The Enzyme Database

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EC 1.1.3.14     
Accepted name: catechol oxidase (dimerizing)
Reaction: 4 catechol + 3 O2 = 2 dibenzo[1,4]dioxin-2,3-dione + 6 H2O
For diagram of reaction, 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. [PMID: 14217190]
[EC 1.1.3.14 created 1972]
 
 
EC 1.2.1.10     
Accepted name: acetaldehyde dehydrogenase (acetylating)
Reaction: acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
For diagram of 3-phenylpropanoate catabolism, click here, for diagram of catechol catabolism (meta ring cleavage), click here and for diagram of cinnamate catabolism, click here
Other name(s): aldehyde dehydrogenase (acylating); ADA; acylating acetaldehyde dehyrogenase; DmpF; BphJ
Systematic name: acetaldehyde:NAD+ oxidoreductase (CoA-acetylating)
Comments: Also acts, more slowly, on glycolaldehyde, propanal and butanal. In several bacterial species this enzyme forms a bifunctional complex with EC 4.1.3.39, 4-hydroxy-2-oxovalerate aldolase. The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 1.2.1.87, propanal dehydrogenase (propanoylating). Involved in the meta-cleavage pathway for the degradation of phenols, methylphenols and catechols. NADP+ can replace NAD+ but the rate of reaction is much slower [3].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9028-91-5
References:
1.  Burton, R.M. and Stadtman, E.R. The oxidation of acetaldehyde to acetyl coenzyme A. J. Biol. Chem. 202 (1953) 873–890. [PMID: 13061511]
2.  Smith, L.T. and Kaplan, N.O. Purification, properties, and kinetic mechanism of coenzyme A-linked aldehyde dehydrogenase from Clostridium kluyveri. Arch. Biochem. Biophys. 203 (1980) 663–675. [DOI] [PMID: 7458347]
3.  Powlowski, J., Sahlman, L. and Shingler, V. Purification and properties of the physically associated meta-cleavage pathway enzymes 4-hydroxy-2-ketovalerate aldolase and aldehyde dehydrogenase (acylating) from Pseudomonas sp. strain CF600. J. Bacteriol. 175 (1993) 377–385. [DOI] [PMID: 8419288]
4.  Baker, P., Pan, D., Carere, J., Rossi, A., Wang, W. and Seah, S.Y.K. Characterization of an aldolase-dehydrogenase complex that exhibits substrate channeling in the polychlorinated biphenyls degradation pathway. Biochemistry 48 (2009) 6551–6558. [DOI] [PMID: 19476337]
5.  Baker, P., Hillis, C., Carere, J. and Seah, S.Y.K. Protein-protein interactions and substrate channeling in orthologous and chimeric aldolase-dehydrogenase complexes. Biochemistry 51 (2012) 1942–1952. [DOI] [PMID: 22316175]
[EC 1.2.1.10 created 1961, modified 2006, modified 2011]
 
 
EC 1.2.1.85     
Accepted name: 2-hydroxymuconate-6-semialdehyde dehydrogenase
Reaction: 2-hydroxymuconate-6-semialdehyde + NAD+ + H2O = (2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
For diagram of catechol catabolism (meta ring cleavage), click here
Glossary: 2-hydroxymuconate-6-semialdehyde = (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate
Other name(s): xylG (gene name); praB (gene name)
Systematic name: 2-hydroxymuconate-6-semialdehyde:NAD+ oxidoreductase
Comments: This substrate for this enzyme is formed by meta ring cleavage of catechol (EC 1.13.11.2, catechol 2,3-dioxygenase), and is an intermediate in the bacterial degradation of several aromatic compounds. Has lower activity with benzaldehyde [1]. Activity with NAD+ is more than 10-fold higher than with NADP+ [3]. cf. EC 1.2.1.32, aminomuconate-semialdehyde dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Inoue, J., Shaw, J.P., Rekik, M. and Harayama, S. Overlapping substrate specificities of benzaldehyde dehydrogenase (the xylC gene product) and 2-hydroxymuconic semialdehyde dehydrogenase (the xylG gene product) encoded by TOL plasmid pWW0 of Pseudomonas putida. J. Bacteriol. 177 (1995) 1196–1201. [DOI] [PMID: 7868591]
2.  Orii, C., Takenaka, S., Murakami, S. and Aoki, K. Metabolism of 4-amino-3-hydroxybenzoic acid by Bordetella sp. strain 10d: A different modified meta-cleavage pathway for 2-aminophenols. Biosci. Biotechnol. Biochem. 70 (2006) 2653–2661. [DOI] [PMID: 17090920]
3.  Kasai, D., Fujinami, T., Abe, T., Mase, K., Katayama, Y., Fukuda, M. and Masai, E. Uncovering the protocatechuate 2,3-cleavage pathway genes. J. Bacteriol. 191 (2009) 6758–6768. [DOI] [PMID: 19717587]
[EC 1.2.1.85 created 2012]
 
 
EC 1.3.1.19     
Accepted name: cis-1,2-dihydrobenzene-1,2-diol dehydrogenase
Reaction: cis-1,2-dihydrobenzene-1,2-diol + NAD+ = catechol + NADH + H+
Other name(s): cis-benzene glycol dehydrogenase; cis-1,2-dihydrocyclohexa-3,5-diene (nicotinamide adenine dinucleotide) oxidoreductase;
Systematic name: cis-1,2-dihydrobenzene-1,2-diol:NAD+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 51923-03-6
References:
1.  Axcell, B.C. and Geary, P.J. The metabolism of benzene by bacteria. Purification and some properties of the enzyme cis-1,2-dihydroxycyclohexa-3,5-diene (nicotinamide adenine dinucleotide) oxidoreductase (cis-benzene glycol dehydrogenase). Biochem. J. 136 (1973) 927–934. [PMID: 4362337]
2.  Gibson, D.T., Koch, J.R. and Kallio, R.E. Oxidative degradation of aromatic hydrocarbons by microorganisms. I. Enzymatic formation of catechol from benzene. Biochemistry 7 (1968) 2653–2662. [PMID: 4298226]
[EC 1.3.1.19 created 1972]
 
 
EC 1.3.1.20     
Accepted name: trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
Reaction: trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
Other name(s): dihydrodiol dehydrogenase
Systematic name: trans-1,2-dihydrobenzene-1,2-diol:NADP+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37255-32-6
References:
1.  Ayengar, P.K., Hayaishi, O., Nakajima, M. and Tomida, I. Enzymic aromatization of 3,5-cyclohexadiene-1,2-diol. Biochim. Biophys. Acta 33 (1959) 111–119. [DOI] [PMID: 13651190]
[EC 1.3.1.20 created 1972]
 
 
EC 1.3.1.25     
Accepted name: 1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase
Reaction: (1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+ = catechol + CO2 + NADH + H+
For diagram of benzoate metabolism, click here
Other name(s): 3,5-cyclohexadiene-1,2-diol-1-carboxylate dehydrogenase; 3,5-cyclohexadiene-1,2-diol-1-carboxylic acid dehydrogenase; dihydrodihydroxybenzoate dehydrogenase; DHBDH; cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase; 2-hydro-1,2-dihydroxybenzoate dehydrogenase; cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate:NAD+ oxidoreductase; dihydrodihydroxybenzoate dehydrogenase; (1R,6R)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate:NAD+ oxidoreductase (decarboxylating)
Systematic name: (1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate:NAD+ oxidoreductase (decarboxylating)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 60496-16-4
References:
1.  Reiner, A.M. Metabolism of aromatic compounds in bacteria. Purification and properties of the catechol-forming enzyme, 3,5-cyclohexadiene-1,2-diol-1-carboxylic acid (NAD+) oxidoreductase (decarboxylating). J. Biol. Chem. 247 (1972) 4960–4965. [PMID: 4341530]
2.  Neidle, E., Hartnett, C., Ornston, L.N., Bairoch, A., Rekik, M. and 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. [DOI] [PMID: 1740120]
[EC 1.3.1.25 created 1976, modified 2004 (EC 1.3.1.55 created 1999, incorporated 2004)]
 
 
EC 1.3.1.59      
Deleted entry: 1,2-dihydroxy-3-methyl-1,2-dihydrobenzoate dehydrogenase. No evidence in the paper cited that the enzyme exists
[EC 1.3.1.59 created 2000, deleted 2006]
 
 
EC 1.3.1.66     
Accepted name: cis-dihydroethylcatechol dehydrogenase
Reaction: cis-1,2-dihydro-3-ethylcatechol + NAD+ = 3-ethylcatechol + NADH + H+
Systematic name: cis-1,2-dihydro-3-ethylcatechol:NAD+ oxidoreductase
Comments: Involved in the ethylbenzene degradation pathway in bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD
References:
1.  Gibson, D.T., Gschwendt, B., Yeh, W.K. and Kobal, V.M. Initial reactions in the oxidation of ethylbenzene by Pseudomonas putida. Biochemistry 12 (1973) 1520–1528. [PMID: 4699984]
[EC 1.3.1.66 created 2000]
 
 
EC 1.3.1.67     
Accepted name: cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate dehydrogenase
Reaction: cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate + NAD(P)+ = 4-methylcatechol + NAD(P)H + CO2
Systematic name: cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate:NAD(P)+ oxidoreductase (decarboxylating)
Comments: Involved in the p-xylene degradation pathway in bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD
References:
1.  Whited, G.M., McCombie, W.R., Kwart, L.D. and Gibson, D.T. Identification of cis-diols as intermediates in the oxidation of aromatic acids by a strain of Pseudomonas putida that contains a TOL plasmid. J. Bacteriol. 166 (1986) 1028–1039. [DOI] [PMID: 3711022]
[EC 1.3.1.67 created 2000]
 
 
EC 1.3.1.68     
Accepted name: 1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate dehydrogenase
Reaction: 1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate + NAD+ = 3-methylcatechol + NADH + CO2
Systematic name: 1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate:NAD+ oxidoreductase (decarboxylating)
Comments: Involved in the o-xylene degradation pathway in bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD
References:
1.  Higson, F.K. and Focht, D.D. Degradation of 2-methylbenzoic acid by Pseudomonas cepacia MB2. Appl. Environ. Microbiol. 58 (1992) 194–200. [PMID: 1371658]
[EC 1.3.1.68 created 2000]
 
 
EC 1.3.1.119     
Accepted name: chlorobenzene dihydrodiol dehydrogenase
Reaction: (1R,2R)-3-chlorocyclohexa-3,5-diene-1,2-diol + NAD+ = 3-chlorocatechol + NADH + H+
Other name(s): tecB (gene name)
Systematic name: (1R,2R)-3-chlorocyclohexa-3,5-diene-1,2-diol:NAD+ oxidoreductase
Comments: This bacterial enzyme can transform various dihydrodiols of chlorobenzenes into the respective catechols, including the dihydrodiols of mono-, di-, tri-, and tetra-chlorinated benzenes. It also accepts the dihydrodiols of various chlorotoluenes. Substrates for the enzyme are generated by the broad spectrum EC 1.14.12.26, chlorobenzene dioxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Spiess, E. and Gorisch, H. Purification and characterization of chlorobenzene cis-dihydrodiol dehydrogenase from Xanthobacter flavus 14p1. Arch. Microbiol. 165 (1996) 201–205. [PMID: 8599538]
2.  Pollmann, K., Beil, S. and Pieper, D.H. Transformation of chlorinated benzenes and toluenes by Ralstonia sp. strain PS12 tecA (tetrachlorobenzene dioxygenase) and tecB (chlorobenzene dihydrodiol dehydrogenase) gene products. Appl. Environ. Microbiol. 67 (2001) 4057–4063. [PMID: 11526005]
3.  Pollmann, K., Wray, V. and Pieper, D.H. Chloromethylmuconolactones as critical metabolites in the degradation of chloromethylcatechols: recalcitrance of 2-chlorotoluene. J. Bacteriol. 187 (2005) 2332–2340. [PMID: 15774876]
[EC 1.3.1.119 created 2018]
 
 
EC 1.10.3.1     
Accepted name: catechol oxidase
Reaction: 2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O
Glossary: catechol = 1,2-benzenediol
Other name(s): diphenol oxidase; o-diphenolase; polyphenol oxidase; pyrocatechol oxidase; dopa oxidase; catecholase; o-diphenol:oxygen oxidoreductase; o-diphenol oxidoreductase
Systematic name: 1,2-benzenediol:oxygen oxidoreductase
Comments: A type 3 copper protein that catalyses exclusively the oxidation of catechol (i.e., o-diphenol) to the corresponding o-quinone. The enzyme also acts on a variety of substituted catechols. It is different from tyrosinase, EC 1.14.18.1, which can catalyse both the monooxygenation of monophenols and the oxidation of catechols.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9002-10-2
References:
1.  Brown, F.C. and Ward, D.N. Preparation of a soluble mammalian tyrosinase. J. Am. Chem. Soc. 79 (1957) 2647–2648.
2.  Dawson, C.R. and Tarpley, W.B. The copper oxidases. In: Sumner, J.B. and Myrbäck, K. (Ed.), The Enzymes, 1st edn, vol. 2, Academic Press, New York, 1951, pp. 454–498.
3.  Gregory, R.P.F. and Bendall, D.S. The purification and some properties of the polyphenol oxidse from tea (Camellia sinensis L.). Biochem. J. 101 (1966) 569–581. [PMID: 16742427]
4.  Mason, H.S. Structures and functions of the phenolase complex. Nature (Lond.) 177 (1956) 79–81. [PMID: 13288597]
5.  Mayer, A.M. and Harel, E. Polyphenol oxidases in plants. Phytochemistry 18 (1979) 193–215.
6.  Patil, S.S. and Zucker, M. Potato phenolases. Purification and properties. J. Biol. Chem. 240 (1965) 3938–3943. [PMID: 5842066]
7.  Pomerantz, S.H. 3,4-Dihydroxy-L-phenylalanine as the tyrosinase cofactor. Occurrence in melanoma and binding constant. J. Biol. Chem. 242 (1967) 5308–5314. [PMID: 4965136]
8.  Robb, D.A. `Tyrosinase. In: Lontie, R. (Ed.), Copper Proteins and Copper Enzymes, vol. 2, CRC Press, Boca Raton, FL, 1984, pp. 207–240.
9.  Gerdemann, C., Eicken, C. and Krebs, B. The crystal structure of catechol oxidase: new insight into the function of type-3 copper proteins. Acc. Chem. Res. 35 (2002) 183–191. [DOI] [PMID: 11900522]
[EC 1.10.3.1 created 1961, deleted 1972, reinstated 1978]
 
 
EC 1.10.3.6     
Accepted name: rifamycin-B oxidase
Reaction: rifamycin B + O2 = rifamycin O + H2O2
Other name(s): rifamycin B oxidase
Systematic name: rifamycin-B:oxygen oxidoreductase
Comments: Acts also on benzene-1,4-diol and, more slowly, on some other p-quinols. Not identical with EC 1.10.3.1 (catechol oxidase), EC 1.10.3.2 (laccase), EC 1.10.3.4 (o-aminophenol oxidase) or EC 1.10.3.5 (3-hydroxyanthranilate oxidase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 84932-52-5
References:
1.  Han, M.H., Seong, B.-L., Son, H.-J. and Mheen, T.-I. Rifamycin B oxidase from Monocillium spp., a new type of diphenol oxidase. FEBS Lett. 151 (1983) 36–40. [DOI] [PMID: 6825839]
[EC 1.10.3.6 created 1986]
 
 
EC 1.11.1.7     
Accepted name: peroxidase
Reaction: 2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O
Other name(s): lactoperoxidase; guaiacol peroxidase; plant peroxidase; Japanese radish peroxidase; horseradish peroxidase (HRP); soybean peroxidase (SBP); extensin peroxidase; heme peroxidase; oxyperoxidase; protoheme peroxidase; pyrocatechol peroxidase; scopoletin peroxidase; Coprinus cinereus peroxidase; Arthromyces ramosus peroxidase
Systematic name: phenolic donor:hydrogen-peroxide oxidoreductase
Comments: Heme proteins with histidine as proximal ligand. The iron in the resting enzyme is Fe(III). They also peroxidize non-phenolic substrates such as 3,3′,5,5′-tetramethylbenzidine (TMB) and 2,2′-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS). Certain peroxidases (e.g. lactoperoxidase, SBP) oxidize bromide, iodide and thiocyanate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9003-99-0
References:
1.  Kenten, R.H. and Mann, P.J.G. Simple method for the preparation of horseradish peroxidase. Biochem. J. 57 (1954) 347–348. [PMID: 13172193]
2.  Morrison, M., Hamilton, H.B. and Stotz, E. The isolation and purification of lactoperoxidase by ion exchange chromatography. J. Biol. Chem. 228 (1957) 767–776. [PMID: 13475358]
3.  Paul, K.G. Peroxidases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 8, Academic Press, New York, 1963, pp. 227–274.
4.  Tagawa, K., Shin, M. and Okunuki, K. Peroxidases from wheat germ. Nature (Lond.) 183 (1959) 111. [PMID: 13622706]
5.  Theorell, H. The preparation and some properties of crystalline horse-radish peroxidase. Ark. Kemi Mineral. Geol. 16A No. 2 (1943) 1–11.
6.  Farhangrazi, Z.S., Copeland, B.R., Nakayama, T., Amachi, T., Yamazaki, I. and Powers, L.S. Oxidation-reduction properties of compounds I and II of Arthromyces ramosus peroxidase. Biochemistry 33 (1994) 5647–5652. [PMID: 8180190]
7.  Aitken, M.D. and Heck, P.E. Turnover capacity of coprinus cinereus peroxidase for phenol and monosubstituted phenol. Biotechnol. Prog. 14 (1998) 487–492. [DOI] [PMID: 9622531]
8.  Dunford, H.B. Heme peroxidases, Wiley-VCH, New York, 1999, pp. 33–218.
9.  Torres, E and Ayala, M. Biocatalysis based on heme peroxidases, Springer, Berlin, 2010, pp. 7–110.
[EC 1.11.1.7 created 1961, modified 2011]
 
 
EC 1.13.1.1      
Transferred entry: Now EC 1.13.11.1, catechol 1,2-dioxygenase
[EC 1.13.1.1 created 1961 as EC 1.99.2.2, transferred 1965 to EC 1.13.1.1, deleted 1972]
 
 
EC 1.13.1.2      
Transferred entry: Now EC 1.13.11.2, catechol 2,3-dioxygenase
[EC 1.13.1.2 created 1965, deleted 1972]
 
 
EC 1.13.11.1     
Accepted name: catechol 1,2-dioxygenase
Reaction: catechol + O2 = cis,cis-muconate
For diagram of benzoate metabolism, click here
Other name(s): catechol-oxygen 1,2-oxidoreductase; 1,2-pyrocatechase; catechase; catechol 1,2-oxygenase; catechol dioxygenase; pyrocatechase; pyrocatechol 1,2-dioxygenase; CD I; CD II
Systematic name: catechol:oxygen 1,2-oxidoreductase
Comments: Requires Fe3+. Involved in the metabolism of nitro-aromatic compounds by a strain of Pseudomonas putida.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 9027-16-1
References:
1.  Hayaishi, O. Direct oxygenation by O2, oxygenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 8, Academic Press, New York, 1963, pp. 353–371.
2.  Hayaishi, O., Katagiri, M. and Rothberg, S. Studies on oxygenases: pyrocatechase. J. Biol. Chem. 229 (1957) 905–920. [PMID: 13502352]
3.  Sistrom, W.R. and Stanier, R.Y. The mechanism of formation of β-ketoadipic acid by bacteria. J. Biol. Chem. 210 (1954) 821–836. [PMID: 13211620]
4.  Zeyer, J., Kocher, H.P. and Timmis, N. Influence of para-substituents on the oxidative metabolism of o-nitrophenols by Pseudomonas putida B2. Appl. Environ. Microbiol. 52 (1986) 334–339. [PMID: 3752997]
[EC 1.13.11.1 created 1961 as EC 1.99.2.2, transferred 1965 to EC 1.13.1.1, transferred 1972 to EC 1.13.11.1]
 
 
EC 1.13.11.2     
Accepted name: catechol 2,3-dioxygenase
Reaction: catechol + O2 = 2-hydroxymuconate-6-semialdehyde
For diagram of catechol catabolism (meta ring cleavage), click here
Glossary: 2-hydroxymuconate-6-semialdehyde = (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate
Other name(s): 2,3-pyrocatechase; catechol 2,3-oxygenase; catechol oxygenase; metapyrocatechase; pyrocatechol 2,3-dioxygenase; xylE (gene name); catechol:oxygen 2,3-oxidoreductase (decyclizing)
Systematic name: catechol:oxygen 2,3-oxidoreductase (ring-opening)
Comments: Requires FeII. The enzyme initiates the meta-cleavage pathway of catechol degradation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 9029-46-3
References:
1.  Hayaishi, O. Direct oxygenation by O2, oxygenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 8, Academic Press, New York, 1963, pp. 353–371.
2.  Kojima, Y., Itada, N. and Hayaishi, O. Metapyrocatechase: a new catechol-cleaving enzyme. J. Biol. Chem. 236 (1961) 2223–2228. [PMID: 13757654]
3.  Nozaki, M., Kagamiyama, H. and Hayaishi, O. Metapyrocatechase. I. Purification, crystallization and some properties. Biochem. Z. 338 (1963) 582–590. [PMID: 14087325]
4.  Nakai, C., Hori, K., Kagamiyama, H., Nakazawa, T. and Nozaki, M. Purification, subunit structure, and partial amino acid sequence of metapyrocatechase. J. Biol. Chem. 258 (1983) 2916–2922. [PMID: 6826545]
5.  Junker, F., Field, J.A., Bangerter, F., Ramsteiner, K., Kohler, H.-P., Joannou, C.L., Mason, J.R., Leisinger, T. and Cook, A.M. Oxygenation and spontaneous deamination of 2-aminobenzenesulphonic 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]
6.  Junker, F., Leisinger, T. and Cook, A.M. 3-Sulphocatechol 2,3-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 Alcaligenes sp. strain O-1. Microbiology 140 (1994) 1713–1722. [DOI] [PMID: 8075807]
[EC 1.13.11.2 created 1965 as EC 1.13.1.2, transferred 1972 to EC 1.13.11.2, modified 1999, modified 2013]
 
 
EC 1.13.11.16     
Accepted name: 3-carboxyethylcatechol 2,3-dioxygenase
Reaction: (1) 3-(2,3-dihydroxyphenyl)propanoate + O2 = (2Z,4E)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate
(2) (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + O2 = (2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate
For diagram of 3-phenylpropanoate catabolism, click here and for diagram of cinnamate catabolism, click here
Glossary: (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate = trans-2,3-dihydroxycinnamate
Other name(s): 2,3-dihydroxy-β-phenylpropionic dioxygenase; 2,3-dihydroxy-β-phenylpropionate oxygenase; 3-(2,3-dihydroxyphenyl)propanoate:oxygen 1,2-oxidoreductase; 3-(2,3-dihydroxyphenyl)propanoate:oxygen 1,2-oxidoreductase (decyclizing)
Systematic name: 3-(2,3-dihydroxyphenyl)propanoate:oxygen 1,2-oxidoreductase (ring-opening)
Comments: An iron protein. This enzyme catalyses a step in the pathway of phenylpropanoid compounds degradation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 105503-63-7
References:
1.  Dagley, S., Chapman, P.J. and Gibson, D.T. The metabolism of β-phenylpropionic acid by an Achromobacter. Biochem. J. 97 (1965) 643–650. [PMID: 5881653]
2.  Lam, W. W. Y and Bugg, T. D. H. Chemistry of extradiol aromatic ring cleavage: isolation of a stable dienol ring fission intermediate and stereochemistry of its enzymatic hydrolytic clevage. J. Chem. Soc., Chem. Commun. 10 (1994) 1163–1164.
3.  Díaz, E., Ferrández, A. and García, J.L. Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12. J. Bacteriol. 180 (1998) 2915–2923. [PMID: 9603882]
[EC 1.13.11.16 created 1972, modified 2011, modified 2012]
 
 
EC 1.13.11.25     
Accepted name: 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione 4,5-dioxygenase
Reaction: 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione + O2 = 3-hydroxy-5,9,17-trioxo-4,5:9,10-disecoandrosta-1(10),2-dien-4-oate
Other name(s): steroid 4,5-dioxygenase; 3-alkylcatechol 2,3-dioxygenase; 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione:oxygen 4,5-oxidoreductase (decyclizing)
Systematic name: 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione:oxygen 4,5-oxidoreductase (ring-opening)
Comments: Requires Fe2+. Also acts on 3-isopropylcatechol and 3-tert-butyl-5-methylcatechol.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 37256-63-6
References:
1.  Gibson, D.T., Wang, K.C., Sih, C.J. and Whitlock, J.H. Mechanisms of steroid oxidation by microorganisms. IX. On the mechanism of ring A cleavage in the degradation of 9,10-seco steroids by microorganisms. J. Biol. Chem. 241 (1966) 551–559. [PMID: 5908121]
[EC 1.13.11.25 created 1972]
 
 
EC 1.13.11.36     
Accepted name: chloridazon-catechol dioxygenase
Reaction: 5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone + O2 = 5-amino-4-chloro-2-(2-hydroxymuconoyl)-3(2H)-pyridazinone
Other name(s): 5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone 1,2-oxidoreductase (decyclizing)
Systematic name: 5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone 1,2-oxidoreductase (ring-opening)
Comments: An iron protein, requiring additional Fe2+. Not identical with EC 1.13.11.1 (catechol 1,2-dioxygenase), EC 1.13.11.2 (catechol 2,3-dioxygenase) or EC 1.13.11.5 (homogentisate 1,2-dioxygenase). Involved in the breakdown of the herbicide chloridazon.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 82869-32-7
References:
1.  Müller, R, Haug, S., Eberspächer, J. and Lingens, F. Catechol-2,3-Dioxygenase aus Pyrazon-abbauenden Bakterien. Hoppe-Seyler's Z. Physiol. Chem. 358 (1977) 797–805. [PMID: 19349]
2.  Müller, R., Schmitt, S. and Lingens, F. A novel non-heme iron-containing dioxygenase. Chloridazon-catechol dioxygenase from Phenylobacterium immobilis DSM 1986. Eur. J. Biochem. 125 (1982) 579–584. [DOI] [PMID: 6811270]
[EC 1.13.11.36 created 1984]
 
 
EC 1.13.11.37     
Accepted name: hydroxyquinol 1,2-dioxygenase
Reaction: hydroxyquinol + O2 = maleylacetate
For diagram of 4-nitrophenol metabolism, click here
Glossary: hydroxyquinol = 1,2,4-trihydroxybenzene
maleylacetate = (2Z)-4-oxohex-2-enedioate
Other name(s): hydroxyquinol dioxygenase; benzene-1,2,4-triol:oxygen 1,2-oxidoreductase (decyclizing); benzene-1,2,4-triol:oxygen 1,2-oxidoreductase (ring-opening)
Systematic name: hydroxyquinol:oxygen 1,2-oxidoreductase (ring-opening)
Comments: An iron protein. Highly specific; catechol and pyrogallol are acted on at less than 1% of the rate at which hydroxyquinol is oxidized.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 91847-14-2
References:
1.  Sze, I.S.-Y. and Dagley, S. Properties of salicylate hydroxylase and hydroxyquinol 1,2-dioxygenase purified from Trichosporon cutaneum. J. Bacteriol. 159 (1984) 353–359. [PMID: 6539772]
2.  Ferraroni, M., Seifert, J., Travkin, V.M., Thiel, M., Kaschabek, S., Scozzafava, A., Golovleva, L., Schlomann, M. and Briganti, F. Crystal structure of the hydroxyquinol 1,2-dioxygenase from Nocardioides simplex 3E, a key enzyme involved in polychlorinated aromatics biodegradation. J. Biol. Chem. 280 (2005) 21144–21154. [DOI] [PMID: 15772073]
3.  Hatta, T., Nakano, O., Imai, N., Takizawa, N. and Kiyohara, H. Cloning and sequence analysis of hydroxyquinol 1,2-dioxygenase gene in 2,4,6-trichlorophenol-degrading Ralstonia pickettii DTP0602 and characterization of its product. J. Biosci. Bioeng. 87 (1999) 267–272. [DOI] [PMID: 16232466]
[EC 1.13.11.37 created 1989, modified 2013]
 
 
EC 1.13.11.39     
Accepted name: biphenyl-2,3-diol 1,2-dioxygenase
Reaction: biphenyl-2,3-diol + O2 = 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
Other name(s): 2,3-dihydroxybiphenyl dioxygenase; biphenyl-2,3-diol dioxygenase; bphC (gene name); biphenyl-2,3-diol:oxygen 1,2-oxidoreductase (decyclizing)
Systematic name: biphenyl-2,3-diol:oxygen 1,2-oxidoreductase (ring-opening)
Comments: Contains Fe2+ or Mn2+ [3]. This enzyme participates in the degradation pathway of biphenyl and PCB (poly chlorinated biphenyls), and catalyses the first ring cleavage step by incorporating two oxygen atoms into the catechol ring formed by EC 1.3.1.56, cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase.The enzyme from the bacterium Burkholderia xenovorans LB400 can also process catechol, 3-methylcatechol, and 4-methylcatechol, but less efficiently [1]. The enzyme from the carbazole-degrader Pseudomonas resinovorans strain CA10 also accepts 2′-aminobiphenyl-2,3-diol [5]. The enzyme from Ralstonia sp. SBUG 290 can also accept 1,2-dihydroxydibenzofuran and 1,2-dihydroxynaphthalene [4]. The enzyme is strongly inhibited by the substrate [1].Not identical with EC 1.13.11.2 catechol 2,3-dioxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 103679-58-9
References:
1.  Eltis, L.D., Hofmann, B., Hecht, H.J., Lunsdorf, H. and Timmis, K.N. Purification and crystallization of 2,3-dihydroxybiphenyl 1,2-dioxygenase. J. Biol. Chem. 268 (1993) 2727–2732. [PMID: 8428946]
2.  Uragami, Y., Senda, T., Sugimoto, K., Sato, N., Nagarajan, V., Masai, E., Fukuda, M. and Mitsu, Y. Crystal structures of substrate free and complex forms of reactivated BphC, an extradiol type ring-cleavage dioxygenase. J. Inorg. Biochem. 83 (2001) 269–279. [DOI] [PMID: 11293547]
3.  Hatta, T., Mukerjee-Dhar, G., Damborsky, J., Kiyohara, H. and Kimbara, K. Characterization of a novel thermostable Mn(II)-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase from a polychlorinated biphenyl- and naphthalene-degrading Bacillus sp. JF8. J. Biol. Chem. 278 (2003) 21483–21492. [DOI] [PMID: 12672826]
4.  Wesche, J., Hammer, E., Becher, D., Burchhardt, G. and Schauer, F. The bphC gene-encoded 2,3-dihydroxybiphenyl-1,2-dioxygenase is involved in complete degradation of dibenzofuran by the biphenyl-degrading bacterium Ralstonia sp. SBUG 290. J. Appl. Microbiol. 98 (2005) 635–645. [DOI] [PMID: 15715866]
5.  Iwata, K., Nojiri, H., Shimizu, K., Yoshida, T., Habe, H. and Omori, T. Expression, purification, and characterization of 2′-aminobiphenyl-2,3-diol 1,2-dioxygenase from carbazole-degrader Pseudomonas resinovorans strain CA10. Biosci. Biotechnol. Biochem. 67 (2003) 300–307. [PMID: 12728990]
[EC 1.13.11.39 created 1989]
 
 
EC 1.14.12.1     
Accepted name: anthranilate 1,2-dioxygenase (deaminating, decarboxylating)
Reaction: anthranilate + NAD(P)H + 2 H+ + O2 = catechol + CO2 + NAD(P)+ + NH3
For diagram of reaction, click here
Other name(s): anthranilate hydroxylase; anthranilic hydroxylase; anthranilic acid hydroxylase
Systematic name: anthranilate,NAD(P)H:oxygen oxidoreductase (1,2-hydroxylating, deaminating, decarboxylating)
Comments: Requires Fe2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 9059-17-0
References:
1.  Kobayashi, S. and Hayaishi, O. Anthranilic acid conversion to catechol (Pseudomonas). Methods Enzymol. 17A (1970) 505–510.
2.  Taniguchi, H., Hatanaka, M., Kuno, S., Hayaishi, O., Nakajima, M. and Kurihara, N. Enzymatic formation of catechol from anthranilic acid. J. Biol. Chem. 239 (1964) 2204–2211. [PMID: 14209949]
[EC 1.14.12.1 created 1972]
 
 
EC 1.14.12.3     
Accepted name: benzene 1,2-dioxygenase
Reaction: benzene + NADH + H+ + O2 = cis-cyclohexa-3,5-diene-1,2-diol + NAD+
For diagram of reaction, click here
Other name(s): benzene hydroxylase; benzene dioxygenase
Systematic name: benzene,NADH:oxygen oxidoreductase (1,2-hydroxylating)
Comments: A system, containing a reductase which is an iron-sulfur flavoprotein (FAD), an iron-sulfur oxygenase and ferredoxin. Requires Fe2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 9075-66-5
References:
1.  Gibson, D.T., Koch, J.R. and Kallio, R.E. Oxidative degradation of aromatic hydrocarbons by microorganisms. I. Enzymatic formation of catechol from benzene. Biochemistry 7 (1968) 2653–2662. [PMID: 4298226]
[EC 1.14.12.3 created 1972]
 
 
EC 1.14.12.13     
Accepted name: 2-halobenzoate 1,2-dioxygenase
Reaction: a 2-halobenzoate + NADH + H+ + O2 = catechol + a halide anion + NAD+ + CO2
For diagram of benzoate metabolism, click here, and for mechanism, click here
Other name(s): 2-chlorobenzoate 1,2-dioxygenase
Systematic name: 2-halobenzoate,NADH:oxygen oxidoreductase (1,2-hydroxylating, dehalogenating, decarboxylating)
Comments: A multicomponent enzyme system composed of a dioxygenase component and an electron transfer component. The latter contains FAD. The enzyme, characterized from the bacterium Burkholderia cepacia 2CBS, has a broad substrate specificity. Substrates include 2-fluorobenzoate, 2-chlorobenzoate, 2-bromobenzoate, and 2-iodobenzoate, which are processed in this order of preference.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 125268-83-9
References:
1.  Fetzner, S., Mueller, R. and Lingens, F. Degradation of 2-chlorobenzoate by Pseudomonas cepacia 2CBS. Biol. Chem. Hoppe-Seyler 370 (1989) 1173–1182. [PMID: 2610934]
2.  Fetzner, S., Muller, R. and Lingens, F. Purification and some properties of 2-halobenzoate 1,2-dioxygenase, a two-component enzyme system from Pseudomonas cepacia 2CBS. J. Bacteriol. 174 (1992) 279–290. [DOI] [PMID: 1370284]
3.  Haak, B., Fetzner, S. and Lingens, F. Cloning, nucleotide sequence, and expression of the plasmid-encoded genes for the two-component 2-halobenzoate 1,2-dioxygenase from Pseudomonas cepacia 2CBS. J. Bacteriol. 177 (1995) 667–675. [DOI] [PMID: 7530709]
[EC 1.14.12.13 created 1992, modified 2012]
 
 
EC 1.14.12.14     
Accepted name: 2-aminobenzenesulfonate 2,3-dioxygenase
Reaction: 2-aminobenzenesulfonate + NADH + H+ + O2 = 2,3-dihydroxybenzenesulfonate + NH3 + NAD+
For diagram of reaction, click here
Other name(s): 2-aminosulfobenzene 2,3-dioxygenase
Systematic name: 2-aminobenzenesulfonate,NADH:oxygen oxidoreductase (2,3-hydroxylating, ammonia-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 156621-16-8
References:
1.  Junker, F., Field, J.A., Bangerter, F., Ramsteiner, K., Kohler, H.-P., Joannou, C.L., Mason, J.R., Leisinger, T. and Cook, A.M. Oxygenation and spontaneous deamination of 2-aminobenzenesulphonic acid in Alcaligenes sp. strain O-1 with subsequent meta ring cleavage and spontaneous desulphonation to 2-hydroxymuconic acid. Biochem. J. 300 (1994) 429–436. [PMID: 8002948]
2.  Junker, F., Leisinger, T. and Cook, A.M. 3-Sulphocatechol 2,3-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 Alcaligenes sp. strain O-1. Microbiology 140 (1994) 1713–1722. [DOI] [PMID: 8075807]
[EC 1.14.12.14 created 1999]
 
 
EC 1.14.12.22     
Accepted name: carbazole 1,9a-dioxygenase
Reaction: 9H-carbazole + NAD(P)H + H+ + O2 = 2′-aminobiphenyl-2,3-diol + NAD(P)+
Other name(s): CARDO
Systematic name: 9H-carbazole,NAD(P)H:oxygen oxidoreductase (2,3-hydroxylating)
Comments: This enzyme catalyses the first reaction in the pathway of carbazole degradation. The enzyme attacks at the 1 and 9a positions of carbazole, resulting in the formation of a highly unstable hemiaminal intermediate that undergoes a spontaneous cleavage and rearomatization, resulting in 2′-aminobiphenyl-2,3-diol. In most bacteria the enzyme is a complex composed of a terminal oxygenase, a ferredoxin, and a ferredoxin reductase. The terminal oxygenase component contains a nonheme iron centre and a Rieske [2Fe-2S] iron-sulfur cluster.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD
References:
1.  Nam, J.W., Nojiri, H., Noguchi, H., Uchimura, H., Yoshida, T., Habe, H., Yamane, H. and Omori, T. Purification and characterization of carbazole 1,9a-dioxygenase, a three-component dioxygenase system of Pseudomonas resinovorans strain CA10. Appl. Environ. Microbiol. 68 (2002) 5882–5890. [DOI] [PMID: 12450807]
2.  Gai, Z., Wang, X., Liu, X., Tai, C., Tang, H., He, X., Wu, G., Deng, Z. and Xu, P. The genes coding for the conversion of carbazole to catechol are flanked by IS6100 elements in Sphingomonas sp. strain XLDN2-5. PLoS One 5:e10018 (2010). [DOI] [PMID: 20368802]
[EC 1.14.12.22 created 2010]
 
 
EC 1.14.12.23     
Accepted name: nitroarene dioxygenase
Reaction: nitrobenzene + NADH + O2 = catechol + nitrite + NAD+
Other name(s): cnbA (gene name)
Systematic name: nitrobenzene,NADH:oxygen oxidoreductase (1,2-hydroxylating, nitrite-releasing)
Comments: This enzyme is a member of the naphthalene family of bacterial Rieske non-heme iron dioxygenases. It comprises a multicomponent system, containing a Rieske [2Fe-2S] ferredoxin, an NADH-dependent flavoprotein reductase (EC 1.18.1.3, ferredoxin—NAD+ reductase), and an α3β3 oxygenase. The enzyme forms of a cis-dihydroxylated product that spontaneously rearranges to form a catechol with accompanying release of nitrite. It can typically act on many different nitroaromatic compounds, including chlorinated species. Enzymes found in different strains may have different substrate preferences. Requires Fe2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Parales, J.V., Parales, R.E., Resnick, S.M. and Gibson, D.T. Enzyme specificity of 2-nitrotoluene 2,3-dioxygenase from Pseudomonas sp. strain JS42 is determined by the C-terminal region of the α subunit of the oxygenase component. J. Bacteriol. 180 (1998) 1194–1199. [PMID: 9495758]
2.  Lessner, D.J., Johnson, G.R., Parales, R.E., Spain, J.C. and Gibson, D.T. Molecular characterization and substrate specificity of nitrobenzene dioxygenase from Comamonas sp. strain JS765. Appl. Environ. Microbiol. 68 (2002) 634–641. [DOI] [PMID: 11823201]
3.  Liu, H., Wang, S.J., Zhang, J.J., Dai, H., Tang, H. and Zhou, N.Y. Patchwork assembly of nag-like nitroarene dioxygenase genes and the 3-chlorocatechol degradation cluster for evolution of the 2-chloronitrobenzene catabolism pathway in Pseudomonas stutzeri ZWLR2-1. Appl. Environ. Microbiol. 77 (2011) 4547–4552. [DOI] [PMID: 21602392]
4.  Singh, D., Kumari, A., Ramaswamy, S. and Ramanathan, G. Expression, purification and substrate specificities of 3-nitrotoluene dioxygenase from Diaphorobacter sp. strain DS2. Biochem. Biophys. Res. Commun. 445 (2014) 36–42. [DOI] [PMID: 24491551]
[EC 1.14.12.23 created 2015]
 
 
EC 1.14.12.24     
Accepted name: 2,4-dinitrotoluene dioxygenase
Reaction: 2,4-dinitrotoluene + NADH + O2 = 4-methyl-5-nitrocatechol + nitrite + NAD+
Other name(s): dntA (gene name)
Systematic name: 2,4-dinitrotoluene,NADH:oxygen oxidoreductase (4,5-hydroxylating, nitrite-releasing)
Comments: This enzyme, characterized from the bacterium Burkholderia sp. strain DNT, is a member of the naphthalene family of bacterial Rieske non-heme iron dioxygenases. It comprises a multicomponent system, containing a Rieske [2Fe-2S] ferredoxin, an NADH-dependent flavoprotein reductase (EC 1.18.1.3, ferredoxin—NAD+ reductase), and an α3β3 oxygenase. The enzyme forms a cis-dihydroxylated product that spontaneously rearranges to form a catechol with accompanying release of nitrite. It does not act on nitrobenzene. cf. EC 1.14.12.23, nitroarene dioxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Suen, W.C., Haigler, B.E. and Spain, J.C. 2,4-Dinitrotoluene dioxygenase from Burkholderia sp. strain DNT: similarity to naphthalene dioxygenase. J. Bacteriol. 178 (1996) 4926–4934. [DOI] [PMID: 8759857]
[EC 1.14.12.24 created 2015]
 
 
EC 1.14.13.1     
Accepted name: salicylate 1-monooxygenase
Reaction: salicylate + NADH + 2 H+ + O2 = catechol + NAD+ + H2O + CO2
Other name(s): salicylate hydroxylase; salicylate 1-hydroxylase; salicylate monooxygenase; salicylate hydroxylase (decarboxylating)
Systematic name: salicylate,NADH:oxygen oxidoreductase (1-hydroxylating, decarboxylating)
Comments: A flavoprotein (FAD).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 9059-28-3
References:
1.  Suzuki, K., Takemori, S. and Katagiri, M. Mechanism of the salicylate hydroxylase reaction. IV. Fluorimetric analysis of the complex formation. Biochim. Biophys. Acta 191 (1969) 77–85. [DOI] [PMID: 4390441]
2.  Takemori, S., Yasuda, H., Mihara, K., Suzuki, K. and Katagiri, M. Mechanism of the salicylate hydroxylase reaction. II. The enzyme-substrate complex. Biochim. Biophys. Acta 191 (1969) 58–68. [DOI] [PMID: 4898626]
3.  Takemori, S., Yasuda, H., Mihara, K., Suzuki, K. and Katagiri, M. Mechanism of the salicylate hydroxylase reaction. 3. Characterization and reactivity of chemically or photochemically reduced enzyme-flavin. Biochim. Biophys. Acta 191 (1969) 69–76. [DOI] [PMID: 4309912]
4.  Yamamoto, S., Katagiri, M., Maeno, H. and Hayaishi, O. Salicylate hydroxylase, a monooxygenase requiring flavin adenine dinucleotide. J. Biol. Chem. 240 (1965) 3408–3413. [PMID: 14321380]
[EC 1.14.13.1 created 1972]
 
 
EC 1.14.13.7     
Accepted name: phenol 2-monooxygenase (NADPH)
Reaction: phenol + NADPH + H+ + O2 = catechol + NADP+ + H2O
Glossary: o-cresol = 2-cresol = 2-methylphenol
Other name(s): phenol hydroxylase; phenol o-hydroxylase
Systematic name: phenol,NADPH:oxygen oxidoreductase (2-hydroxylating)
Comments: A flavoprotein (FAD). The enzyme from the fungus Trichosporon cutaneum has a broad substrate specificity, and has been reported to catalyse the hydroxylation of a variety of substituted phenols, such as fluoro-, chloro-, amino- and methyl-phenols and also dihydroxybenzenes. cf. EC 1.14.14.20, phenol 2-monooxygenase (FADH2).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 37256-84-1
References:
1.  Nakagawa, H. and Takeda, Y. Phenol hydroxylase. Biochim. Biophys. Acta 62 (1962) 423–426. [DOI] [PMID: 14478080]
2.  Neujahr, H.Y. and Gaal, A. Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum. Eur. J. Biochem. 35 (1973) 386–400. [DOI] [PMID: 4146224]
3.  Neujahr, H.Y. and Gaal, A. Phenol hydroxylase from yeast. Sulfhydryl groups in phenol hydroxylase from Trichosporon cutaneum. Eur. J. Biochem. 58 (1975) 351–357. [DOI] [PMID: 810352]
[EC 1.14.13.7 created 1972, modified 2011, modified 2016]
 
 
EC 1.14.13.20     
Accepted name: 2,4-dichlorophenol 6-monooxygenase
Reaction: 2,4-dichlorophenol + NADPH + H+ + O2 = 3,5-dichlorocatechol + NADP+ + H2O
Other name(s): 2,4-dichlorophenol hydroxylase; 2,4-dichlorophenol monooxygenase
Systematic name: 2,4-dichlorophenol,NADPH:oxygen oxidoreductase (6-hydroxylating)
Comments: A flavoprotein (FAD). Also acts, more slowly, on 4-chlorophenol and 4-chloro-2-methylphenol; NADH can act instead of NADPH, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 82047-82-3
References:
1.  Beadle, C.A. and Smith, A.R.W. The purification and properties of 2,4-dichlorophenol hydroxylase from a strain of Acinetobacter species. Eur. J. Biochem. 123 (1982) 323–332. [DOI] [PMID: 7075592]
[EC 1.14.13.20 created 1983]
 
 
EC 1.14.13.29     
Accepted name: 4-nitrophenol 2-monooxygenase
Reaction: 4-nitrophenol + NADH + H+ + O2 = 4-nitrocatechol + NAD+ + H2O
For diagram of 4-nitrophenol metabolism, click here
Other name(s): 4-nitrophenol hydroxylase; 4-nitrophenol-2-hydroxylase
Systematic name: 4-nitrophenol,NADH:oxygen oxidoreductase (2-hydroxylating)
Comments: A flavoprotein (FAD).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 91116-87-9
References:
1.  Mitra, D. and Vaidyanathan, C.S. A new 4-nitrophenol 2-hydroxylase from a Nocardia sp. Biochem. Int. 8 (1984) 609–615. [PMID: 6477623]
[EC 1.14.13.29 created 1989]
 
 
EC 1.14.13.31     
Accepted name: 2-nitrophenol 2-monooxygenase
Reaction: 2-nitrophenol + 2 NADPH + 2 H+ + O2 = catechol + nitrite + 2 NADP+ + H2O
Other name(s): 2-nitrophenol oxygenase; nitrophenol oxygenase
Systematic name: 2-nitrophenol,NADPH:oxygen 2-oxidoreductase (2-hydroxylating, nitrite-forming)
Comments: Involved in the metabolism of nitro-aromatic compounds by a strain of Pseudomonas putida.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 104520-84-5
References:
1.  Zeyer, J., Kocher, H.P. and Timmis, N. Influence of para-substituents on the oxidative metabolism of o-nitrophenols by Pseudomonas putida B2. Appl. Environ. Microbiol. 52 (1986) 334–339. [PMID: 3752997]
[EC 1.14.13.31 created 1989]
 
 
EC 1.14.13.166     
Accepted name: 4-nitrocatechol 4-monooxygenase
Reaction: 4-nitrocatechol + NAD(P)H + H+ + O2 = 2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
For diagram of 4-nitrophenol metabolism, click here
Systematic name: 4-nitrocatechol,NAD(P)H:oxygen 4-oxidoreductase (4-hydroxylating, nitrite-forming)
Comments: Contains FAD. The enzyme catalyses the oxidation of 4-nitrocatechol with the concomitant removal of the nitro group as nitrite. Forms a two-component system with a flavoprotein reductase [1]. The enzymes from the bacteria Lysinibacillus sphaericus JS905 and Rhodococcus sp. strain PN1 were shown to also catalyse EC 1.14.13.29, 4-nitrophenol 2-monooxygenase [1,2] while the enzyme from Pseudomonas sp. WBC-3 was shown to also catalyse EC 1.14.13.167, 4-nitrophenol 4-monooxygenase [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD
References:
1.  Kadiyala, V. and Spain, J.C. A two-component monooxygenase catalyzes both the hydroxylation of p-nitrophenol and the oxidative release of nitrite from 4-nitrocatechol in Bacillus sphaericus JS905. Appl. Environ. Microbiol. 64 (1998) 2479–2484. [PMID: 9647818]
2.  Kitagawa, W., Kimura, N. and Kamagata, Y. A novel p-nitrophenol degradation gene cluster from a gram-positive bacterium, Rhodococcus opacus SAO101. J. Bacteriol. 186 (2004) 4894–4902. [DOI] [PMID: 15262926]
3.  Zhang, J.J., Liu, H., Xiao, Y., Zhang, X.E. and Zhou, N.Y. Identification and characterization of catabolic para-nitrophenol 4-monooxygenase and para-benzoquinone reductase from Pseudomonas sp. strain WBC-3. J. Bacteriol. 191 (2009) 2703–2710. [DOI] [PMID: 19218392]
[EC 1.14.13.166 created 2012]
 
 
EC 1.14.13.167     
Accepted name: 4-nitrophenol 4-monooxygenase
Reaction: 4-nitrophenol + NADPH + H+ + O2 = 1,4-benzoquinone + nitrite + NADP+ + H2O
For diagram of 4-nitrophenol metabolism, click here
Other name(s): pnpA (gene name); pdcA (gene name)
Systematic name: 4-nitrophenol,NAD(P)H:oxygen 4-oxidoreductase (4-hydroxylating, nitrite-forming)
Comments: Contains FAD. The enzyme catalyses the first step in a degradation pathway for 4-nitrophenol, the oxidation of 4-nitrophenol at position 4 with the concomitant removal of the nitro group as nitrite. The enzyme from the bacterium Pseudomonas sp. strain WBC-3 also catalyses EC 1.14.13.166, 4-nitrocatechol 4-monooxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Zhang, J.J., Liu, H., Xiao, Y., Zhang, X.E. and Zhou, N.Y. Identification and characterization of catabolic para-nitrophenol 4-monooxygenase and para-benzoquinone reductase from Pseudomonas sp. strain WBC-3. J. Bacteriol. 191 (2009) 2703–2710. [DOI] [PMID: 19218392]
[EC 1.14.13.167 created 2012]
 
 
EC 1.14.13.210     
Accepted name: 4-methyl-5-nitrocatechol 5-monooxygenase
Reaction: 4-methyl-5-nitrocatechol + NAD(P)H + H+ + O2 = 2-hydroxy-5-methylquinone + nitrite + NAD(P)+ + H2O
Other name(s): dntB (gene name); 4-methyl-5-nitrocatechol oxygenase; MNC monooxygenase
Systematic name: 4-methyl-5-nitrocatechol,NAD(P)H:oxygen 5-oxidoreductase (5-hydroxylating, nitrite-forming)
Comments: Contains FAD. The enzyme, isolated from the bacterium Burkholderia sp. DNT, can use both NADH and NADPH, but prefers NADPH. It has a narrow substrate range, but can also act on 4-nitrocatechol.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Haigler, B.E., Suen, W.C. and Spain, J.C. Purification and sequence analysis of 4-methyl-5-nitrocatechol oxygenase from Burkholderia sp. strain DNT. J. Bacteriol. 178 (1996) 6019–6024. [DOI] [PMID: 8830701]
2.  Leungsakul, T., Johnson, G.R. and Wood, T.K. Protein engineering of the 4-methyl-5-nitrocatechol monooxygenase from Burkholderia sp. strain DNT for enhanced degradation of nitroaromatics. Appl. Environ. Microbiol. 72 (2006) 3933–3939. [DOI] [PMID: 16751499]
[EC 1.14.13.210 created 2016]
 
 
EC 1.14.13.243     
Accepted name: toluene 2-monooxygenase
Reaction: (1) toluene + NADH + H+ + O2 = 2-methylphenol + NAD+ + H2O
(2) 2-methylphenol + NADH + H+ + O2 = 3-methylcatechol + NAD+ + H2O
Other name(s): tomA1/2/3/4/5 (gene names); toluene ortho-monooxygenase
Systematic name: toluene,NADH:oxygen oxidoreductase (2,3-dihydroxylating)
Comments: The enzyme, characterized from the bacterium Burkholderia cepacia, belongs to a class of nonheme, oxygen-dependent diiron enzymes. It contains a hydroxylase component with two binuclear iron centers, an NADH-oxidoreductase component containing FAD and a [2Fe-2S] iron-sulfur cluster, and a third component involved in electron transfer between the hydroxylase and the reductase. The enzyme dihydroxylates its substrate in two sequential hydroxylations, initially forming 2-methylphenol, which is hydroxylated to 3-methylcatechol.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Newman, L.M. and Wackett, L.P. Purification and characterization of toluene 2-monooxygenase from Burkholderia cepacia G4. Biochemistry 34 (1995) 14066–14076. [PMID: 7578004]
2.  Yeager, C.M., Bottomley, P.J., Arp, D.J. and Hyman, M.R. Inactivation of toluene 2-monooxygenase in Burkholderia cepacia G4 by alkynes. Appl. Environ. Microbiol. 65 (1999) 632–639. [PMID: 9925593]
3.  Canada, K.A., Iwashita, S., Shim, H. and Wood, T.K. Directed evolution of toluene ortho-monooxygenase for enhanced 1-naphthol synthesis and chlorinated ethene degradation. J. Bacteriol. 184 (2002) 344–349. [PMID: 11751810]
[EC 1.14.13.243 created 2019]
 
 
EC 1.14.13.244     
Accepted name: phenol 2-monooxygenase (NADH)
Reaction: phenol + NADH + H+ + O2 = catechol + NAD+ + H2O
Other name(s): dmpLMNOP (gene names)
Systematic name: phenol,NADH:oxygen oxidoreductase (2-hydroxylating)
Comments: The enzyme, characterized from the bacteria Pseudomonas sp. CF600 and Acinetobacter radioresistens, consists of a multisubunit oxygenease component that contains the active site and a dinuclear iron center, a reductase component that contains FAD and one iron-sulfur cluster, and a regulatory component. The reductase component is responsible for transferring electrons from NADH to the dinuclear iron center.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Nordlund, I., Powlowski, J. and Shingler, V. Complete nucleotide sequence and polypeptide analysis of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600. J. Bacteriol. 172 (1990) 6826–6833. [PMID: 2254258]
2.  Powlowski, J. and Shingler, V. In vitro analysis of polypeptide requirements of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600. J. Bacteriol. 172 (1990) 6834–6840. [PMID: 2254259]
3.  Powlowski, J., Sealy, J., Shingler, V. and Cadieux, E. On the role of DmpK, an auxiliary protein associated with multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600. J. Biol. Chem. 272 (1997) 945–951. [PMID: 8995386]
4.  Qian, H., Edlund, U., Powlowski, J., Shingler, V. and Sethson, I. Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy. Biochemistry 36 (1997) 495–504. [PMID: 9012665]
5.  Cadieux, E., Vrajmasu, V., Achim, C., Powlowski, J. and Munck, E. Biochemical, Mossbauer, and EPR studies of the diiron cluster of phenol hydroxylase from Pseudomonas sp. strain CF 600. Biochemistry 41 (2002) 10680–10691. [PMID: 12186554]
[EC 1.14.13.244 created 2019]
 
 
EC 1.14.14.20     
Accepted name: phenol 2-monooxygenase (FADH2)
Reaction: phenol + FADH2 + O2 = catechol + FAD + H2O
Other name(s): pheA1 (gene name)
Systematic name: phenol,FADH2:oxygen oxidoreductase (2-hydroxylating)
Comments: The enzyme catalyses the ortho-hydroxylation of simple phenols into the corresponding catechols. It accepts 4-methylphenol, 4-chlorophenol, and 4-fluorophenol [1] as well as 4-nitrophenol, 3-nitrophenol, and resorcinol [3]. The enzyme is part of a two-component system that also includes an NADH-dependent flavin reductase. It is strictly dependent on FADH2 and does not accept FMNH2 [1,3]. cf. EC 1.14.13.7, phenol 2-monooxygenase (NADPH).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kirchner, U., Westphal, A.H., Muller, R. and van Berkel, W.J. Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual role for FAD. J. Biol. Chem. 278 (2003) 47545–47553. [DOI] [PMID: 12968028]
2.  van den Heuvel, R.H., Westphal, A.H., Heck, A.J., Walsh, M.A., Rovida, S., van Berkel, W.J. and Mattevi, A. Structural studies on flavin reductase PheA2 reveal binding of NAD in an unusual folded conformation and support novel mechanism of action. J. Biol. Chem. 279 (2004) 12860–12867. [DOI] [PMID: 14703520]
3.  Saa, L., Jaureguibeitia, A., Largo, E., Llama, M.J. and Serra, J.L. Cloning, purification and characterization of two components of phenol hydroxylase from Rhodococcus erythropolis UPV-1. Appl. Microbiol. Biotechnol. 86 (2010) 201–211. [DOI] [PMID: 19787347]
[EC 1.14.14.20 created 2016]
 
 
EC 1.14.17.1     
Accepted name: dopamine β-monooxygenase
Reaction: dopamine + 2 ascorbate + O2 = noradrenaline + 2 monodehydroascorbate + H2O
For diagram of dopa biosynthesis, click here
Glossary: dopamine = 4-(2-aminoethyl)benzene-1,2-diol
Other name(s): dopamine β-hydroxylase; MDBH (membrane-associated dopamine β-monooxygenase); SDBH (soluble dopamine β-monooxygenase); dopamine-B-hydroxylase; 3,4-dihydroxyphenethylamine β-oxidase; 4-(2-aminoethyl)pyrocatechol β-oxidase; dopa β-hydroxylase; dopamine β-oxidase; dopamine hydroxylase; phenylamine β-hydroxylase; (3,4-dihydroxyphenethylamine)β-mono-oxygenase; DβM (gene name)
Systematic name: dopamine,ascorbate:oxygen oxidoreductase (β-hydroxylating)
Comments: A copper protein. The enzyme, found in animals, binds two copper ions with distinct roles during catalysis. Stimulated by fumarate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9013-38-1
References:
1.  Levin, E.Y., Levenberg, B. and Kaufman, S. The enzymatic conversion of 3,4-dihydroxyphenylethylamine to norepinephrine. J. Biol. Chem. 235 (1960) 2080–2086. [PMID: 14416204]
2.  Friedman, S. and Kaufman, S. 3,4-Dihydroxyphenylethylamine β-hydroxylase. Physical properties, copper content, and role of copper in the catalytic activity. J. Biol. Chem. 240 (1965) 4763–4773. [PMID: 5846992]
3.  Skotland, T. and Ljones, T. Direct spectrophotometric detection of ascorbate free radical formed by dopamine β-monooxygenase and by ascorbate oxidase. Biochim. Biophys. Acta 630 (1980) 30–35. [PMID: 7388045]
4.  Evans, J.P., Ahn, K. and Klinman, J.P. Evidence that dioxygen and substrate activation are tightly coupled in dopamine β-monooxygenase. Implications for the reactive oxygen species. J. Biol. Chem. 278 (2003) 49691–49698. [PMID: 12966104]
[EC 1.14.17.1 created 1965 as EC 1.14.2.1, transferred 1972 to EC 1.14.17.1, modified 2020]
 
 
EC 1.14.18.1     
Accepted name: tyrosinase
Reaction: (1) L-tyrosine + O2 = dopaquinone + H2O (overall reaction)
(1a) L-tyrosine + ½ O2 = L-dopa
(1b) L-dopa + ½ O2 = dopaquinone + H2O
(2) 2 L-dopa + O2 = 2 dopaquinone + 2 H2O
For diagram of melanin biosynthesis, click here
Other name(s): monophenol monooxygenase; phenolase; monophenol oxidase; cresolase; monophenolase; tyrosine-dopa oxidase; monophenol monooxidase; monophenol dihydroxyphenylalanine:oxygen oxidoreductase; N-acetyl-6-hydroxytryptophan oxidase; monophenol, dihydroxy-L-phenylalanine oxygen oxidoreductase; o-diphenol:O2 oxidoreductase; phenol oxidase
Systematic name: L-tyrosine,L-dopa:oxygen oxidoreductase
Comments: A type III copper protein found in a broad variety of bacteria, fungi, plants, insects, crustaceans, and mammals, which is involved in the synthesis of betalains and melanin. The enzyme, which is activated upon binding molecular oxygen, can catalyse both a monophenolase reaction cycle (reaction 1) or a diphenolase reaction cycle (reaction 2). During the monophenolase cycle, one of the bound oxygen atoms is transferred to a monophenol (such as L-tyrosine), generating an o-diphenol intermediate, which is subsequently oxidized to an o-quinone and released, along with a water molecule. The enzyme remains in an inactive deoxy state, and is restored to the active oxy state by the binding of a new oxygen molecule. During the diphenolase cycle the enzyme binds an external diphenol molecule (such as L-dopa) and oxidizes it to an o-quinone that is released along with a water molecule, leaving the enzyme in the intermediate met state. The enzyme then binds a second diphenol molecule and repeats the process, ending in a deoxy state [7]. The second reaction is identical to that catalysed by the related enzyme catechol oxidase (EC 1.10.3.1). However, the latter can not catalyse the hydroxylation or monooxygenation of monophenols.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9002-10-2
References:
1.  Dawson, C.R. and Tarpley, W.B. The copper oxidases. In: Sumner, J.B. and Myrbäck, K. (Ed.), The Enzymes, 1st edn, vol. 2, Academic Press, New York, 1951, pp. 454–498.
2.  Patil, S.S. and Zucker, M. Potato phenolases. Purification and properties. J. Biol. Chem. 240 (1965) 3938–3943. [PMID: 5842066]
3.  Pomerantz, S.H. Separation, purification, and properties of two tyrosinases from hamster melanoma. J. Biol. Chem. 238 (1963) 2351–2357. [PMID: 13972077]
4.  Robb, D.A. `Tyrosinase. In: Lontie, R. (Ed.), Copper Proteins and Copper Enzymes, vol. 2, CRC Press, Boca Raton, FL, 1984, pp. 207–240.
5.  Sanchez-Ferrer, A., Rodriguez-Lopez, J.N., Garcia-Canovas, F. and Garcia-Carmona, F. Tyrosinase: a comprehensive review of its mechanism. Biochim. Biophys. Acta 1247 (1995) 1–11. [DOI] [PMID: 7873577]
6.  Steiner, U., Schliemann, W. and Strack, D. Assay for tyrosine hydroxylation activity of tyrosinase from betalain-forming plants and cell cultures. Anal. Biochem. 238 (1996) 72–75. [DOI] [PMID: 8660589]
7.  Rolff, M., Schottenheim, J., Decker, H. and Tuczek, F. Copper-O2 reactivity of tyrosinase models towards external monophenolic substrates: molecular mechanism and comparison with the enzyme. Chem Soc Rev 40 (2011) 4077–4098. [DOI] [PMID: 21416076]
[EC 1.14.18.1 created 1972, modified 1976, modified 1980 (EC 1.14.17.2 created 1972, incorporated 1984), modified 2012]
 
 
EC 1.16.1.9     
Accepted name: ferric-chelate reductase (NADPH)
Reaction: 2 Fe(II)-siderophore + NADP+ + H+ = 2 Fe(III)-siderophore + NADPH
Other name(s): ferric chelate reductase (ambiguous); iron chelate reductase (ambiguous); NADPH:Fe3+-EDTA reductase; NADPH-dependent ferric reductase; yqjH (gene name); Fe(II):NADP+ oxidoreductase
Systematic name: Fe(II)-siderophore:NADP+ oxidoreductase
Comments: Contains FAD. The enzyme, which is widespread among bacteria, catalyses the reduction of ferric iron bound to a variety of iron chelators (siderophores), including ferric triscatecholates and ferric dicitrate, resulting in the release of ferrous iron. The enzyme from the bacterium Escherichia coli has the highest efficiency with the hydrolysed ferric enterobactin complex ferric N-(2,3-dihydroxybenzoyl)-L-serine [3]. cf. EC 1.16.1.7, ferric-chelate reductase (NADH) and EC 1.16.1.10, ferric-chelate reductase [NAD(P)H].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 120720-17-4
References:
1.  Bamford, V.A., Armour, M., Mitchell, S.A., Cartron, M., Andrews, S.C. and Watson, K.A. Preliminary X-ray diffraction analysis of YqjH from Escherichia coli: a putative cytoplasmic ferri-siderophore reductase. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 (2008) 792–796. [DOI] [PMID: 18765906]
2.  Wang, S., Wu, Y. and Outten, F.W. Fur and the novel regulator YqjI control transcription of the ferric reductase gene yqjH in Escherichia coli. J. Bacteriol. 193 (2011) 563–574. [DOI] [PMID: 21097627]
3.  Miethke, M., Hou, J. and Marahiel, M.A. The siderophore-interacting protein YqjH acts as a ferric reductase in different iron assimilation pathways of Escherichia coli. Biochemistry 50 (2011) 10951–10964. [DOI] [PMID: 22098718]
[EC 1.16.1.9 created 1992 as EC 1.6.99.13, transferred 2002 to EC 1.16.1.7, transferred 2011 to EC 1.16.1.9, modified 2012, modified 2014]
 
 
EC 1.99.2.2      
Transferred entry: Now EC 1.13.11.1, catechol 1,2-dioxygenase
[EC 1.99.2.2 created 1961, deleted 1965]
 
 
EC 2.1.1.6     
Accepted name: catechol O-methyltransferase
Reaction: S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol
Other name(s): COMT I ; COMT II; S-COMT (soluble form of catechol-O-methyltransferase); MB-COMT (membrane-bound form of catechol-O-methyltransferase); catechol methyltransferase; catecholamine O-methyltransferase
Systematic name: S-adenosyl-L-methionine:catechol O-methyltransferase
Comments: The mammalian enzyme acts more rapidly on catecholamines such as adrenaline or noradrenaline than on catechols.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9012-25-3
References:
1.  Axelrod, J. and Tomchick, R. Enzymatic O-methylation of epinephrine and other catechols. J. Biol. Chem. 233 (1958) 702–705. [PMID: 13575440]
2.  Gulliver, P.A. and Tipton, K.F. The purification and properties of pig brain catechol-O-methyltransferase. J. Neurochem. 32 (1979) 1525–1529. [DOI] [PMID: 438821]
3.  Huh, M.M.O. and Friedhof, A.J. Multiple molecular forms of catechol-O-methyltransferase. Evidence for two distinct forms, and their purification and physical characterization. J. Biol. Chem. 254 (1979) 299–308. [PMID: 762061]
[EC 2.1.1.6 created 1965]
 
 
EC 2.1.1.68     
Accepted name: caffeate O-methyltransferase
Reaction: S-adenosyl-L-methionine + 3,4-dihydroxy-trans-cinnamate = S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate
Other name(s): caffeate methyltransferase; caffeate 3-O-methyltransferase; S-adenosyl-L-methionine:caffeic acid-O-methyltransferase
Systematic name: S-adenosyl-L-methionine:3,4-dihydroxy-trans-cinnamate 3-O-methyltransferase
Comments: 3,4-Dihydroxybenzaldehyde and catechol can act as acceptors, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 50936-45-3
References:
1.  Ebel, J., Schaller-Hekeler, B., Knobloch, K.-H., Wellman, E., Grisebach, H. and Hahlbrock, K. Coordinated changes in enzyme activities of phenylpropanoid metabolism during the growth of soybean cell suspension cultures. Biochim. Biophys. Acta 362 (1974) 417–424. [DOI] [PMID: 4472044]
2.  Poulton, J.E. and Butt, V.S. Purification and properties of S-adenosyl-L-methionine: caffeic acid O-methyltransferase from leaves of spinach beet (Beta vulgaris L). Biochim. Biophys. Acta 403 (1975) 301–314. [DOI] [PMID: 241400]
3.  Shimada, M., Kuroda, H. and Higuchi, T. Evidence for the formation of methoxyl groups of ferulic and sinapic acid in Bambusa by the same O-methyltransferase. Phytochemistry 12 (1973) 2873–2875.
[EC 2.1.1.68 created 1984]
 
 
EC 2.7.2.1     
Accepted name: acetate kinase
Reaction: ATP + acetate = ADP + acetyl phosphate
Other name(s): acetokinase; AckA; AK; acetic kinase; acetate kinase (phosphorylating)
Systematic name: ATP:acetate phosphotransferase
Comments: Requires Mg2+ for activity. While purified enzyme from Escherichia coli is specific for acetate [4], others have found that the enzyme can also use propanoate as a substrate, but more slowly [7]. Acetate can be converted into the key metabolic intermediate acetyl-CoA by coupling acetate kinase with EC 2.3.1.8, phosphate acetyltransferase. Both this enzyme and EC 2.7.2.15, propionate kinase, play important roles in the production of propanoate [9].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9027-42-3
References:
1.  Romain, Y., Demassieux, S. and Carriere, S. Partial purification and characterization of two isoenzymes involved in the sulfurylation of catecholamines. Biochem. Biophys. Res. Commun. 106 (1982) 999–1005. [DOI] [PMID: 6956338]
2.  Romano, A.H. and Nickerson, W.J. Cystine reductase of pea seeds and yeast. J. Biol. Chem. 208 (1954) 409–416. [PMID: 13174550]
3.  Stern, J.R. and Ochoa, S. Enzymatic synthesis of citric acid. I. Synthesis with soluble enzymes. J. Biol. Chem. 191 (1951) 161–172. [PMID: 14850456]
4.  Fox, D.K. and Roseman, S. Isolation and characterization of homogeneous acetate kinase from Salmonella typhimurium and Escherichia coli. J. Biol. Chem. 261 (1986) 13487–13497. [PMID: 3020034]
5.  Knorr, R., Ehrmann, M.A. and Vogel, R.F. Cloning, expression, and characterization of acetate kinase from Lactobacillus sanfranciscensis. Microbiol. Res. 156 (2001) 267–277. [DOI] [PMID: 11716215]
6.  Buss, K.A., Cooper, D.R., Ingram-Smith, C., Ferry, J.G., Sanders, D.A. and Hasson, M.S. Urkinase: structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases. J. Bacteriol. 183 (2001) 680–686. [DOI] [PMID: 11133963]
7.  Ingram-Smith, C., Gorrell, A., Lawrence, S.H., Iyer, P., Smith, K. and Ferry, J.G. Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase. J. Bacteriol. 187 (2005) 2386–2394. [DOI] [PMID: 15774882]
8.  Gorrell, A., Lawrence, S.H. and Ferry, J.G. Structural and kinetic analyses of arginine residues in the active site of the acetate kinase from Methanosarcina thermophila. J. Biol. Chem. 280 (2005) 10731–10742. [DOI] [PMID: 15647264]
9.  Heßlinger, C., Fairhurst, S.A. and Sawers, G. Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate. Mol. Microbiol. 27 (1998) 477–492. [DOI] [PMID: 9484901]
[EC 2.7.2.1 created 1961, modified 2005]
 
 
EC 2.8.2.1     
Accepted name: aryl sulfotransferase
Reaction: 3′-phosphoadenylyl sulfate + a phenol = adenosine 3′,5′-bisphosphate + an aryl sulfate
Glossary: dopamine = 4-(2-aminoethyl)benzene-1,2-diol
3′-phosphoadenylyl sulfate = PAPS
Other name(s): phenol sulfotransferase; sulfokinase; 1-naphthol phenol sulfotransferase; 2-naphtholsulfotransferase; 4-nitrocatechol sulfokinase; arylsulfotransferase; dopamine sulfotransferase; p-nitrophenol sulfotransferase; phenol sulfokinase; ritodrine sulfotransferase; PST; 3′-phosphoadenylyl-sulfate:phenol sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:phenol sulfonotransferase
Comments: A number of aromatic compounds can act as acceptors. Organic hydroxylamines are not substrates (cf. EC 2.8.2.9 tyrosine-ester sulfotransferase).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9026-09-9
References:
1.  Romain, Y., Demassieux, S. and Carriere, S. Partial purification and characterization of two isoenzymes involved in the sulfurylation of catecholamines. Biochem. Biophys. Res. Commun. 106 (1982) 999–1005. [DOI] [PMID: 6956338]
2.  Sekura, R. and Jakoby, W.B. Phenol sulfotransferases. J. Biol. Chem. 254 (1979) 5658–5663. [PMID: 447677]
[EC 2.8.2.1 created 1961, modified 1980]
 
 
EC 2.8.3.6     
Accepted name: 3-oxoadipate CoA-transferase
Reaction: succinyl-CoA + 3-oxoadipate = succinate + 3-oxoadipyl-CoA
For diagram of benzoate metabolism, click here and for diagram of 4-nitrophenol metabolism, click here
Other name(s): 3-oxoadipate coenzyme A-transferase; 3-oxoadipate succinyl-CoA transferase
Systematic name: succinyl-CoA:3-oxoadipate CoA-transferase
Comments: The enzyme, often found in soil bacteria and fungi, is involved in the catabolism of a variety of aromatic compounds, including catechol and protocatechuate, which are degraded via 3-oxoadipate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 9026-16-8
References:
1.  Katagiri, M. and Hayaishi, O. Enzymatic degradation of β-ketoadipic acid. J. Biol. Chem. 226 (1957) 439–448. [PMID: 13428776]
2.  Kaschabek, S.R., Kuhn, B., Müller, D., Schmidt, E. and Reineke, W. Degradation of aromatics and chloroaromatics by Pseudomonas sp. strain B13: purification and characterization of 3-oxoadipate:succinyl-coenzyme A (CoA) transferase and 3-oxoadipyl-CoA thiolase. J. Bacteriol. 184 (2002) 207–215. [DOI] [PMID: 11741862]
3.  Gobel, M., Kassel-Cati, K., Schmidt, E. and Reineke, W. Degradation of aromatics and chloroaromatics by Pseudomonas sp. strain B13: cloning, characterization, and analysis of sequences encoding 3-oxoadipate:succinyl-coenzyme A (CoA) transferase and 3-oxoadipyl-CoA thiolase. J. Bacteriol. 184 (2002) 216–223. [DOI] [PMID: 11741863]
[EC 2.8.3.6 created 1961]
 
 


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