NEW ENTRIES
EC 1.1.1.247
Recommended name: codeinone reductase (NADPH2)
Reaction: codeinone + NADPH2 = codeine + NADP
Systematic name: codeine:NADP oxidoreductase
Comments: catalyses the reversible reduction of codeinone to codeine, which is a direct precursor of morphine in the opium poppy plant, Papaver somniferum.
References:
1. Lenz, R., Zenk, M.H. Stereoselective reduction of codeinone, the penultimate step during morphine biosynthesis in Papaver somniferum. Tetrahedron Lett. 36 (1995) 2449-2452.
2. Lenz, R., Zenk, M.H. Purification and properties of codeinone reductase (NADPH) from Papaver somniferum cell cultures. Eur. J. Biochem. 233 (1995) 132-139. [PMID: 7588736]
EC 1.1.1.248
Recommended name: salutaridine reductase (NADPH2)
Reaction: salutaridine + NADPH2 = salutaridinol + NADP
Systematic name: salutaridinol:NADP 7-oxidoreductase
Comments: catalyses the reversible reduction of salutaridine to salutaridinol, which is a direct precursor of morphinan alkaloids in the poppy plant.
References:
1. Gerady, R., Zenk, M.H. Purification and characterization of salutaridine:NADPH 7-oxidoreductase from Papaver somniferum. Phytochemistry 34 (1993) 125-132.
EC 1.1.1.249 provisional entry deleted and transferred to EC 2.4.1.46
EC 1.1.1.250
Recommended name: D-arabinitol 2-dehydrogenase
Reaction: D-arabinitol + NAD = D-ribulose + NADH2
Other name(s): D-arabinitol 2-dehydrogenase (ribulose-forming)
Systematic name: D-arabinitol:NAD 2-oxidoreductase (D-ribulose-forming)
References:
1. Wong, B., Murray, J.S., Castellanos, M., Croen, K.D. D-Arabitol metabolism in Candida albicans: studies of the biosynthetic pathway and the gene that encodes NAD-dependent D-arabitol dehydrogenase. J. Bacteriol. 175 (1993) 6314-6320. [PMID: 8407803]
2.Quong, M.W., Miyada, C.G., Switchenko, A.C., Goodman, T.C. Identification, purification, and characterization of a D-arabinitol-specific dehydrogenase from Candida tropicalis. Biochem. Biophys. Res. Commun. 196 (1993) 1323-1329. [PMID: 8250887]
EC 1.1.1.251
Recommended name: galactitol-1-phosphate 5-dehydrogenase
Reaction: galactitol-1-phosphate + NAD = L-tagatose 6-phosphate + NADH2
Systematic name: galactitol-1-phosphate:NAD oxidoreductase
Comments: contains zinc.
References:
1. Nobelmann, B., Lengeler, J.W. Sequence of the gat operon for galactitol utilization from a wild-type strain EC3132 of Escherichia coli. Biochim. Biophys. Acta 1262 (1995) 69-72. [PMID: 7772602]
EC 1.1.1.252
Recommended name: tetrahydroxynaphthalene reductase
Reaction: scytalone + NADP = 1,3,6,8-tetrahydroxynaphthalene + NADPH2
Systematic name: scytalone:NADP δ5-oxidoreductase
Comments: reduces 1,3,6,8-tetrahydroxynaphthalene to scytalone and also reduces 1,3,8-trihydroxynaphthalene to vermelone. Involved with EC 4.2.1.94 in the biosynthesis of melanin in pathogenic fungi.
References:
1. Wheeler, M.H., Greenblatt, G.A. The inhibition of melanin biosynthetic reactions in Pyricularia oryzae by compounds that prevent rice blast disease. Exp. Mycol. 12 (1988) 151-160.
2. Vidal-Cros, A., Viviani, F., Labesse, G., Boccara, M., Gaudry M. Polyhydroxynaphthalene reductase involved in melanin biosynthesis in Magnaporthe grisea. Purification, cDNA cloning and sequencing. Eur. J. Biochem. 219 (1994) 985-992. [PMID: 8112349]
3. Thompson, J.E., Basarab, G.S., Andersson, A., Lindqvist, Y., Jordan, D.B. Trihydroxynaphthalene reductase from Magnaporthe grisea: realization of an active center inhibitor and elucidation of the kinetic mechanism. Biochemistry 36 (1997) 1852-1860. [PMID: 9048570]
EC 1.1.1.253
Recommended name: pteridine reductase
Reaction: 5,6,7,8-tetrahydrobiopterin + 2 NADP = biopterin + 2 NADPH2
Other name(s): pteridine reductase 1; PTR1
Systematic name: 5,6,7,8-tetrahydrobiopterin:NADP oxidoreductase
Comments: the enzyme from Leishmania (both amastigote and promastigote forms) catalyses the NADPH2-dependent reduction of folate and a wide variety of unconjugated pterins, including biopterin, to their tetrahydro forms. It also catalyses the reduction of 7,8-dihydropterins and 7,8-dihydrofolate to their tetrahydro forms. In contrast to dihydrofolate reductase (EC 1.5.1.3) and dihydropteridine reductase (EC 1.6.99.7), pteridine reductase will not catalyse the reduction of the quinonoid form of dihydrobiopterin. The enzyme is specific for NADPH2; no activity has been detected with NADH2. It also differs from EC 1.5.1.3 in being specific for the B side of NADPH2.
References:
1. Nare, B., Hardy, L., Beverley, S.M. The roles of pteridine reductase 1 and dihydrofolate reductase-thymidylate synthase in pteridine metabolism in the protozoan parasite Leishmania major. J. Biol. Chem. 272 (1997) 13883-13891. [PMID: 9153248]
EC 1.1.1.254
Recommended name: (S)-carnitine 3-dehydrogenase
Reaction: (S)-carnitine + NAD = 3-dehydrocarnitine + NADH2
Systematic name: (S)-carnitine:NAD oxidoreductase
Comments: specific for the (S)-enantiomer of carnitine, i.e., the enantiomer of the substrate of EC 1.1.1.108
References:
1. Setyahadi, S., Tomoko, U., Arimoto, T., Mori, N., Kitamoto, Y. Purification and properties of a new enzyme, D-carnitine dehydrogenase, from Agrobacterium sp. 525a. Biosci. Biotechnol. Biochem. 61 (1997) 1055-1058. [PMID: 9214773]
EC 1.1.3.32
Recommended name: (S)-stylopine synthase
Reaction: (S)-cheilanthifoline + NADPH2 + O2 = (S)-stylopine + NADP + 2 H2O
Other name(s): (S)-cheilanthifoline oxidase (methylenedioxy-bridge-forming)
Systematic name: (S)-cheilanthifoline, NADPH2: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.
References:
1. Bauer, W., Zenk, M.H. Two methylenedioxy bridge-forming cytochrome P-450 dependent enzymes are involved in (S)-stylopine biosynthesis. Phytochemistry 30 (1991) 2953-2961.
EC 1.1.3.33
Recommended name: S-cheilanthifoline synthase
Reaction: (S)-scoulerine + NADPH2 + O2 = (S)-cheilanthifoline + NADP + 2 H2O
Other name(s): (S)-scoulerine oxidase (methylenedioxy-bridge-forming)
Systematic name: (S)-scoulerine, NADPH2: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.
References: 1. Bauer, W., Zenk, M.H. Two methylenedioxy bridge-forming cytochrome P-450 dependent enzymes are involved in (S)-stylopine biosynthesis. Phytochemistry 30 (1991) 2953-2961.
EC 1.1.3.34
Recommended name: berbamunine synthase
Reaction: (S)-N-methylcoclaurine + (R)-N-methylcoclaurine + NADPH2 + O2 = berbamunine + NADP + 2 H2O
Other name(s): (S)-N-methylcoclaurine oxidase (C-O phenol-coupling)
Systematic name: (S)-N-methylcoclaurine, NADPH2: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 2 molecules of (R)-N-methylcoclaurine gives the dimer guattagaumerine.
References:
1. Stadler, R., 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) 822-831. [PMID: 8380416]
EC 1.1.3.35
Recommended name: salutaridine synthase
Reaction: (R)-reticuline + NADPH2 + O2 = salutaridine + NADP + 2 H2O
Other name(s): (R)-reticuline oxidase (C-C phenol-coupling)
Systematic name: (R)-reticuline, NADPH2: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.
References:
1. Gerady, R., 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.
EC 1.1.3.36
Recommended name: (S)-canadine synthase
Reaction: (S)-tetrahydrocolumbamine + NADPH2 + O2 = (S)-canadine + NADP + 2 H2O
Other name(s): (S)-tetrahydrocolumbamine oxidase (methylenedioxy-bridge-forming); (S)-tetrahydroberberine synthase
Systematic name: (S)-tetrahydrocolumbamine, NADPH2: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.
References:
1. Rueffer, M., 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
EC 1.1.3.37
Recommended name: D-arabinono-1,4-lactone oxidase
Reaction: D-arabinono-1,4-lactone + O2 = D-erythro-ascorbate + H2O2
Systematic name: D-arabinono-1,4-lactone:oxygen oxidoreductase
Comments: a flavoprotein (FAD).
References:
1. Huh, W.K., Kim, S.T., Yang, K.S., Seok, Y.J., Hah, Y.C., 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]
EC 1.1.3.38
Recommended 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.
References:
1. de Jong, E., van Berkel, W.J.H., van der Zwan, R.P., 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., 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]
EC 1.1.99.27
Recommended name: (R)-pantolactone dehydrogenase (flavin)
Reaction: (R)-pantolactone + acceptor = 2-dehydropantolactone + reduced acceptor
Other name(s): 2-dehydropantolactone reductase (flavin); 2-dehydropantoyl-lactone reductase (flavin); (R)-pantoyllactone dehydrogenase (flavin)
Systematic name: (R)-pantolactone:acceptor oxidoreductase (flavin-containing)
Comments: high specificity for (R)-pantolactone. Phenazine methosulfate (PMS) can act as acceptor. The enzyme has been studied in the bacterium Nocardia asteroides and shown to be membrane-bound and induced by 1,2-propanediol. The FMN cofactor is non-covalently bound.
References:
1. Kataoka, M., Shimizu, S., Yamada, H. Purification and characterization of a novel FMN-dependent enzyme. Membrane-bound L-(+)-pantoyl lactone dehydrogenase from Nocardia asteroides. Eur. J. Biochem. 204 (1992) 799-806. [PMID: 1541293]
EC 1.1.99.28
Recommended name: glucose-fructose oxidoreductase
Reaction: D-glucose + D-fructose = D-gluconolactone + D-glucitol
Systematic name: D-glucose:D-fructose oxidoreductase
Comments: D-mannose, D-xylose, D-galactose, 2-deoxy-D-glucose and L-arabinose will function as aldose substrates, but with low affinities. The ketose substrate must be in the open-chain form. The apparent affinity for fructose is low, because little of the fructose substrate is in the open-chain form. Xylulose and glycerone (dihydroxyacetone) will replace fructose, but they are poor substrates. The enzyme from Zymomonas mobilis contains tightly bound NADP.
References:
1. Zachariou, M., Scopes, R.K. Glucose-fructose oxidoreductase: a new enzyme isolated from Zymomonas mobilis that is responsible for sorbitol production. J. Bacteriol. 167 (1986) 863-869.
2. Hardman, M.J., Scopes, R.K. The kinetics of glucose-fructose oxidoreductase from Zymomonas mobilis. Eur. J. Biochem. 173 (1988) 203-209.
3. Kanagasundaram, V., Scopes, R.K. Cloning, sequence analysis and expression of the structural gene encoding glucose-fructose oxidoreductase. J. Bacteriol. 174 (1992) 1439-1447. [PMID: 1537789]
EC 1.2.1.58
Recommended name: phenylglyoxylate dehydrogenase (acylating)
Reaction: phenylglyoxylate + NAD + CoA-SH = benzoyl-S-CoA + CO2 + NADH2
Systematic name: phenylglyoxylate:NAD oxidoreductase
Comments: requires thiamine diphosphate as cofactor. The enzyme from the denitrifying bacterium Azoarcus evansii is specific for phenylglyoxylate. 2-Oxoisovalerate is oxidised at 15% of the rate for phenylglyoxylate. Also reduces viologen dyes. Contains iron-sulfur centres and FAD.
References:
1. Hirsch, W., Schägger, H., Fuchs, G. Phenylglyoxylate:NAD+ oxidoreductase (CoA benzoylating), a new enzyme of anaerobic phenylalanine metabolism in the denitrifying bacterium Axoarcus evansii. Eur. J. Biochem. 251 (1998) 907-915. [PMID: 9490067]
EC 1.2.1.59
Recommended name: glyceraldehyde-3-phosphate dehydrogenase (NAD(P)) (phosphorylating)
Reaction: D-glyceraldehyde-3-phosphate + phosphate + NAD(P) = 3-phospho-D-glyceroyl phosphate + NAD(P)H2
Other name(s): triosephosphate dehydrogenase (NAD(P))
Systematic name: D-glyceraldehyde 3-phosphate:NAD(P) oxidoreductase (phosphorylating)
Comments: NAD and NADP can be used as cofactors with similar efficiency, unlike EC 1.2.1.12 and EC 1.2.1.13, which are NAD- and NADP-dependent, respectively.
References:
1. Valverde, F., Losada, M., Serrano, A. Cloning by functional complementation in E. coli of the gap2 gene of Synechocystis PCC 6803 supports an amphibolic role for cyanobacterial NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase. In: Photosynthesis: From Light to Biosphere (P. Mathis, ed.), Vol. 1 (1995) pp. 959-962. Kluwer Academic Publishers.
2. Valverde, F., Losada, M., Serrano, A. Functional complementation of an Escherichia coli gap mutant supports an amphibolic role for NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase of Synechocystis sp. strain PCC 6803. J. Bacteriol. 179 (1997) 4513-4522. [PMID: 9226260]
EC 1.2.2.4
Recommended name: carbon-monoxide oxygenase (cytochrome b-561)
Reaction: CO + H2O + ferrocytochrome b-561 = CO2 + 2 H+ + ferricytochrome b-561
Systematic name: carbon monoxide, water:cytochrome b-561 oxidoreductase
Comments: contains molybdopterin cytosine dinucleotide, FAD and [2Fe-2S]-clusters. Methylene blue and iodonitrotetrazolium chloride can act as artificial electron acceptors.
References:
1. Meyer, O., Jacobitz, S., Krüger, B. Biochemistry and physiology of aerobic carbon monoxide-utilizing bacteria. FEMS Microbiol. Rev. 39 (1986) 161-179.
2. Jacobitz, S., Meyer, O. Removal of CO dehydrogenase from Pseudomonas carboxydovorans cytoplasmic membranes, rebinding of CO dehydrogenase to depleted membranes and restoration of respiratory activities. J. Bacteriol. 171 (1989) 6294-6299. [PMID: 2808305]
EC 1.3.1.53
Recommended name: (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate dehydrogenase
Reaction: (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate + NAD = 3,4-dihydroxybenzoate + CO2 + NADH2
Other name(s): (1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase
Systematic name: (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate:NADoxidoreductase
Comments: requires FeII.
References:
1. Saller, E., Laue, H.R., Schläfli Oppenberg, H.R., Cook, A.M. Purification and some properties of (1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase from Comamonas testosteroni T-2. FEMS Microbiol. Lett. 130 (1996) 97-102.
EC 1.3.1.54
Recommended name: precorrin-6X reductase
Reaction: precorrin-6Y + NADP = precorrin-6X + NADPH2
Systematic name: precorrin-6Y:NADP oxidoreductase
References:
1. Blanche, F., Thibaut, D., Famechon, A., Debussche, L., Cameron, B., Crouzet, J. Precorrin-6X reductase from Pseudomonas denitrificans: purification and characterization of the enzyme and identification of the structural gene. J. Bacteriol. 174 (1992) 1036-1042. [PMID: 1732193]
EC 1.3.1.55
Recommended name: cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase
Reaction: cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate + NAD = catechol + CO2 + NADH2
Other name(s): 2-hydro-1,2-dihydroxybenzoate dehydrogenase
Systematic name: cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate:NAD oxidoreductase
References:
1. Neidle, E.L., Hartnett, C., Ornston, N.L., Bairoch, A., Rekik, M., Harayama, S. cis-Diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily. Eur. J. Biochem. 204 (1992) 113-120. [PMID: 1740120]
EC 1.3.99.15
Recommended name: benzoyl-CoA reductase
Reaction: benzoyl-CoA + reduced acceptor + 2 ATP = cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + 2 ADP + 2 phosphate
Other name(s): benzoyl-CoA reductase (dearomatizing)
Systematic name: cyclohexa-1,5-diene-1-carbonyl-CoA:acceptor oxidoreductase (aromatizing, ATP-forming)
Comments: an iron-sulfur protein. Requires Mg2+ or Mn2+. Reduced methyl viologen can act as electron donor. Inactive towards aromatic acids that are not CoA esters but will also catalyse the reaction: ammonia + acceptor + 2 ADP + 2 phosphate + H2O = hydroxylamine + reduced acceptor + 2 ATP. In the presence of reduced acceptor, but in the absence of oxidizable substrate, the enzyme catalyses the hydrolysis of ATP to ADP plus phosphate.
References:
1. Boll, M., Fuchs, G. Benzoyl-coenzyme A reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism. ATP dependence of the reaction, purification and some properties of the enzyme from Thauera aromatica strain K172. Eur. J. Biochem. 234 (1995) 921-933. [PMID: 8575453]
EC 1.3.99.16
Recommended name: isoquinoline 1-oxidoreductase
Reaction: isoquinoline + acceptor + H2O = isoquinolin-1(2H)-one + reduced acceptor
Systematic name: isoquinoline:acceptor 1-oxidoreductase (hydroxylating)
Comments: the enzyme from Pseudomonas diminuta is specific towards N-containing N-heterocyclic substrates, including isoquinoline, isoquinolin-5-ol, phthalazine and quinazoline. Electron acceptors include 1,2-benzoquinone, cytochrome c, ferricyanide, iodonitrotetrazolium chloride, nitroblue tetrazolium, Meldola blue and phenazine methosulfate.
References:
1. Lehmann, M., Tshisuaka, B., Fetzner, S., Roger, P., Lingens, F. Purification and characterization of isoquinoline 1-oxidoreductase from Pseudomonas diminuta 7, a novel molybdenum-containing hydroxylase. J. Biol. Chem. 269 (1994) 11254-11260. [PMID: 8157655]
2. Lehmann, M., Tshisuaka, B., Fetzner, S., Lingens, F. Molecular cloning of the isoquinoline 1-oxidoreductase genes from Pseudomonas diminuta 7, structural analysis of iorA and iorB, and sequence comparisons with other molybdenum-containing hydroxylases. J. Biol. Chem. 270 (1995) 14420-14429. [PMID: 7782304]
EC 1.3.99.17
Recommended name: quinoline 2-oxidoreductase
Reaction: quinoline + acceptor + H2O = isoquinolin-1(2H)-one + reduced acceptor
Systematic name: quinoline:acceptor 2-oxidoreductase (hydroxylating)
Comments: quinolin-2-ol, quinolin-7-ol, quinolin-8-ol, 3-, 4- and 8-methylquinolines and 8-chloroquinoline are substrates. Iodonitrotetrazolium chloride can act as an electron acceptor.
References:
1. Bauder, R., Tshisuaka, B., Lingens, F. Microbial metabolism of quinoline and related compounds. VII. Quinoline oxidoreductase from Pseudomonas putida: a molybdenum-containing enzyme. Biol. Chem. Hoppe-Seyler 371 (1990) 1137-1144.
2. Tshisuaka, B., Kappl, R., Huttermann, J., Lingens, F. Quinoline oxidoreductase from Pseudomonas putida 86: an improved purification procedure and electron paramagnetic resonance spectroscopy. Biochemistry 32 (1993) 12928-12934. [PMID: 8251516]
3. Peschke, B., Lingens, F. Microbial metabolism of quinoline and related compounds. XII. Isolation and characterization of the quinoline oxidoreductase from Rhodococcus sp. B1 compared with the quinoline oxidoreductase from Pseudomonas putida 86. Biol. Chem. Hoppe-Seyler 372 (1991) 1081-1088. [PMID: 1789933]
4. Schach, S., Tshisuaka, B., Fetzner, S., Lingens, F. Quinoline 2-oxidoreductase and 2-oxo-1,2-dihydroquinoline 5,6-dioxygenase from Comamonas testosteroni 63. The first two enzymes in quinoline and 3-methylquinoline degradation. Eur. J. Biochem. 232 (1995) 536-544. [PMID: 7556204]
EC 1.3.99.18
Recommended name: quinaldate 4-oxidoreductase
Reaction: quinaldate + acceptor + H2O = kynurenate + reduced acceptor
Other name(s): quinaldic acid 4-oxidoreductase
Systematic name: quinoline-2-carboxylate:acceptor 4-oxidoreductase (hydroxylating)
Comments: the enzyme from Pseudomonas sp. AK2 also acts on quinoline-8-carboxylate, whereas that from Serratia marcescens 2CC-1 will oxidize nicotinate; quinaldate is a substrate for both of these enzymes. 2,4,6-Trinitrobenzene sulfonate acid, 1,4-benzoquinone, 1,2-naphthoquinone, nitroblue tetrazolium, thionine and menadione will serve as an electron acceptor for the former enzyme and ferricyanide for the latter; Meldola blue, iodonitrotetrazolium chloride, phenazine methosulfate, 2,6-dichlorophenolindophenol and cytochrome c will act as electron acceptors for both.
References:
1. Sauter, M., Tshisuaka, B., Fetzner, S., Lingens, F. Microbial metabolism of quinoline and related compounds. XX. Quinaldic acid 4-oxidoreductase from Pseudomonas sp. AK-2 compared to other procaryotic molybdenum-containing hydroxylases. Biol. Chem. Hoppe Seyler 374 (1993) 1037-1046. [PMID: 8292263]
2. Fetzner, S., Lingens, F. Microbial metabolism of quinoline and related compounds. XVIII. Purification and some properties of the molybdenum- and iron-containing quinaldic acid 4-oxidoreductase from Serratia marcescens 2CC-1. Biol. Chem. Hoppe-Seyler 374 (1993) 363-376. [PMID: 8357532]
EC 1.3.99.19
Recommended name: quinoline-4-carboxylate 2-oxidoreductase
Reaction: quinoline-4-carboxylate + acceptor + H2O = quinolin-2(1H)-one + reduced acceptor
Other name(s): quinaldic acid 4-oxidoreductase
Systematic name: quinoline-4-carboxylate:acceptor 2-oxidoreductase (hydroxylating)
Comments: quinoline-4-carboxylate, quinoline, 4-methyl quinoline and 4-chloroquinoline will also serve as substrates for the enzyme from Agrobacterium sp. 1B. 1,4-Benzoquinone, iodonitrotetrazolium chloride, thionine, menadione and 2,6-dichlorophenolindophenol will act as electron acceptors.
References:
1. Sauter, M., Tshisuaka, B., Fetzner, S., Lingens, F. Microbial metabolism of quinoline and related compounds. XX. Quinaldic acid 4-oxidoreductase from Pseudomonas sp. AK-2 compared to other procaryotic molybdenum-containing hydroxylases. Biol. Chem. Hoppe Seyler 374 (1993) 1037-1046. [PMID: 8292263]
2. Fetzner, S., Lingens, F. Microbial metabolism of quinoline and related compounds. XVIII. Purification and some properties of the molybdenum- and iron-containing quinaldic acid 4-oxidoreductase from Serratia marcescens 2CC-1. Biol. Chem. Hoppe Seyler 374 (1993) 363-376. [PMID: 8357532]
EC 1.5.1.27
Recommended name: 1,2-dehydroreticulinium reductase (NADPH2)
Reaction: 1,2-dehydroreticulinium + NADPH2 = (R)-reticuline + NADP
Other name(s): 1,2-dehydroreticulinium ion reductase
Systematic name: (R)-reticuline:NADP oxidoreductase
Comments: reduces the 1,2-dehydroreticulinium ion to (R)-reticuline, which is a direct precursor of morphinan alkaloids in the poppy plant. The enzyme does not catalyse the reverse reaction to any significant extent under physiological conditions.
References:
1. De-Eknamkul, W., Zenk, M.H. Purification and properties of 1,2-dehydroreticulinium reductase from Papaver somniferum seedlings. Phytochemistry 31 (1992) 813-821.
EC 1.5.1.28
Recommended name: opine dehydrogenase
Reaction: (2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate + NAD + H2O = L-2-aminopentanoic acid + pyruvate + NADH2
Systematic name: (2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate dehydrogenase (NAD, L-aminopentanoate-forming)
Comments: in the forward direction, the enzyme from Arthrobacter sp. acts also on secondary amine dicarboxylates such as N-(1-carboxyethyl)methionine and N-(1-carboxyethyl)phenylalanine. Dehydrogenation forms an imine, which dissociates to the amino acid and pyruvate. In the reverse direction, the enzyme acts also on neutral amino acids as an amino donor. They include L-amino acids such as 2-aminopentanoic acid, 2-aminobutyric acid, 2-aminohexanoic acid, 3-chloroalanine, O-acetylserine, methionine, isoleucine, valine, phenylalanine, leucine and alanine. The amino acceptors include 2-oxoacids such as pyruvate, oxaloacetate, glyoxylate and 2-oxobutyrate.
References:
1. Asano, Y., Yamaguchi, K., Kondo, K. A new NAD+-dependent opine dehydrogenase from Arthrobacter sp. strain 1C. J. Bacteriol. 171 (1989) 4466-4471. [PMID: 2753861]
2. Dairi, T., Asano, Y. Cloning, nucleotide sequencing, and expression of an opine dehydrogenase gene from Arthrobacter sp. strain 1C. Appl. Environ. Microbiol. 61 (1995) 3169-3171. [PMID: 7487048]
3. Kato, Y., Yamada, H., Asano, Y. Stereoselective synthesis of opine-type secondary amine carboxylic acids by a new enzyme opine dehydrogenase. Use of recombinant enzymes. J. Mol. Catalysis B: Enzymatic 1 (1996) 151-160.
EC 1.5.3.12
Recommended name: dihydrobenzophenanthridine oxidase
Reaction:
dihydrosanguinarine + O2 = sanguinarine + H2O2;
dihydrochelirubine + O2 = chelirubine + H2O2;
dihydromacarpine + O2 = macarpine + H2O2
Systematic name: dihydrobenzophenanthridine:oxygen oxidoreductase
Comments: a CuII enzyme found in higher plants that produces oxidized forms of the benzophenanthridine alkaloids
References:
1. Schumacher, H.-M., Zenk, M.H. Partial purification and characterization of dihydrobenzophenanthridine oxidase from Eschscholtzia tenuifolia cell suspension cultures. Plant Cell Reports 7 (1988) 43-46.
2. Arakawa, H., Clark, W.G., Psenak. M., Coscia, C.J. Purification and characterization of dihydrobenzophenanthridine oxidase from elicited Sanguinaria canadensis cell cultures. Arch. Biochem. Biophys. 299 (1992) 1-7. [PMID: 1444440]
EC 1.5.99.10
Recommended name: dimethylamine dehydrogenase
Reaction: dimethylamine + H2O + acceptor = methylamine + formaldehyde + reduced acceptor
Systematic name: dimethylamine:(acceptor) oxidoreductase
References:
1. Yang, C.C., Packman, L.C., Scrutton, N.S. The primary structure of Hyphomicrobium X dimethylamine dehydrogenase. Relationship to trimethylamine dehydrogenase and implications for substrate recognition. Eur. J. Biochem. 232 (1995) 264-271. [PMID: 7556160]
EC 1.6.5.5
Recommended name: NADPH2:quinone reductase
Reaction: NADPH2 + quinone = NADP + semiquinone
Systematic name: NADPH2:quinone oxidoreductase
Comments: a zinc enzyme, specific for NADPH2. Catalyses the one-electron reduction of certain quinones; orthoquinones are the best substrates. Dicoumarol (cf. EC 1.6.99.2) and nitrofurantoin are competitive inhibitors with respect to the quinone substrate. In some mammals the enzyme is abundant in the lens of the eye, where it is identified with the protein ζ-crystallin.
References:
1. Rao, P.V., Krishna, C.M., Zigler, J.S., Jr. Identification and characterization of the enzymatic activity of zeta-crystallin from guinea pig lens. A novel NADPH:quinone oxidoreductase. J. Biol. Chem. 267 (1992) 96-102. [PMID: 1370456]
EC 1.8.99.4
Recommended name: phosphoadenosine-phosphosulfate reductase
Reaction: 5-phosphoadenosine 3-phosphosulfate (PAPS) + reduced thioredoxin = phosphoadenosine phosphate (PAP) + oxidized thioredoxin + sulfite
Other name(s): PAPS reductase, thioredoxin-dependent; PAPS reductase; thioredoxin:adenosine 3'-phosphate 5'-phosphosulfate reductase; 3'-phosphoadenylylsulfate reductase; thioredoxin:3'-phospho-adenylylsulfate reductase
Systematic name: adenosine 3'-phosphate 5'-phosphosulfate:thioredoxin oxidoreductase (sulfite-forming)
Comments: specific for PAPS. The enzyme from E. coli will use thioredoxins from other species.
References:
1. Berendt, U., Haverkamp, T., Prior, A., Schwenn, J.D. Reaction mechanism of thioredoxin: 3'-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis. Eur. J. Biochem. 233 (1995) 347-356. [PMID: 7588765]
EC 1.12.99.3
Recommended name: hydrogen:quinone oxidoreductase
Reaction: H2 + Menaquinone = reduced menaquinone
Other name(s): hydrogen:menaquinone oxidoreductase
Systematic name: hydrogen:quinone oxidoreductase
Comments: also catalyses the reduction of water-soluble quinones (e.g. 2,3-dimethylnaphthoquinone) or viologen dyes (benzyl viologen or methyl viologen) by H2.
References:
1. Dross, F., Geisler, V., Lenger, R., Theis, F., Krafft, T., Fahrenholz, F., Kojro, E., Duchene, A., Tripier, D., Juvenal, K. The quinone-reactive Ni/Fe-hydrogenase of Wolinella succinogenes. Eur. J. Biochem. 206 (1992) 93-102. [PMID: 1587288] [An erratum appears in Eur. J. Biochem. 214 (1993) 949-50 - PMID: 8319698].
EC 1.12.99.4
Recommended name: N5,N10-methenyltetrahydromethanopterin hydrogenase
Reaction: N5,N10-methenyltetrahydromethanopterin + H2 = N5,N10-methylenetetrahydromethanopterin + H+
Other name(s): H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase
Systematic name: hydrogen:N5,N10-methenyltetraydromethanopterin oxidoreductase
Comments: does not catalyse the reduction of artificial dyes by H2. Does not by itself catalyse a H2/H+ exchange reaction. Does not contain nickel or iron-sulfur clusters.
References:
1. Zirngibl, C., Hedderich, R., Thauer, R.K. N5,N10-Methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum has hydrogenase activity. FEBS Lett. 261 (1990) 112-116.
2. Klein, A., Fernandez, V.M., Thauer, R.K. H2-Forming N5,N10-methylenetetrahydromethanopterin dehydrogenase: mechanism of H2-formation analyzed using hydrogen isotopes. FEBS Lett. 368 (1995) 203-206.
EC 1.13.99.5
Recommended name: 3,4-dihydroxyquinoline 2,4-dioxygenase
Reaction: quinoline-3,4-diol + O2 = N-formylanthranilate + CO
Other name(s): (1H)-3-hydroxy-4-oxoquinoline 2,4-dioxygenase; 3-hydroxy-4-oxo-1,4-dihydroquinoline 2,4-dioxygenase; 3-hydroxy-4(1H)-one, 2,4-dioxygenase; quinoline-3,4-diol 2,4-dioxygenase
Systematic name: quinoline-3,4-diol 2,4-dioxygenase (carbon monoxide-forming)
Comments: fission of two C-C bonds: 2,4-Dioxygenolytic cleavage with concomitant release of carbon monoxide. Since quinolin-4-ols exist largely as their quinolin-4(1H)-one tautomers, the substrate can also be called 3-hydroxy-4-oxo-1,4-dihydroquinoline. Although the enzyme from Pseudomonas putida appears to be highly specific for this substrate, that from Arthrobacter also acts on 2-methylquinoline-3,4-diol to form N-acetylanthranilate.
References:
1. Bauer, I., De Beyer, A., Tsisuaka, B., Fetzner, S., Lingens, F. A novel type of oxygenolytic ring cleavage: 2,4-Oxygenation and decarbonylation of 1H-3-hydroxy-4-oxoquinaldine and 1H-3-hydroxy-4-oxoquinoline. FEMS Microbiol. Lett. 117 (1995) 299-304.
EC 1.14.12.14
Recommended name: 2-aminobenzenesulfonate 2,3-dioxygenase
Reaction: 2-aminobenzenesulfonate + NADH2 + O2 = 2,3-dihydroxybenzenesulfonate + NH3+ + NAD
Other name(s): 2-aminosulfobenzene 2,3-dioxygenase
Systematic name: 2-aminobenzenesulfonate, NADH:oxygen oxidoreductase (2,3-hydroxylating, ammonia-forming)
References:
1. Junker, F., Field, J.A., Bangerter, F., Ramsteiner, K., Kohler, H.-P., Joannou, C.L., Mason, J.R., Leisinger, T., Cook, A.M. Dioxygenation and spontaneous deamination of 2-aminobenzene sulphonic acid in Alcaligenes sp. strain O-1 with subsequent meta ring cleavage and spontaneous desulphonation to 2-hydroxymuconic acid. Biochem. J. 300 (1994) 429-436. [PMID: 8002948]
2. Junker, F., Leisinger, T., Cook, A.M. 3-Sulphocatechol dioxygenase and other dioxygenases (1.13.11.2 and 1.14.12.-) in the degradative pathways of 2-aminobenzenesulphonic, benzenesulphonic and 4-toluenesulphonic acids in Alcaligenes sp. strain O-1. J. Gen. Microbiol. 140 (1994) 1713-1722. [PMID: 8075807]
EC 1.14.12.15
Recommended name: terephthalate 1,2-dioxygenase
Reaction: terephthalate + NADH2 + H+ + O2 = (1R,6S)-dihydroxycyclohexa-2,4-diene-1,4-dicarboxylate + NAD
Other name(s): benzene-1,4-dicarboxylate 1,2-dioxygenase; 1,4-dicarboxybenzoate 1,2-dioxygenase
Systematic name: benzene-1,4-dicarboxylate, NADH:oxygen oxidoreductase (1,2-hydroxylating)
Comments: has been shown to contain a Rieske [2Fe-2S] cluster
References:
1. Schläfli, H.R., Weiss, M.A., Leisinger, T., Cook, A.M. Terephthalate 1,2-dioxygenase system from Comamonas testosteroni T-2; purification and some properties of the oxygenase component. J. Bacteriol. 176 (1994) 6644-6652. [PMID: 7961417]
EC 1.14.12.16
Recommended name: 2-hydroxyquinoline 5,6-dioxygenase
Reaction: quinolin-2-ol + NADH2 + O2 = 2,5,6-trihydroxy-5,6-dihydroquinoline + NAD
Other name(s): 2-oxo-1,2-dihydroquinoline 5,6-dioxygenase; 2-hydroxyquinoline 5,6-dioxygenase; quinolin-2-ol 5,6-dioxygenase, quinolin-2(1H)-one 5,6-dioxygenase
Systematic name: quinolin-2-ol, NADH:oxygen oxidoreductase (5,6-hydroxylating)
Comments: 3-methylquinolin-2-ol, quinolin-8-ol and quinolin-2,8-diol are also substrates. Quinolin-2-ols exist largely as their quinolin-2(1H)-one tautomers
References:
1. Schach, S.B., Tshisuaka, B., Fetzner, S., Lingens, F. Quinoline 2-oxidoreductase and 2-oxo-1,2-dihydroquinoline 5,6-dioxygenase from Comamonas testosteroni 63. The first two enzymes in quinoline and 3-methylquinoline degradation. Eur. J. Biochem. 232 (1995) 536-544. [PMID: 7556204]
EC 1.14.13.54
Recommended name: ketosteroid monooxygenase
Reaction: ketosteroid + NADPH2 + O2 = steroid ester/lactone + NADP + H2O
Other name(s): steroid-ketone monooxygenase; progesterone, NADPH2:oxygen oxidoreductase (20-hydroxylating, ester-producing); 17α-hydroxyprogesterone, NADPH2:oxygen oxidoreductase (20-hydroxylating, side-chain cleaving); androstenedione, NADPH2:oxygen oxidoreductase (17-hydroxylating, lactonizing)
Systematic name: ketosteroid, NADPH2:oxygen oxidoreductase (20-hydroxylating, ester-producing/20-hydroxylating, side-chain cleaving/17-hydroxylating, lactonizing)
Comments: a single FAD-containing enzyme catalyses three types of monooxygenase (Baeyer-Villiger oxidation) reaction.
(1) The oxidative esterification of a number of derivatives of pregn-4-ene-3,20-dione (progesterone) to produce the corresponding 17α-hydroxysteroid 17-acetate ester, such as testosterone acetate: progesterone + NADPH2 + O2 = testosterone acetate + NADP + H2O.
(2) The oxidative lactonization of a number of derivatives of androst-4-ene-3,17-dione (androstenedione) to produce the 13,17-secoandrosteno-17,13α-lactone, such as 3-oxo-13,17-secoandrost-4-eno-17,13α-lactone (testololactone): androstenedione + NADPH2 + O2 = testololactone + NADP + H2O.
(3) The oxidative cleavage of the 17β-side-chain of 17α-hydroxypregn-4-ene-3,20-dione (17α-hydroxyprogesterone) to produce androst-4-ene-3,17-dione (androstenedione) and acetate: 17α-hydroxyprogesterone + NADPH2 + O2 = androstenedione + acetate + NADP + H2O.
Reaction 1 is also catalysed by EC 1.14.99.4, and reactions 2 and 3 correspond to that catalysed by EC 1.14.99.12. The possibility that a single enzyme is responsible for the reactions ascribed to EC 1.14.99.4 and EC 1.14.99.12 in other tissues cannot be excluded.
References:
1. Katagiri, M., Itagaki, E. A steroid ketone monooxygenase from Cylindrocarpon radicicola. in Chemistry and Biochemistry of Flavoenzymes, (Müller, F., ed.) (1991) pp. 102-108, CRC Press, Florida.
2. Itagaki, E. Studies on a steroid monooxygenase from Cylindrocarpon radicicola ATCC 11011. Purification and characterization. J. Biochem. (Tokyo) 99 (1986) 815-824. [PMID: 3486863]
3. Itagaki, E. Studies on a steroid monooxygenase from Cylindrocarpon radicicola ATCC11011. Oxygenative lactonization of androstenedione to testololactone. J. Biochem. (Tokyo) 99 (1986) 825-832. [PMID: 3486864]
EC 1.14.13.55
Recommended name: protopine 6-monooxygenase
Reaction: protopine + NADPH2 + O2 = 6-hydroxyprotopine + NADP + H2O
Other name(s): protopine 6-hydroxylase
Systematic name: protopine, NADPH2:oxygen oxidoreductase (6-hydroxylating)
Comments: a heme-thiolate protein (P-450) involved in benzophenanthridine alkaloid synthesis in higher plants.
References:
1. Tanahashi, T., Zenk, M.H. Elicitor induction and characterization of microsomal protopine-6-hydroxylase, the central enzyme in benzophenanthridine alkaloid biosynthesis. Phytochemistry 29 (1990) 1113-1122.
EC 1.14.13.56
Recommended name: dihydrosanguinarine 10-monooxygenase
Reaction: dihydrosanguinarine + NADPH2 + O2 = 10-hydroxydihydrosanguinarine + NADP + H2O
Other name(s): dihydrosanguinarine 10-hydroxylase
Systematic name: dihydrosanguinarine, NADPH:oxygen oxidoreductase (10-hydroxylating),
Comments: a heme-thiolate protein (P-450) involved in benzophenanthridine alkaloid synthesis in higher plants.
References:
1. De-Eknamkul, W., Tanahashi, T., Zenk, M.H. Enzymic 10-hydroxylation and 10-O-methylation of dihydrosanguinarine in dihydrochelirubine formation by Eschscholtzia. Phytochemistry 31 (1992) 2713-2717.
EC 1.14.13.57
Recommended name: dihydrochelirubine 12-monooxygenase
Reaction:dihydrochelirubine + NADPH2 + O2 = 12-hydroxydihydrochelirubine + NADP + H2O
Other name(s): dihydrochelirubine 12-hydroxylase
Systematic name: dihydrochelirubine, NADPH2:oxygen oxidoreductase (12-hydroxylating)
Comments: a heme-thiolate protein (P-450)
References:
1. Kammerer, L., De-Eknamkul, W., Zenk, M.H. Enzymic 12-hydroxylation and 12-O-methylation of dihydrochelirubine in dihydromacarpine formation by Thalictrum bulgaricum. Phytochemistry 36 (1994) 1409-1416.
EC 1.14.13.58
Recommended name: benzoyl-CoA 3-monooxygenase
Reaction: benzoyl-CoA + NADPH2 + O2 = 3-hydroxybenzoyl-CoA + NADP + H2O
Other name(s): benzoyl-CoA 3-hydroxylase
Systematic name: benzoyl-CoA, NADPH2:oxygen oxidoreductase (3-hydroxylating)
Comments: the enzyme from the denitrifying bacterium Pseudomonas KB740 catalyses a flavin-requiring reaction (FAD or FMN). Benzoate is not a substrate.
References:
1. Niemetz, R., Altenschmidt, U., Herrmann, H., Fuchs, G. Benzoyl-coenzyme-A 3-monooxygenase, a flavin-dependent hydroxylase. Purification, some properties and its role in aerobic benzoate oxidation via gentisate in a denitrifying bacterium. Eur. J. Biochem. 227 (1995) 161-168. [PMID: 7851381]
EC 1.14.13.59
Recommended name: L-lysine 6-monooxygenase (NADPH2)
Reaction: L-lysine + NADPH2 + O2 = N6-hydroxy-L-lysine + NADP + H2O
Other name(s): lysine N6-hydroxylase
Systematic name: L-lysine, NADPH2:oxygen oxidoreductase (6-hydroxylating)
Comments: a flavoprotein (FAD). The enzyme from strain EN 222 of E. coli is highly specific for L-lysine; L-ornithine and L-homolysine are, for example, not substrates. A lysine monooxygenase (EC 1.13.12.10) from this organism has been reported to catalyse the same hydroxylation without the involvement of NAD(P)H2
References:
1. Plattner, H.J., Pfefferle, P., Romaguera, A., Waschutza, S., Diekmann, H. Isolation and some properties of lysine N6-hydroxylase from Escherichia coli strain EN222. Biol Met. 2 (1989) 1-5. [PMID: 2518519]
2. Macheroux, P., Plattner, H.J., Romaguera, A.and Diekmann, H. FAD and substrate analogs as probes for lysine N6-hydroxylase from Escherichia coli EN 222. Eur. J. Biochem. 213 (1993) 995-1002. [PMID: 8504838]
3. Thariath, A.M., Fatum, K.L., Valvano, M.A., Viswanatha, T. Physico-chemical characterization of a recombinant cytoplasmic form of lysine: N6-hydroxylase. Biochim. Biophys. Acta 1203 (1993) 27-35. [PMID: 8218389]
EC 1.14.13.60
Recommended name: 27-hydroxycholesterol 7α-monooxygenase
Reaction: 27-hydroxycholesterol + NADPH2 + O2 = 7α,27-dihydroxycholesterol + NADP + H2O
Other name(s): 27-hydroxycholesterol 7α-hydroxylase
Systematic name: 27-hydroxycholesterol, NADPH2:oxygen oxidoreductase (7α-hydroxylating)
Comments: a heme-thiolate protein (P-450). The enzyme from mammalian liver differs from cholesterol 7α-monooxygenase (EC 1.14.13.17) in having no activity towards cholesterol.
References:
1. Kumiko, O.M., Budai, K., Javitt, N.B. Cholesterol and 27-hydroxycholesterol 7α-hydroxylation: evidence for two different enzymes. J. Lipid Res. 34 (1993) 581-588.
EC 1.14.13.61
Recommended name: 2-hydroxyquinoline 8-monooxygenase
Reaction: quinolin-2-ol + NADH2 + O2 = quinolin-2,8-diol + NAD + H2O
Other name(s): 2-oxo-1,2-dihydroquinoline 8-monooxygenase
Systematic name: quinolin-2(1H)-one, NADH2:oxygen oxidoreductase (8-oxygenating)
Comments: requires iron. Quinolin-2-ol exists largely as the quinolin-2(1H)-one tautomer.
References:
1. Rosche, B., Tshisuaka, B., Fetzner, S., Lingens, F. 2-Oxo-1,2-dihydroquinoline 8-monooxygenase, a two-component enzyme system from Pseudomonas putida 86. J. Biol. Chem. 270 (1995) 17836-17842. [PMID: 7629085]
EC 1.14.13.62
Recommended name: 4-hydroxyquinoline 3-monooxygenase
Reaction: quinolin-4-ol + NADH2 + O2 = quinolin-3,4-diol + NAD + H2O
Other name(s): quinolin-4(1H)-one 3-monooxygenase
Systematic name: quinolin-4(1H)-one, NADH2:oxygen oxidoreductase (3-oxygenating)
Comments: quinolin-4-ol exists largely as the quinolin-4(1H)-one tautomer.
References:
1. Block, D.W., Lingens, F. Microbial metabolism of quinoline and related compounds. XIV. Purification and properties of 1H-3-hydroxy-4-oxoquinoline oxygenase, a new estradiol cleavage enzyme from Pseudomonas putida strain 33/1. Biol. Chem. Hoppe Seyler 373 (1992) 249-254. [PMID: 1627263]
EC 1.14.13.63
Recommended name: 3-hydroxyphenylacetate 6-hydroxylase
Reaction: 3-hydroxyphenylacetate + NAD(P)H2 + O2 = 2,5-dihydroxyphenylacetate (homogentisate) + NAD(P) + H2O
Other name(s): 3-hydroxyphenylacetate 6-monooxygenase
Systematic name: 3-hydroxyphenylacetate, NAD(P)H2:oxygen oxidoreductase (6-hydroxylating)
Comments: 3-hydroxyphenylacetate 6-hydroxylase from Flavobacterium sp. is highly specific for 3-hydroxyphenylacetate and uses NADH2 and NADPH2 as electron donors with similar efficiency.
References:
1. van Berkel, W.H.J., van den Tweel, W.J.J. Purification and characterisation of 3-hydroxyphenylacetate 6-hydroxylase: a novel FAD-dependent monooxygenase from a Flavobacterium sp. Eur. J. Biochem. 201 (1991) 585-592. [PMID: 1935954]
EC 1.14.13.64
Recommended name: 4-hydroxybenzoate 1-hydroxylase
Reaction: 4-hydroxybenzoate + NAD(P)H2 + O2 = hydroquinone + NAD(P) + H2O + CO2
Other name(s): 4-hydroxybenzoate 1-monooxygenase
Systematic name: 4-hydroxybenzoate, NAD(P)H2:oxygen oxidoreductase (1-hydroxylating, decarboxylating)
Comments: requires FAD. The enzyme from Candida parapsilosis is specific for 4-hydroxybenzoate derivatives and prefers NADH2 to NADPH2 as electron donor.
References:
1. van Berkel, W.J.H., Eppink, M.H.M., Middelhoven, W.J., Vervoort, J., Rietjens, I.M.C.M. Catabolism of 4-hydroxybenzoate in Candida parapsilosis proceeds through initial oxidative decarboxylation by a FAD-dependent 4-hydroxybenzoate 1-hydroxylase. FEMS Microbiol. Lett. 121 (1994) 207-216. [PMID: 7926672]
EC 1.14.13.65
Recommended name: 2-hydroxyquinoline 8-monooxygenase
Reaction: quinolin-2-ol + NADH2 + O2 = quinolin-2,8-diol + NAD
Other name(s): 2-oxo-1,2-dihydroquinoline 5,6-dioxygenase
Systematic name: quinolin-2-ol, NADH2:oxygen oxidoreductase (8-hydroxylating)
Comments: 3-methyl-quinolin-2-ol is also a substrate. Quinolin-2-ols exist largely as the quinolin-2(1H)-one tautomers.
References:
1. Schach, S.B., Tshisuaka, B., Fetzner, S., Lingens, F. Quinoline 2-oxidoreductase and 2-oxo-1,2-dihydroquinoline 5,6-dioxygenase from Comamonas testosteroni 63. The first two enzymes in quinoline and 3-methylquinoline degradation. Eur. J. Biochem. 232 (1995) 536-544. [PMID: 7556204]
EC 1.14.13.66
Recommended name: 2-hydroxycyclohexanone 2-monooxygenase
Reaction: 2-hydroxycyclohexan-1-one + NADPH2 + O2 = 6-hydroxyhexan-6-olide + NADP + H2O
Systematic name: 2-hydroxycyclohexan-1-one, NADPH2:oxygen 2-oxidoreductase (1,2-lactonizing)
Comment: the product decomposes spontaneously to 6-oxohexanoic acid (adipic semialdehyde).
References
1. Davey, J.F., Trudgill, P.W. The metabolism of trans-cyclohexan-1,2-diol by an Acinetobacter species. Eur. J. Biochem. 74 (1977) 115-127. [PMID: 856571]
EC 1.14.99.30
Recommended name: carotene 7,8-desaturase
Reaction: neurosporene + AH2 + O2 = lycopene + A + 2 H2O
Other name(s): ζ-carotene desaturase
Systematic name: carotene, hydrogen-donor:oxygen oxidoreductase.
Comments: also acts on ζ-carotene twice to give lycopene and converts β-zeacarotene to γ-carotene, and pro-ζ-carotene to prolycopene (via double reaction)
References:
1. Albrecht, M., Linden, H., Sandmann, G. Biochemical characterization of purified ζ-carotene desaturase from Anabaena PCC 7120 after expression in E. coli. Eur. J. Biochem. 236 (1996) 115-120. [PMID: 8617254]
EC 1.97.1.4
Recommended name: formate acetyltransferase activating enzyme
Reaction: S-adenosyl-L-methionine + dihydroflavodoxin + Formate acetyltransferase-glycine = 5'-deoxyadenosine + methionine + flavodoxin + formate acetyltransferase-glycine-2-yl radical
Other name(s): PFL activase; PFL-glycine:S-adenosyl-L-methionine H transferase (flavodoxin-oxidizing, S-adenosyl-L-methionine-cleaving)
Systematic name: formate acetyltransferase-glycine dihydroflavodoxin:S-adenosyl-L-methionine oxidoreductase (S-adenosyl-L-methionine cleaving)
Comments: an iron-sulfur protein. A single glycine residue in formate C-acetyltransferase (EC 2.3.1.54) is oxidized to the corresponding radical by transfer of H from its CH2 into AdoMet with concomitant cleavage of the latter. The reaction requires FeII. The flavodoxin may be in the partially reduced, radical form.
References:
1. Frey, M., Rothe, M., Wagner, A.F.V., Knappe, J. Adenosylmethionine-dependent synthesis of the glycyl radical in pyruvate formate-lyase by abstraction of the glycine C-2 pro-S-hydrogen atom. J. Biol. Chem. 269 (1994) 12432-12437.
AMENDMENTS TO EXISTING ENTRIES
The alterations listed below are necessitated from nomenclature changes, the need to account for additions to the list, to clarify existing descriptions or to correct errors that have been brought to our attention. Where references are cited by number, these refer to those given in the 1992 edition of the Enzyme List .
Deleted entry: 1.3.1.50: tetrahydroxynaphthalene reductase. Transferred to EC 1.1.1.252
Deleted entry: 1.14.12.6: 2-hydroxycyclohexanone 2-monooxygenase. Transferred to EC 1.14.13.66
EC 1.1.1.168
Recommended name: 2-dehydropantolactone reductase (A-specific)
Reaction: (R)-pantolactone + NADP = 2-dehydropantolactone + NADPH2
Other name(s): 2-dehydropantoyl-lactone reductase (A-specific)
Systematic name: (R)-pantolactone:NADP oxidoreductase (A-specific)
Comments: the yeast enzyme differs from that from E. coli (EC 1.1.1.214), which is specific for the B-face of NADP, and in receptor requirements from EC 1.1.99.26.
References:
1. King, H.L., Jr., Wilken, D.R. Separation and preliminary studies on 2-ketopantoyl lactone and 2-ketopantoic acid reductases of yeast. J. Biol. Chem. 247 (1972) 4096-4098.
2. Wilken, D.R., King, H.L.,Jr., Dyar, R.E. Ketopantoic acid and ketopantoyl lactone reductases. Stereospecificity of transfer of hydrogen from reduced nicotinamide adenine dinucleotide phosphate. J. Biol. Chem. 250 (1975) 2311-2314. [PMID: 234966]
EC 1.1.1.214
Recommended name: 2-dehydropantolactone reductase (B-specific)
Reaction: (R)-pantolactone + NADP = 2-dehydropantolactone + NADPH2
Other name(s): 2-dehydropantoyl-lactone reductase (B-specific)
Systematic name: (R)-pantolactone:NADP oxidoreductase (B-specific)
Comments: The E. coli enzyme differs from that from yeast (EC 1.1.1.168), which is specific for the A-face of NADP, and in receptor requirements from EC 1.1.99.26.
References:
1. Wilken, D.R., King, H.L., Jr., Dyar, R.E. Ketopantoic acid and ketopantoyl lactone reductases. Stereospecificity of transfer of hydrogen from reduced nicotinamide adenine dinucleotide phosphate. J. Biol. Chem. 250 (1975) 2311-2314. [PMID: 234966]
EC 1.5.3.9
Recommended name: reticuline oxidase
Reaction: (S)-reticuline + O2 = (S)-scoulerine + H2O2
Other name(s): berberine-bridge-forming enzyme; tetrahydroprotoberberine synthase
Systematic name: (S)-reticuline:oxygen oxidoreductase (methylene-bridge-forming)
Comments: the product of the reaction, (S)-scoulerine, is a precursor of protopine, protoberberine and benzophenanthridine alkaloid biosynthesis in plants. Acts on (S)-reticuline and related compounds, converting the N-methyl group into the methylene bridge ('berberine bridge') of (S)-tetrahydroprotoberberines
References:
1. Dittrich, H., Kutchan, T.M. Molecular cloning, expression and induction of the berberine bridge enzyme, an enzyme essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack. Proc. Natl. Acad. Sci. U.S.A. 88 (1991) 9969-9973. [PMID: 1946465]
2. Kutchan, T.M., Dittrich, H. Characterization and mechanism of the berberine bridge enzyme, a covalently flavinylated oxidase of benzophenanthridine alkaloid biosynthesis in higher plants. J. Biol. Chem. 270 (1995) 24475-24481. [PMID: 7592663]
EC 1.7.7.1
Recommended name: ferredoxin-nitrite reductase
Reaction: ammonia + 2 H2O + 6 oxidized ferredoxin = nitrite + 6 reduced ferredoxin + 7 H+
Systematic name: ammonia:ferredoxin oxidoreductase
Comments: an iron protein. Contains siroheme and [4Fe-4S]clusters.
References:
1. Joy, K.W., Hageman, R.H. The purification and properties of nitrite reductase from higher plants, and its dependence on ferredoxin. Biochem. J. 100 (1966) 263-273. [PMID: 4381617]
2. Ramirez, J.M., Del Campo, F.F., Paneque, A., Losada, M. Ferredoxin-nitrite reductase from spinach. Biochim. Biophys. Acta 118 (1966) 58-71. [PMID: 5954064]
3. Zumft, W.G., Paneque, A., Aparicio, P.J., Losada, M. Mechanism of nitrate reduction in Chlorella. Biochem. Biophys. Res. Commun. 36 (1969) 980-986. [PMID: 4390523]
EC 1.7.99.1
Recommended name: hydroxylamine reductase
Reaction: ammonia + H2O + acceptor = hydroxylamine + reduced acceptor
Systematic name: ammonia:(acceptor) oxidoreductase
Comments: a flavoprotein. Reduced pyocyanine, methylene blue and flavins act as donors for the reduction of hydroxylamine.
References:
1. Taniguchi, H., Mitsui, H., Nakamura, K., Egami, F. Hydroxylamine reductase. Ann. Acad. Sci. Fenn. Ser. A II 60 (1955) 200-215.
2. Walker, G.C., Nicholas, D.J.D. Hydroxylamine reductase from Pseudomonas aeruginosa. Biochim. Biophys. Acta 49 (1961) 361-368.
EC 1.7.99.6
Recommended name: nitrous-oxide reductase
Reaction: nitrogen + H2O + acceptor = nitrous oxide + reduced acceptor
Systematic name: nitrogen:(acceptor) oxidoreductase (N2O-forming)
Comments: a copper protein. Reduced viologens or methylene blue act as donors for the reduction of nitrous oxide.
References:
1. Coyle, C.L., Zumft, W.G., Kroneck, P.M.H., Körner, H., Jakob, W. Nitrous oxide reductase from denitrifying Pseudomonas perfectomarina. Purification and properties of a novel multicopper enzyme. Eur. J. Biochem. 153 (1985) 459-467. [PMID: 3000778]
EC 1.7.99.7
Recommended name: nitric-oxide reductase
Reaction: nitrous oxide + acceptor + H2O = 2 nitric oxide + reduced acceptor
Systematic name: nitrous-oxide:(acceptor) oxidoreductase (nitric oxide-forming)
Comments: a heterodimer of cytochromes b and c. Phenazine methosulfate can act as acceptor
References:
1. Heiss, B., Frunzke, K., Zumpft, W.G. Formation of the N-N bond from nitric oxide by a membrane-bound cytochrome bc complex of nitrate-respiring (denitrifying) Pseudomonas stutzeri. J. Bacteriol. 171 (1989) 3288-3297. [PMID: 2542222]
EC 1.11.1.6
Recommended name: catalase
Reaction: 2 H2O2 = O2 + 2 H2O
Systematic name: hydrogen-peroxide:hydrogen-peroxide oxidoreductase
Comments: a hemoprotein. This enzyme can also act as a peroxidase (EC 1.11.1.7) for which several organic substances, especially ethanol, can act as a hydrogen donor. A manganese protein containing MnIII in the resting state, which also belongs here, is often called pseudocatalase. Enzymes from some microorganisms, such as Penicillium simplicissimum, which exhibit both catalase and peroxidase activity, have sometimes been referred to as catalase-peroxidase.
References:
1. Herbert, D., Pinsent, J. Crystalline bacterial catalase. Biochem. J. 43 (1948) 193-202 and 203.
2. Herbert, D., Pinsent, J. Crystalline human erythrocyte catalase. Biochem. J. 43 (1948) 203-205.
3. Keilin, D., Hartree, E.F. Coupled oxidation of alcohol. Proc. R. Soc. Lond. B Biol. Sci. 119 (1936) 141-159.
4. Kono, Y., Fridovich, I. Isolation and characterization of the pseudocatalase of Lactobacillus plantarum. J. Biol. Chem. 258 (1983) 6015-6019. [PMID: 6853475]
5. Nicholls, P., Schonbaum, G.R. Catalases, in The Enzymes, 2nd edn (Boyer, P.D., Lardy, H., Myrbäck, K., eds.) vol.8 (1963) p.147, Academic Press, New York.
6. Sumner, J.B., Dounce, A.L. Crystalline catalase. J. Biol. Chem. 121 (1937) 417-424.
7. Fraaije, M.W., Roubroeks, H.P., van Berkel, W.H.J. Purification and characterization of an intracellular catalase-peroxidase from Penicillium simplicissimum. Eur. J. Biochem. 235 (1996) 192-198. [PMID: 8631329]
EC 1.13.11.2
Recommended name: catechol 2,3-dioxygenase
Reaction: catechol + O2 = 2-hydroxymuconate semialdehyde
Other name(s): metapyrocatechase; cato2ase
Systematic name: catechol:oxygen 2,3-oxidoreductase (decyclicizing)
Comments: requires FeII. Formerly EC 1.13.1.2. The enzyme from Alcaligines sp. strain O-1 has also been shown to catalyse the reaction: 2,3-dihydroxybenzenesulphonate + O2 + H2O = 2-hydroxymuconate + bisulfite and has been referred to as 2,3-dihydroxybenzenesulphonate 2,3-dioxygenase. Further work will be necessary to show whether or not this is a distinct enzyme.
References:
1. Junker, F., Field, J.A., Bangerter, F., Ramsteiner, K., Kohler, H.-P., Joannou, C.L., Mason, J.R., Leisinger, T., Cook, A.M. Dioxygenation and spontaneous deamination of 2-aminobenzene sulphonic acid in Alcaligines sp. strain O-1 with subsequent meta ring cleavage and spontaneous desulphonation to 2-hydroxymuconic acid. Biochem. J. 300 (1994) 429-436. [PMID: 8002948]
2. Junker, F., Leisinger, T., Cook, A.M. 3-Sulphocatechol dioxygenase and other dioxygenases (EC 1.13.11.2 and EC 1.14.12.-) in the degradative pathways of 2-aminobenzenesulphonic, benzenesulphonic and 4-toluenesulphonic acids in Alcaligines sp. strain O-1. J. Gen. Microbiol. 140 (1994) 1713-1722. [PMID: 8075807]
3. Hayaishi, O. Direct oxygenation of O2, oxygenases, in The Enzymes, 2nd edn. (Boyer, P.D., Lardy, H., Myrbäck, K., eds.) vol. 8, Academic Press, New York (1963) p.353.
4. Kojima, Y., Itada, N., Hayaishi, O. Metapyrocatechase: a new catechol-cleaving enzyme. J. Biol. Chem. 236 (1961) 2223-2238.
5. Nozaki, M., Kagamiyama, H., Hayaishi, O. Metapyrocatechase. I. Purification, crystallization and some properties. Biochem. Z. 338 (1963) 582-590.
EC 1.13.12.10
Recommended name: L-lysine 6-monooxygenase
Reaction: L-lysine + O2 = N6-hydroxy-L-lysine + H2O
Comments: involved in the synthesis of aerobactin from lysine in a strain of E. coli. EC 1.14.13.59 catalyses the same hydroxylation, but with the oxidation of NADPH2.
References:
1. De Lorenzo, V., Bindereif, A., Paw, B.H., Neilands, J.B. Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in Escherichia coli K-12. J. Bacteriol. 165 (1986) 570-578. [PMID: 2935523]
EC 1.14.13.2
Recommended name: 4-hydroxybenzoate 3-monooxygenase
Reaction: 4-hydroxybenzoate + NADPH2 + O2 = protocatechuate + NADP + H2O
Other name(s): p-hydroxybenzoate hydroxylase
Systematic name: 4-hydroxybenzoate,NADPH2:oxygen oxidoreductase (3-hydroxylating)
Comments: a flavoprotein (FAD). Most enzymes from Pseudomonas are highly specific for NADPH2 (cf. EC 1.14.13.33).
References:
1. Hosokawa, K., Stanier, R.Y. Crystallization and properties of p-hydroxybenzoate hydroxylase from Pseudomonas putida. J. Biol. Chem. 241 (1966) 2453-2460. [PMID: 4380381]
2. Howell, L.G., Spector, T., Massey, V. Purification and properties of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. J. Biol. Chem. 247 (1972) 4340-4350. [PMID: 4402514]
3. Spector, T., Massey, V. Studies on the effector specificity of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. J. Biol. Chem. 247 (1972) 4679-4687. [PMID: 4402938]
4. Spector, T., Massey, V. p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Evidence for an oxygenated flavin intermediate. J. Biol. Chem. 247 (1972) 5632-5636. [PMID: 4403446]
5. Spector, T., Massey, V. p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Reactivity with oxygen. J. Biol. Chem. 247 (1972) 7123-7127. [PMID: 4404745]
6. Seibold, B., Matthes, M., Eppink, M.H., Lingens, F., Van Berkel, W.J., Muller, R. 4-Hydroxybenzoate hydroxylase from Pseudomonas sp. CBS3. Purification, characterization, gene cloning, sequence analysis and assignment of structural features determining the coenzyme specificity. Eur. J. Biochem. 239 (1996) 469-478. [PMID: 8706756]
EC 1.14.13.33
Recommended name: 4-hydroxybenzoate 3-monooxygenase [NAD(P)H2]
Reaction: 4-hydroxybenzoate + NAD(P)H2 + O2 = 3,4-dihydroxybenzoate + NAD(P) + H2O
Systematic name: 4-hydroxybenzoate,NAD(P)H2:oxygen oxidoreductase (3-hydroxylating)
Comments: a flavoprotein (FAD). The enzyme from Corynebacterium cyclohexanicum is highly specific for 4-hydroxybenzoate, but uses NADH2 and NADPH2 at approximately equal rates (cf. EC 1.14.13.2). It is less specific for NADPH2 than EC 1.14.13.2.
References:
1. Fujii, T., Kaneda, T. Purification and properties of NADH/NADPH-dependent p-hydroxybenzoate hydroxylase from Corynebacterium cyclohexanicum. Eur. J. Biochem. 147 (1985) 97-104. [PMID: 3971979]
2. Seibold, B., Matthes, M., Eppink, M.H., Lingens, F., Van Berkel, W.J., Muller, R. 4-Hydroxybenzoate hydroxylase from Pseudomonas sp. CBS3. Purification, characterization, gene cloning, sequence analysis and assignment of structural features determining the coenzyme specificity. Eur. J. Biochem. 239 (1996) 469-478. [PMID: 8706756]
EC 1.14.99.4
Recommended name: progesterone monooxygenase
Reaction: progesterone + AH2 + O2 = testosterone acetate + A + H2O
Systematic name: progesterone, hydrogen-donor:oxygen oxidoreductase (hydroxylating)
Comments: has a wide specificity. A single enzyme from Cylindrocarpon radicicola (EC 1.14.13.54) catalyses both this reaction and that catalysed by EC 1.14.99.12.
References:
1. Rahim, M.A., Sih, C.J. Mechanisms of steroid oxidation by microorganisms. XI. Enzymatic cleavage of the pregnane side chain. J. Biol. Chem. 241 (1965) 3615-3623.
Change necessitated by new entry: (EC 1.14.13.54)
EC 1.14.99.12
Recommended name: androst-4-ene-3,17-dione monooxygenase
Reaction: androst-4-ene-3,17-dione + AH2 + O2 = 3-oxo-13,17-secoandrost-4-eno-17,13α-lactone + A + H2O
Other name(s): 4-androstene-3,17-dione monooxygenase
Systematic name: androst-4-ene-3,17-dione, hydrogen-donor:oxygen oxidoreductase (13-hydroxylating, lactonizing)
Comments: has a wide specificity. A single enzyme from Cylindrocarpon radicicola (EC 1.14.13.54) catalyses both this reaction and that catalysed by EC 1.4.99.4.
References:
1. Prairie, R.L., Talalay, P. Enzymatic formation of testololactone.Biochemistry 2 (1963) 203-208.
Change necessitated by new entry: (EC 1.14.13.54)
EC 1.14.99.18
Recommended name: CMP-N-acetylneuraminate monooxygenase
Reaction: CMP-N-acetylneuraminate + AH2 + O2 = CMP-N-glycoloylneuraminate + A + H2O
Other name(s)N-acetylneuraminate,hydrogen-donor:oxygen oxidoreductase (N-acetyl-hydroxylating); N-acetylneuraminate monooxygenase
Comments: the enzyme is specific for the sugar nucleotide cytidine-5'-monophosphate-N-acetylneuraminic acid and not for the free N-acetylneuraminic acid sugar. The enzyme accepts reducing equivalents from NADH2 and, to a lesser extent, from NADPH2 via the cytochrome b5 reductase: cytochrome b5 system. Requires FeII. Either NADPH2 or ascorbate can act as AH2.
References
1. Schauer, R. [Biosynthesis of N-glycoloylneuraminic acid by an ascorbic acid- or NADP-dependent N-acetyl hydroxylating "N-acetylneuraminate: O2-oxidoreductase" in homogenates of porcine submaxillary gland]. Hoppe-Seyler's Z. Physiol. Chem. 351 (1970) 783-791. [German] [PMID: 4317421]
2. Schauer, R., Wember, M. Hydroxylation and O-acetylation of N-acetylneuraminic acid bound to glycoproteins of isolated subcellular membranes from porcine and bovine submaxillary glands. Hoppe-Seyler's Z. Physiol. Chem. 352 (1971) 1282-1290. [PMID: 5128308]
3. Shaw, L., Schneckenburger, P., Carlsen, J., Christiansen, K., Schauer, R. Mouse liver cytidine-5'-monophosphate-N-acetylneuraminic acid hydroxylase. Catalytic function and regulation. Eur. J. Biochem. 206 (1992) 269-277. [PMID: 1587278]