. [PMID: 4708670]
Accepted name: cholesterol oxidase
Reaction: cholesterol + O2 = cholest-5-en-3-one + H2O2
For diagram of reaction click here
Other name(s): cholesterol- O2 oxidoreductase; 3β-hydroxy steroid oxidoreductase; 3β-hydroxysteroid:oxygen oxidoreductase
Systematic name: cholesterol:oxygen oxidoreductase
Comments: Contains flavin adenine dinucleotide (FAD). Cholesterol oxidases are secreted bacterial bifunctional enzymes that catalyse the first two steps in the degradation of cholesterol. The enzyme catalyses the oxidation of the 3β-hydroxyl group to a keto group, and the isomerization of the double bond in the oxidized steroid ring system from the Δ5 position to Δ6 position (cf. EC 5.3.3.1, steroid Δ-isomerase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9028-76-6
References:
1. Richmond, W. Preparation and properties of a cholesterol oxidase from Nocardia sp. and its application to the enzymatic assay of total cholesterol in serum. Clin. Chem. 19 (1973) 1350-1356. [PMID: 4757363]
2. Stadtman, T.C., Cherkes, A. and Anfinsen, C.B. Studies on the microbiological degradation of cholesterol. J. Biol. Chem. 206 (1954) 511-523. [PMID: 13143010]
3. MacLachlan, J., Wotherspoon, A.T., Ansell, R.O. and Brooks, C.J. Cholesterol oxidase: sources, physical properties and analytical applications. J. Steroid Biochem. Mol. Biol. 72 (2000) 169-195. [PMID: 10822008]
4. Vrielink, A. Cholesterol oxidase: structure and function. Subcell. Biochem. 51 (2010) 137-158. [PMID: 20213543]
Accepted name: aryl-alcohol oxidase
Reaction: an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2
Other name(s): aryl alcohol oxidase; veratryl alcohol oxidase; arom. alcohol oxidase
Systematic name: aryl-alcohol:oxygen oxidoreductase
Comments: Oxidizes many primary alcohols containing an aromatic ring; best substrates are (2-naphthyl)methanol and 3-methoxybenzyl alcohol.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9028-77-7
References:
1. Farmer, V.C., Henderson, M.E.K. and Russell, J.D. Aromatic-alcohol-oxidase activity in the growth medium of Polystictus versicolor. Biochem. J. 74 (1960) 257-262.
Accepted name: L-gulonolactone oxidase
Reaction: L-gulono-1,4-lactone + O2 = L-ascorbate + H2O2 (overall reaction)
(1a) L-gulono-1,4-lactone + O2 = L-xylo-hex-2-ulono-1,4-lactone + H2O2
(1b) L-xylo-hex-2-ulono-1,4-lactone = L-ascorbate (spontaneous)
For diagram click here.
Other name(s): L-gulono-γ-lactone: O2 oxidoreductase; L-gulono-γ-lactone oxidase; L-gulono-γ-lactone:oxidoreductase; GLO
Systematic name: L-gulono-1,4-lactone:oxygen 3-oxidoreductase
Comments: A microsomal flavoprotein (FAD). The product spontaneously isomerizes to L-ascorbate. While most higher animals can synthesize asborbic acid, primates and guinea pigs cannot [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9028-78-8
References:
1. Isherwood, F.A., Mapson, L.W. and Chen, Y.T. Synthesis of L-ascorbic acid in rat liver homogenates. Conversion of L-gulono- and L-galactono-γ-lactone and the respective acids into L-ascorbic acid. Biochem. J. 76 (1960) 157-171. [PMID: 14405898]
2. Kiuchi, K., Noshikimi, M. and Yagi, K. Purification and characterization of L-gulonolactone oxidase from chicken kidney microsomes. Biochemistry 21 (1982) 5076-5082. [PMID: 7138847]
3. Nishikimi, M., Fukuyama, R., Minoshima, S., Shimizu, N. and Yagi, K. Cloning and chromosomal mapping of the human nonfunctional gene for L-gulono-γ-lactone oxidase, the enzyme for L-ascorbic acid biosynthesis missing in man. J. Biol. Chem. 269 (1994) 13685-13688. [PMID: 8175804]
4. Chatterjee, I.B., Chatterjee, G.C., Ghosh, N.C. and Guha, B.C. Identification of 2-keto-L-gulonolactone as an intermediate in the biosynthesis of L-ascorbic acid. Naturwissenschaften 46 (1959) 475 only.
Accepted name: galactose oxidase
Reaction: D-galactose + O2 = D-galacto-hexodialdose + H2O2
Other name(s): D-galactose oxidase; β-galactose oxidase
Systematic name: D-galactose:oxygen 6-oxidoreductase
Comments: A copper protein.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9028-79-9
References:
1. Avigad, G., Amaral, D., Asensio, C. and Horecker, B.L. The D-galactose oxidase of Polyporus circinatus. J. Biol. Chem. 237 (1962) 2736-2743.
Accepted name: pyranose oxidase
Reaction: D-glucose + O2 = 2-dehydro-D-glucose + H2O2
Other name(s): glucose 2-oxidase; pyranose-2-oxidase
Systematic name: pyranose:oxygen 2-oxidoreductase
Comments: A flavoprotein (FAD). Also oxidizes D-xylose, L-sorbose and D-glucono-1,5-lactone, which have the same ring conformation and configuration at C-2, C-3 and C-4.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37250-80-9
References:
1. Janssen, F.W. and Ruelius, H.W. Carbohydrate oxidase, a novel enzyme from Polyporus obtusus. II. Specificity and characterization of reaction products. Biochim. Biophys. Acta 167 (1968) 501-510. [PMID: 5722278]
2. Machida, Y. and Nakanishi, T. Purification and properties of pyranose oxidase from Coriolus versicolor. Agric. Biol. Chem. 48 (1984) 2463-2470.
3. Neidleman, S.L., Amon, W.F., Jr. and Geigert, J. Process for the production of fructose. Patent US4246347, 1981. Chem. Abstr. 94 (1981) 207379. (PDF)
4. Ruelius, H.W., Kerwin, R.M. and Janssen, F.W. Carbohydrate oxidase, a novel enzyme from Polyporus obtusus. I. Isolation and purification. Biochim. Biophys. Acta 167 (1968) 493-500. [PMID: 5725162]
Accepted name: L-sorbose oxidase
Reaction: L-sorbose + O2 = 5-dehydro-D-fructose + H2O2
Systematic name: L-sorbose:oxygen 5-oxidoreductase
Comments: Also acts on D-glucose, D-galactose and D-xylose, but not on D-fructose. 2,6-Dichloroindophenol can act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37250-81-0
References:
1. Yamada, Y., Iizuka, K., Aida, K. and Uemura, T. Enzymatic studies on the oxidation of sugar and sugar alcohol. 3. Purification and properties of L-sorbose oxidase from Trametes sanguinea. J. Biochem. (Tokyo) 62 (1967) 223-229. [PMID: 5586487]
Accepted name: pyridoxine 4-oxidase
Reaction: pyridoxine + O2 = pyridoxal + H2O2
Other name(s): pyridoxin 4-oxidase; pyridoxol 4-oxidase
Systematic name: pyridoxine:oxygen 4-oxidoreductase
Comments: A flavoprotein. Can also use 2,6-dichloroindophenol as an acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 37250-82-1
References:
1. Sundaram, T.K. and Snell, E.E. The bacterial oxidation of vitamin B6. V. The enzymatic formation of pyridoxal and isopyridoxal from pyridoxine. J. Biol. Chem. 244 (1969) 2577-2584. [PMID: 5769992]
Accepted name: alcohol oxidase
Reaction: a primary alcohol + O2 = an aldehyde + H2O2
Other name(s): ethanol oxidase
Systematic name: alcohol:oxygen oxidoreductase
Comments: A flavoprotein (FAD); acts on lower primary alcohols and unsaturated alcohols but branched-chain and secondary alcohols are not attacked.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9073-63-6
References:
1. Janssen, F.W. and Ruelius, H.W. Alcohol oxidase, a flavoprotein from several Basidiomycetes species. Crystallization by fractional precipitation with polyethylene glycol. Biochim. Biophys. Acta 151 (1968) 330-342. [PMID: 5636370]
2. Nishida, A., Ishihara, T. and Hiroi, T. [Studies on enzymes related to lignan biodegradation.] Baiomasu Henkan Keikaku Kenkyu Hokoku (1987) 38-59. (in Japanese)
3. Suye, S. Purification and properties of alcohol oxidase from Candida methanosorbosa M-2003. Curr. Microbiol. 34 (1997) 374-377. [PMID: 9142745]
Accepted name: catechol oxidase (dimerizing)
Reaction: 4 catechol + 3 O2 = 2 dibenzo[1,4]dioxin-2,3-dione + 6 H2O
For diagram click here.
Systematic name: catechol:oxygen oxidoreductase (dimerizing)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37250-83-2
References:
1. Nair, P.M. and Vining, L.C. Enzymic oxidation of catechol to diphenylenedioxide-2,3-quinone. Arch. Biochem. Biophys. 106 (1964) 422-427.
Accepted name: (S)-2-hydroxy-acid oxidase
Reaction: an (S)-2-hydroxy carboxylate + O2 = a 2-oxo carboxylate + H2O2
Other name(s): glycolate oxidase; hydroxy-acid oxidase A; hydroxy-acid oxidase B; glycolate oxidase; oxidase, L-2-hydroxy acid; hydroxyacid oxidase A; L-α-hydroxy acid oxidase; L-2-hydroxy acid oxidase
Systematic name: (S)-2-hydroxy-acid:oxygen 2-oxidoreductase
Comments: A flavoprotein (FMN). Exists as two major isoenzymes; the A form preferentially oxidizes short-chain aliphatic hydroxy acids, and was previously listed as EC 1.1.3.1, glycolate oxidase; the B form preferentially oxidizes long-chain and aromatic hydroxy acids. The rat isoenzyme B also acts as EC 1.4.3.2, L-amino-acid oxidase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9028-71-1
References:
1. Blanchard, M., Green, D.E., Nocito-Carroll, V. and Ratner, S. l-Hydroxy acid oxidase. J. Biol. Chem. 163 (1946) 137-144.
2. Frigerio, N.A. and Harbury, H.A. Preparation and some properties of crystalline glycolic acid oxidase of spinach. J. Biol. Chem. 231 (1958) 135-157.
3. Kun, E., Dechary, J.M. and Pitot, H.C. The oxidation of glycolic acid by a liver enzyme. J. Biol. Chem. 210 (1954) 269-280.
4. Nakano, M. and Danowski, T.S. Crystalline mammalian L-amino acid oxidase from rat kidney mitochondria. J. Biol. Chem. 241 (1966) 2075-2083. [PMID: 5946631]
5. Nakano, M., Ushijima, Y., Saga, M., Tsutsumi, Y. and Asami, H. Aliphatic L-α-hydroxyacid oxidase from rat livers: purification and properties. Biochim. Biophys. Acta 167 (1968) 9-22. [PMID: 5686300]
6. Phillips, D.R., Duley, J.A., Fennell, D.J. and Holmes, R.S. The self-association of L-alpha hydroxyacid oxidase. Biochim. Biophys. Acta 427 (1976) 679-687. [PMID: 1268224]
7. Schuman, M. and Massey, V. Purification and characterization of glycolic acid oxidase from pig liver. Biochim. Biophys. Acta 227 (1971) 500-520. [PMID: 5569122]
8. Jones, J.M., Morrell, J.C. and Gould, S.J. Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases. J. Biol. Chem. 275 (2000) 12590-12597. [PMID: 10777549]
Accepted name: ecdysone oxidase
Reaction: ecdysone + O2 = 3-dehydroecdysone + H2O2
Other name(s): β-ecdysone oxidase
Systematic name: ecdysone:oxygen 3-oxidoreductase
Comments: 2,6-Dichloroindophenol can act as an acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 56803-12-4
References:
1. Koolman, J. and Karlson, P. Ecdysone oxidase, an enzyme from the blowfly Calliphora erythrocephala (Meigen). Hoppe-Seyler's Z. Physiol. Chem. 35 (1975) 1131. [PMID: 297]
Accepted name: choline oxidase
Reaction: choline + 2 O2 + H2O = betaine + 2 H2O2 (overall reaction)
(1a) choline + O2 = betaine aldehyde + H2O2
(1b) betaine aldehyde + O2 + H2O = betaine + H2O2
Glossary: choline = (2-hydroxyethyl)trimethylammonium
betaine aldehyde = N,N,N-trimethyl-2-oxoethylammonium
betaine = glycine betaine = N,N,N-trimethylammonioacetate
Systematic name: choline:oxygen 1-oxidoreductase
Comments: A flavoprotein (FAD). In many bacteria, plants and animals, the osmoprotectant betaine is synthesized using different enzymes to catalyse the conversion of (1) choline into betaine aldehyde and (2) betaine aldehyde into betaine. In plants, the first reaction is catalysed by EC 1.14.15.7EC 1.14.15.7, choline monooxygenase, whereas in animals and many bacteria, it is catalysed by either membrane-bound choline dehydrogenase (EC 1.1.99.1) or soluble choline oxidase (EC 1.1.3.17) [6]. The enzyme involved in the second step, EC 1.2.1.8, betaine-aldehyde dehydrogenase, appears to be the same in those plants, animals and bacteria that use two separate enzymes.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9028-67-5
References:
1. Ikuta, S., Imamura, S., Misaki, H. and Horiuti, Y. Purification and characterization of choline oxidase from Arthrobacter globiformis. J. Biochem. (Tokyo) 82 (1977) 1741-1749. [PMID: 599154]
2. Rozwadowski, K.L., Khachatourians, G.G. and Selvaraj, G. Choline oxidase, a catabolic enzyme in Arthrobacter pascens, facilitates adaptation to osmotic stress in Escherichia coli. J. Bacteriol. 173 (1991) 472-478. [PMID: 1987142]
3. Rand, T., Halkier, T. and Hansen, O.C. Structural characterization and mapping of the covalently linked FAD cofactor in choline oxidase from Arthrobacter globiformis. Biochemistry 42 (2003) 7188-7194. [PMID: 12795615]
4. Gadda, G., Powell, N.L. and Menon, P. The trimethylammonium headgroup of choline is a major determinant for substrate binding and specificity in choline oxidase. Arch. Biochem. Biophys. 430 (2004) 264-273. [PMID: 15369826]
5. Fan, F. and Gadda, G. On the catalytic mechanism of choline oxidase. J. Am. Chem. Soc. 127 (2005) 2067-2074. [PMID: 15713082]
6. 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]
7. Fan, F., Ghanem, M. and Gadda, G. Cloning, sequence analysis, and purification of choline oxidase from Arthrobacter globiformis: a bacterial enzyme involved in osmotic stress tolerance. Arch. Biochem. Biophys. 421 (2004) 149-158. [PMID: 14678796]
8. Gadda, G. Kinetic mechanism of choline oxidase from Arthrobacter globiformis. Biochim. Biophys. Acta 1646 (2003) 112-118. [PMID: 12637017]
Accepted name: secondary-alcohol oxidase
Reaction: a secondary alcohol + O2 = a ketone + H2O2
Other name(s): polyvinyl alcohol oxidase; secondary alcohol oxidase
Systematic name: secondary-alcohol:oxygen oxidoreductase
Comments: Acts on secondary alcohols with five or more carbons, and polyvinyl alcohols with molecular mass over 300 Da. The Pseudomonas enzyme contains one atom of non-heme iron per molecule.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 71245-08-4
References:
1. Morita, M., Hamada, N., Sakai, K. and Watanabe, Y. Purification and properties of secondary alcohol oxidase from a strain of Pseudomonas. Agric. Biol. Chem. 43 (1979) 1225-1235.
2. Sakai, K., Hamada, N. and Watanabe, Y. Separation of secondary alcohol oxidase and oxidized poly(vinyl alcohol) hydrolase by hydrophobic and dye-ligand chromatographies. Agric. Biol. Chem. 47 (1983) 153-155.
3. Suzuki, T. Purification and some properties of polyvinyl alcohol-degrading enzyme produced by Pseudomonas O-3. Agric. Biol. Chem. 40 (1976) 497-504.
4. Suzuki, T. Oxidation of secondary alcohols by polyvinyl alcohol-degrading enzyme produced by Pseudomonas O-3. Agric. Biol. Chem. 42 (1977) 1187-1194.
Accepted name: 4-hydroxymandelate oxidase
Reaction: (S)-4-hydroxymandelate + O2 = 4-hydroxybenzaldehyde + CO2 + H2O2
Glossary: (S)-4-hydroxymandelate = (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate
Other name(s): L-4-hydroxymandelate oxidase (decarboxylating); (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate:oxygen 1-oxidoreductase
Systematic name: (S)-4-hydroxymandelate:oxygen 1-oxidoreductase
Comments: A flavoprotein (FAD); requires Mn2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 60976-30-9
References:
1. Bhat, S.G. and Vaidyanathan, C.S. Purification and properties of L-4-hydroxymandelate oxidase from Pseudomonas convexa. Eur. J. Biochem. 68 (1976) 323-331. [PMID: 976259]
Accepted name: long-chain-alcohol oxidase
Reaction: a long-chain alcohol + O2 = a long-chain aldehyde + H2O2
Other name(s): long-chain fatty alcohol oxidase; fatty alcohol oxidase; fatty alcohol:oxygen oxidoreductase; long-chain fatty acid oxidase
Systematic name: long-chain-alcohol:oxygen oxidoreductase
Comments: Oxidizes long-chain fatty alcohols; best substrate is dodecyl alcohol.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 129430-50-8
References:
1. Moreau, R.A. and Huang, A.H.C. Oxidation of fatty alcohol in the cotyledons of jojoba seedlings. Arch. Biochem. Biophys. 194 (1979) 422-430. [PMID: 36040]
2. Moreau, R.A. and Huang, A.H.C. Enzymes of wax ester catabolism in jojoba. Methods Enzymol. 71 (1981) 804-813.
3. Cheng, Q., Liu, H.T., Bombelli, P., Smith, A. and Slabas, A.R. Functional identification of AtFao3, a membrane bound long chain alcohol oxidase in Arabidopsis thaliana. FEBS Lett. 574 (2004) 62-68. [PMID: 15358540]
4. Zhao, S., Lin, Z., Ma, W., Luo, D. and Cheng, Q. Cloning and characterization of long-chain fatty alcohol oxidase LjFAO1 in Lotus japonicus. Biotechnol. Prog. 24 (2008) 773-779. [PMID: 18396913]
5. Cheng, Q., Sanglard, D., Vanhanen, S., Liu, H.T., Bombelli, P., Smith, A. and Slabas, A.R. Candida yeast long chain fatty alcohol oxidase is a c-type haemoprotein and plays an important role in long chain fatty acid metabolism. Biochim. Biophys. Acta 1735 (2005) 192-203. [PMID: 16046182]
Accepted name: glycerol-3-phosphate oxidase
Reaction: sn-glycerol 3-phosphate + O2 = glycerone phosphate + H2O2
Other name(s): glycerol phosphate oxidase; glycerol-1-phosphate oxidase; glycerol phosphate oxidase; L-α-glycerophosphate oxidase; α-glycerophosphate oxidase; L-α-glycerol-3-phosphate oxidase
Systematic name: sn-glycerol-3-phosphate:oxygen 2-oxidoreductase
Comments: A flavoprotein (FAD).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9046-28-0
References:
1. Gancedo, C., Gancedo, J.M. and Sols, A. Glycerol metabolism in yeasts. Pathways of utilization and production. Eur. J. Biochem. 5 (1968) 165-172. [PMID: 5667352]
2. Koditschek, L.K. and Umbreit, W.W. α-Glycerophosphate oxidase in Streptococcus faecium F 24. J. Bacteriol. 93 (1969) 1063-1068. [PMID: 5788698]
[EC 1.1.3.22 Transferred entry: now EC 1.17.3.2, xanthine oxidase. The enzyme was incorrectly classified as acting on a CH-OH group (EC 1.1.3.22 created 1961 as EC 1.2.3.2, transferred 1984 to EC 1.1.3.22, modified 1989, deleted 2004)]
Accepted name: thiamine oxidase
Reaction: thiamine + 2 O2 + H2O = thiamine acetic acid + 2 H2O2
Other name(s): thiamin dehydrogenase; thiamine dehydrogenase; thiamin:oxygen 5-oxidoreductase
Systematic name: thiamine:oxygen 5-oxidoreductase
Comments: A flavoprotein (FAD). The product differs from thiamine in replacement of -CH2.CH2.OH by -CH2.COOH; the two-step oxidation proceeds without the release of the intermediate aldehyde from the enzyme.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 96779-44-1
References:
1. Edmondson, D.E., Kenney, W.C. and Singer, T.P. Structural elucidation and properties of 8α-(N1-histidyl)riboflavin: the flavin component of thiamine dehydrogenase and β-cyclopiazonate oxidocyclase. Biochemistry 15 (1976) 2937-2945. [PMID: 8076]
2. Gomez-Moreno, C. and Edmondson, D.E. Evidence for an aldehyde intermediate in the catalytic mechanism of thiamine oxidase. Arch. Biochem. Biophys. 239 (1985) 46-52. [PMID: 2988447]
3. Neal, R.A. Bacterial metabolism of thiamine. 3. Metabolism of thiamine to 3-(2'-methyl-4'-amino-5'-pyrimidylmethyl)-4-methyl-thiazole-5-acetic acid (thiamine acetic acid) by a flavoprotein isolated from a soil microorganism. J. Biol. Chem. 245 (1970) 2599-2604. [PMID: 4987737]
[EC 1.1.3.24 Transferred entry: L-galactonolactone oxidase. Now EC 1.3.3.12, L-galactonolactone oxidase. The enzyme had been incorrectly classified as acting upon a CH-OH donor rather than a CH-CH donor. (EC 1.1.3.24 created 1984, deleted 2006)]
[EC 1.1.3.25 Transferred entry: now included with EC 1.1.99.18, cellobiose dehydrogenase (acceptor) (EC 1.1.3.25 created 1986, deleted 2005)]
[EC 1.1.3.26 Transferred entry: now EC 1.21.3.2, columbamine oxidase (EC 1.1.3.26 created 1989, deleted 2002)]
Accepted name: hydroxyphytanate oxidase
Reaction: L-2-hydroxyphytanate + O2 = 2-oxophytanate + H2O2
Other name(s): L-2-hydroxyphytanate:oxygen 2-oxidoreductase
Systematic name: L-2-hydroxyphytanate:oxygen 2-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 114454-12-5
References:
1. Vamecq, J. and Draye, J.P. The enzymatic and mass spectrometric identification of 2-oxophytanic acid, a product of the peroxisomal oxidation of l-2-hydroxyphytanic acid. Biomed. Environ. Mass Spectrom. 15 (1988) 345-351. [PMID: 3288289]
Accepted name: nucleoside oxidase
Reaction: inosine + O2 = 9-riburonosylhypoxanthine + 2 H2O
(1a) 2 inosine + O2 = 2 5′-dehydroinosine
(1b) 2 5′-dehydroinosine + O2 = 2 9-riburonosylhypoxanthine + 2 H2O
Systematic name: nucleoside:oxygen 5'-oxidoreductase
Comments: Other purine and pyrimidine nucleosides (as well as 2′-deoxynucleosides) are substrates, but ribose and nucleotides are not substrates. The overall reaction takes place in two separate steps, with the 5′-dehydro nucleoside being released from the enzyme to serve as substrate for the second reaction. This enzyme differs from EC 1.1.3.39, nucleoside oxidase (H2O2-forming), as it produces water rather than hydrogen peroxide.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 82599-71-1
References:
1. Isono, Y., Sudo, T. and Hoshino, M. Purification and reaction of a new enzyme, nucleoside oxidase. Agric. Biol. Chem. 53 (1989) 1663-1669.
2. Isono, Y., Sudo, T. and Hoshino, M. Properties of a new enzyme, nucleoside oxidase, from Pseudomonas maltophilia LB-86. Agric. Biol. Chem. 53 (1989) 1671-1677.
Accepted name: N-acylhexosamine oxidase
Reaction: N-acetyl-D-glucosamine + O2 = N-acetyl-D-glucosaminate + H2O2
Other name(s): N-acyl-D-hexosamine oxidase; N-acyl-β-D-hexosamine:oxygen 1-oxidoreductase
Systematic name: N-acyl-D-hexosamine:oxygen 1-oxidoreductase
Comments: Also acts on N-glycolylglucosamine, N-acetylgalactosamine and, more slowly, on N-acetylmannosamine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 121479-58-1
References:
1. Horiuchi, T. Purification and properties of N-acyl-D-hexosamine oxidase from Pseudomonas sp 15-1. Agric. Biol. Chem. 53 (1989) 361-368.
Accepted name: polyvinyl-alcohol oxidase
Reaction: polyvinyl alcohol + O2 = oxidized polyvinyl alcohol + H2O2
Other name(s): dehydrogenase, polyvinyl alcohol; PVA oxidase
Systematic name: polyvinyl-alcohol:oxygen oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 119940-13-5
References:
1. Shimao, M., Nishimura, Y., Kato, N. and Sakazawa, C. Localization of polyvinyl alcohol oxidase produced by a bacterial symbiont Pseudomonas sp strain VM 15C. Appl. Environ. Microbiol. 49 (1985) 8-10.
2. Shimao, M., Onishi, S., Kato, N. and Sakazawa, C. Pyrroloquinoline quinone-dependent cytochrome reduction in polyvinyl alcohol-degrading Pseudomonas sp strain VM15C. Appl. Environ. Microbiol. 55 (1989) 275-278.
[EC 1.1.3.31 Deleted entry: methanol oxidase. Cannot be distinguished from EC 1.1.3.13, alcohol oxidase. (EC 1.1.3.31 created 1992, deleted 2003)]
[EC 1.1.3.32 Transferred entry: now EC 1.14.21.1, (S)-stylopine synthase (EC 1.1.3.32 created 1999, deleted 2002)]
[EC 1.1.3.33 Transferred entry: now EC 1.14.21.2, (S)-cheilanthifoline synthase (EC 1.1.3.33 created 1999, deleted 2002)]
[EC 1.1.3.34 Transferred entry: now EC 1.14.21.3, berbamunine synthase (EC 1.1.3.34 created 1999, deleted 2002)]
[EC 1.1.3.35 Transferred entry: now EC 1.14.21.4, salutaridine synthase (EC 1.1.3.35 created 1999, deleted 2002)]
[EC 1.1.3.36 Transferred entry: now EC 1.14.21.5, (S)-canadine synthase (EC 1.1.3.36 created 1999, deleted 2002)]
Accepted name: D-arabinono-1,4-lactone oxidase
Reaction: D-arabinono-1,4-lactone + O2 = dehydro-D-arabinono-1,4-lactone + H2O2
For diagram click here.
Glossary: dehydro-D-arabinono-1,4-lactone = (5R)-3,4-dihydroxy-5-(hydroxymethyl)furan-2(5H)-one
Other name(s): D-arabinono-γ-lactone oxidase; ALO
Systematic name: D-arabinono-1,4-lactone:oxygen oxidoreductase
Comments: A flavoprotein (FAD). L-Galactono-1,4-lactone, L-gulono-1,4-lactone and L-xylono-1,4-lactone can also act as substrates but D-glucono-1,5-lactone, L-arabinono-1,4-lactone, D-galactono-1,4-lactone and D-gulono-1,4-lactone cannot [1]. With L-galactono-1,4-lactone as substrate, the product is L-ascorbate [3]. The product dehydro-D-arabinono-1,4-lactone had previously been referred to erroneously as D-erythroascorbate (CAS registry number: 5776-48-7; formula: C6H8O6), although Huh et al. 1994 did refer to it as being a five-carbon compound.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 182372-12-9
References:
1. Huh, W.K., Kim, S.T., Yang, K.S., Seok, Y.J., Hah, Y.C. and Kang, S.O. Characterisation of D-arabinono-1,4-lactone oxidase from Candida albicans ATCC 10231. Eur. J. Biochem. 225 (1994) 1073-1079. [PMID: 7957197]
Accepted name: vanillyl-alcohol oxidase
Reaction: vanillyl alcohol + O2 = vanillin + H2O2
Other name(s): 4-hydroxy-2-methoxybenzyl alcohol oxidase
Systematic name: vanillyl alcohol:oxygen oxidoreductase
Comments: Vanillyl-alcohol oxidase from Penicillium simplicissimum contains covalently bound FAD. It converts a wide range of 4-hydroxybenzyl alcohols and 4-hydroxybenzylamines into the corresponding aldehydes. The allyl group of 4-allylphenols is also converted into the -CH=CH-CH2OH group.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 143929-24-2
References:
1. de Jong, E., van Berkel, W.J.H., van der Zwan, R.P. and de Bont, J.A.M. Purification and characterization of vanillyl-alcohol oxidase from Penicillium simplicissimum, a novel aromatic alcohol oxidase containing covalently bound FAD. Eur. J. Biochem. 208 (1992) 651-657. [PMID: 1396672]
2. Fraaije, M.W., Veeger, C. and van Berkel, W.J.H. Substrate specificity of flavin-dependent vanillyl-alcohol oxidase from Penicillium simplicissimum. Evidence for the production of 4-hydroxycinnamyl alcohols from 4-allylphenols. Eur. J. Biochem. 234 (1995) 271-277. [PMID: 8529652]
Accepted name: nucleoside oxidase (H2O2-forming)
Reaction: adenosine + 2 O2 + H2O = 9-riburonosyladenine + 2 H2O2 (overall reaction)
(1a) adenosine + O2 = 5'-dehydroadenosine + H2O2
(1b) 5'-dehydroadenosine + O2 + H2O = 9-riburonosyladenine + H2O2
Systematic name: nucleoside:oxygen 5'-oxidoreductase (H2O2-forming)
Comments: A heme-containing flavoprotein (FAD). Other purine and pyrimidine nucleosides (as well as 2'-deoxynucleosides and arabinosides) are substrates, but ribose and nucleotides are not substrates. The overall reaction takes place in two separate steps steps, with the 5'-dehydro nucleoside being released from the enzyme to serve as substrate for the second reaction. This enzyme differs from EC 1.1.3.28, nucleoside oxidase, as it produces hydrogen peroxide rather than water. Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Koga, S., Ogawa, J., Cheng, L.Y., Choi, Y.M., Yamada, H. and Shimizu, S. Nucleoside oxidase, a hydrogen peroxide-forming oxidase, from Flavobacterium meningosepticum. Appl. Environ. Microbiol. 63 (1997) 4282-4286.
Accepted name: D-mannitol oxidase
Reaction: mannitol + O2 = mannose + H2O2
Other name(s): mannitol oxidase; D-arabitol oxidase
Systematic name: mannitol:oxygen oxidoreductase (cyclizing)
Comments: Also catalyses the oxidation of D-arabinitol and, to a lesser extent, D-glucitol (sorbitol), whereas L-arabinitol is not a good substrate. The enzyme from the snails Helix aspersa and Arion ater is found in a specialised tubular organelle that has been termed the mannosome.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 73562-29-5
References:
1. Vorhaben, J.E., Scott, J.F., Smith, D.D. and Campbell, J.W. Mannitol oxidase: partial purification and characterisation of the membrane-bound enzyme from the snail Helix aspersa. Int. J. Biochem. 18 (1986) 337-344. [PMID: 3519307]
2. Large, A.T., Jones, C.J.P. and Connock, M.J. The association of mannitol oxidase with a distinct organelle in the digestive gland of the terrestrial slug Arion ater. Protoplasma 175 (1993) 93-101.
Accepted name: alditol oxidase
Reaction: an alditol + O2 = an aldose + H2O2
Other name(s): xylitol oxidase; xylitol:oxygen oxidoreductase; AldO
Systematic name: alditol:oxygen oxidoreductase
Comments: The enzyme from Streptomyces sp. IKD472 and from Streptomyces coelicolor is a monomeric oxidase containing one molecule of FAD per molecule of protein [1,2]. While xylitol (five carbons) and sorbitol (6 carbons) are the preferred substrates, other alditols, including L-threitol (four carbons), D-arabitol (five carbons), D-galactitol (six carbons) and D-mannitol (six carbons) can also act as substrates, but more slowly [1,2]. Belongs in the vanillyl-alcohol-oxidase family of enzymes [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 177322-52-0
References:
1. Yamashita, M., Omura, H., Okamoto, E., Furuya, Y., Yabuuchi, M., Fukahi, K. and Murooka, Y. Isolation, characterization, and molecular cloning of a thermostable xylitol oxidase from Streptomyces sp. IKD472. J. Biosci. Bioeng. 89 (2000) 350-360. [PMID: 16232758]
2. Heuts, D.P., van Hellemond, E.W., Janssen, D.B. and Fraaije, M.W. Discovery, characterization, and kinetic analysis of an alditol oxidase from Streptomyces coelicolor. J. Biol. Chem. 282 (2007) 20283-20291. [PMID: 17517896]
3. Forneris, F., Heuts, D.P., Delvecchio, M., Rovida, S., Fraaije, M.W. and Mattevi, A. Structural analysis of the catalytic mechanism and stereoselectivity in Streptomyces coelicolor alditol oxidase. Biochemistry 47 (2008) 978-985. [PMID: 18154360]
Accepted name: prosolanapyrone-II oxidase
Reaction: prosolanapyrone II + O2 = prosolanapyrone III + H2O2
For diagram of reaction click here
Glossary: prosolanapyrone II = 3-(hydroxymethyl)-4-methoxy-6-(1E,7E,9E)-undeca-1,7,9-trien-1-yl-2H-pyran-2-one
prosolanapyrone III = 4-methoxy-2-oxo-6-(1E,7E,9E)-undeca-1,7,9-trien-1-yl-2H-pyran-3-carboxaldehyde
Other name(s): Sol5 (ambiguous); SPS (ambiguous); solanapyrone synthase (bifunctional enzyme: prosolanapyrone II oxidase/prosolanapyrone III cycloisomerase); prosolanapyrone II oxidase
Systematic name: prosolanapyrone-II:oxygen 3'-oxidoreductase
Comments: The enzyme is involved in the biosynthesis of the phytotoxin solanapyrone by some fungi. The bifunctional enzyme catalyses the oxidation of prosolanapyrone II and the subsequent Diels Alder cycloisomerization of the product prosolanapyrone III to (–)-solanapyrone A (cf. EC 5.5.1.20, prosolanapyrone III cycloisomerase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Kasahara, K., Miyamoto, T., Fujimoto, T., Oguri, H., Tokiwano, T., Oikawa, H., Ebizuka, Y. and Fujii, I. Solanapyrone synthase, a possible Diels-Alderase and iterative type I polyketide synthase encoded in a biosynthetic gene cluster from Alternaria solani. Chembiochem. 11 (2010) 1245-1252. [PMID: 20486243]
2. Katayama, K., Kobayashi, T., Oikawa, H., Honma, M. and Ichihara, A. Enzymatic activity and partial purification of solanapyrone synthase: first enzyme catalyzing Diels-Alder reaction. Biochim. Biophys. Acta 1384 (1998) 387-395. [PMID: 9659400]
3. Katayama, K., Kobayashi, T., Chijimatsu, M., Ichihara, A. and Oikawa, H. Purification and N-terminal amino acid sequence of solanapyrone synthase, a natural Diels-Alderase from Alternaria solani. Biosci. Biotechnol. Biochem. 72 (2008) 604-607. [PMID: 18256508]
Accepted name: paromamine 6'-oxidase
Reaction: paromamine + O2 = 6'-dehydroparomamine + H2O2
For diagram of reaction click here.
Other name(s): btrQ (gene name); neoG (gene name); kanI (gene name); tacB (gene name); neoQ (obsolete gene name)
Systematic name: paromamine:oxygen 6'-oxidoreductase
Comments: Contains FAD. Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. Works in combination with EC 2.6.1.93, neamine transaminase, to replace the 6-hydroxy group of paromamine with an amino group. The enzyme from the bacterium Streptomyces fradiae also catalyses EC 1.1.3.44, 6′′′-hydroxyneomycin C oxidase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Huang, F., Spiteller, D., Koorbanally, N.A., Li, Y., Llewellyn, N.M. and Spencer, J.B. Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin. ChemBioChem. 8 (2007) 283-288. [PMID: 17206729]
2. Yu, Y., Hou, X., Ni, X. and Xia, H. Biosynthesis of 3'-deoxy-carbamoylkanamycin C in a Streptomyces tenebrarius mutant strain by tacB gene disruption. J. Antibiot. (Tokyo) 61 (2008) 63-69. [PMID: 18408324]
3. Clausnitzer, D., Piepersberg, W. and Wehmeier, U.F. The oxidoreductases LivQ and NeoQ are responsible for the different 6'-modifications in the aminoglycosides lividomycin and neomycin. J. Appl. Microbiol. 111 (2011) 642-651. [PMID: 21689223]
Accepted name: 6′′′-hydroxyneomycin C oxidase
Reaction: 6′′′-deamino-6′′′-hydroxyneomycin C + O2 = 6′′′-deamino-6′′′-oxoneomycin C + H2O2
For diagram of reaction click here.
Other name(s): neoG (gene name); neoQ (obsolete gene name)
Systematic name: 6′′′-deamino-6′′′-hydroxyneomycin C:oxygen 6′′′-oxidoreductase
Comments: Contains FAD. Involved in the biosynthetic pathway of aminoglycoside antibiotics of the neomycin family. Works in combination with EC 2.6.1.95, neomycin C transaminase, to replace the 6′′′-hydroxy group of 6′′′-hydroxyneomycin C with an amino group. Also catalyses EC 1.1.3.43, paromamine 6'-oxidase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Huang, F., Spiteller, D., Koorbanally, N.A., Li, Y., Llewellyn, N.M. and Spencer, J.B. Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin. ChemBioChem. 8 (2007) 283-288. [PMID: 17206729]
2. Clausnitzer, D., Piepersberg, W. and Wehmeier, U.F. The oxidoreductases LivQ and NeoQ are responsible for the different 6'-modifications in the aminoglycosides lividomycin and neomycin. J. Appl. Microbiol. 111 (2011) 642-651. [PMID: 21689223]