The Enzyme Database

Your query returned 5 entries.    printer_iconPrintable version

Accepted name: gentisate 1,2-dioxygenase
Reaction: 2,5-dihydroxybenzoate + O2 = maleylpyruvate
Other name(s): gentisate oxygenase; 2,5-dihydroxybenzoate dioxygenase; gentisate dioxygenase; gentisic acid oxidase; gentisate:oxygen 1,2-oxidoreductase (decyclizing)
Systematic name: gentisate:oxygen 1,2-oxidoreductase (ring-opening)
Comments: Requires Fe2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9029-48-5
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.  Sugiyama, S., Yano, K., Komagata, K. and Arima, K. Metabolites of aromatic compounds by microbes. Part VII. Gentisic acid oxidase. Bull. Agric. Chem. Soc. Jpn 24 (1960) 243–248.
3.  Sugiyama, S., Yano, K. and Arima, K. Metabolites of aromatic compounds by microbes. Part VII. Further studies of gentisic acid oxidase. Bull. Agric. Chem. Soc. Jpn 24 (1960) 249–254.
[EC created 1961 as EC, transferred 1965 to EC, transferred 1972 to EC]
Accepted name: 3-hydroxybenzoate 6-monooxygenase
Reaction: 3-hydroxybenzoate + NADH + H+ + O2 = 2,5-dihydroxybenzoate + NAD+ + H2O
Other name(s): 3-hydroxybenzoate 6-hydroxylase; m-hydroxybenzoate 6-hydroxylase; 3-hydroxybenzoic acid-6-hydroxylase
Systematic name: 3-hydroxybenzoate,NADH:oxygen oxidoreductase (6-hydroxylating)
Comments: A flavoprotein (FAD). Acts also on a number of analogues of 3-hydroxybenzoate substituted in the 2, 4, 5 and 6 positions; NADPH can act instead of NADH, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 51570-26-4
1.  Groseclose, E.E. and Ribbons, D.W. 3-Hydroxybenzoate 6-hydroxylase from Pseudomonas aeruginosa. Biochem. Biophys. Res. Commun. 55 (1973) 897–903. [DOI] [PMID: 4357436]
[EC created 1984]
Accepted name: salicylate 5-hydroxylase
Reaction: salicylate + NADH + H+ + O2 = 2,5-dihydroxybenzoate + NAD+ + H2O
Glossary: 2,5-dihydroxybenzoate = gentisate
Other name(s): nagG (gene name); nagH (gene name)
Systematic name: salicylate,NADH:oxygen oxidoreductase (5-hydroxylating)
Comments: This enzyme, which was characterized from the bacterium Ralstonia sp. U2, comprises a multicomponent system, containing a reductase that is an iron-sulfur flavoprotein (FAD; EC, ferredoxin—NAD(P)+ reductase), an iron-sulfur oxygenase, and ferredoxin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD
1.  Fuenmayor, S.L., Wild, M., Boyes, A.L. and Williams, P.A. A gene cluster encoding steps in conversion of naphthalene to gentisate in Pseudomonas sp. strain U2. J. Bacteriol. 180 (1998) 2522–2530. [PMID: 9573207]
[EC created 2013]
Accepted name: salicyloyl-CoA 5-hydroxylase
Reaction: 2-hydroxybenzoyl-CoA + NADH + H+ + O2 = gentisyl-CoA + NAD+ + H2O
Glossary: 2-hydroxybenzoyl-CoA = salicyloyl-CoA
gentisate = 2,5-dihydroxybenzoate
Other name(s): sdgC (gene name)
Systematic name: salicyloyl-CoA,NADH:oxygen oxidoreductase (5-hydroxylating)
Comments: The enzyme, characterized from the bacterium Streptomyces sp. WA46, participates in a pathway for salicylate degradation. cf. EC, salicylate 5-hydroxylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Ishiyama, D., Vujaklija, D. and Davies, J. Novel pathway of salicylate degradation by Streptomyces sp. strain WA46. Appl. Environ. Microbiol. 70 (2004) 1297–1306. [DOI] [PMID: 15006746]
[EC created 2015]
Accepted name: gentisate decarboxylase
Reaction: 2,5-dihydroxybenzoate = hydroquinone + CO2
Glossary: gentisate = 2,5-dihydroxybenzoate
Other name(s): 2,5-dihydroxybenzoate decarboxylase; gentisate carboxy-lyase
Systematic name: 2,5-dihydroxybenzoate carboxy-lyase (hydroquinone-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37290-54-3
1.  Grant, D.J.W. and Patel, J.C. Non-oxidative decarboxylation of p-hydroxybenzoic acid, gentisic acid, protocatechuic acid, and gallic acid by Klebsiella aerogenes (Aerobacter aerogenes). J. Microbiol. Serol. 35 (1969) 325–343. [PMID: 5309907]
[EC created 1972]

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