The Enzyme Database

Your query returned 22 entries.    printer_iconPrintable version



EC 1.13.1.4      
Transferred entry: Now EC 1.13.11.4, gentisate 1,2-dioxygenase
[EC 1.13.1.4 created 1961 as EC 1.99.2.4, transferred 1965 to EC 1.13.1.4, deleted 1972]
 
 
EC 1.13.1.5      
Transferred entry: Now EC 1.13.11.5, homogentisate 1,2-dioxygenase
[EC 1.13.1.5 created 1961 as EC 1.99.2.5, transferred 1965 to EC 1.13.1.5, deleted 1972]
 
 
EC 1.13.11.4     
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
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.  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 1.13.11.4 created 1961 as EC 1.99.2.4, transferred 1965 to EC 1.13.1.4, transferred 1972 to EC 1.13.11.4]
 
 
EC 1.13.11.5     
Accepted name: homogentisate 1,2-dioxygenase
Reaction: homogentisate + O2 = 4-maleylacetoacetate
Other name(s): homogentisicase; homogentisate oxygenase; homogentisate dioxygenase; homogentisate oxidase; homogentisic acid oxidase; homogentisic acid oxygenase; homogentisic oxygenase; homogentisate:oxygen 1,2-oxidoreductase (decyclizing)
Systematic name: homogentisate:oxygen 1,2-oxidoreductase (ring-opening)
Comments: Requires Fe2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 9029-49-6
References:
1.  Adachi, K., Iwayama, Y., Tanioka, H. and Takeda, Y. Purification and properties of homogentisate oxygenase from Pseudomonas fluorescens. Biochim. Biophys. Acta 118 (1966) 88–97. [PMID: 5954067]
2.  Crandall, D.I. and Halikis, D.N. Homogentisic acid oxidase. I. Distribution in animal tissues and relation to tyrosine metabolism in rat kidney. J. Biol. Chem. 208 (1954) 629–638. [PMID: 13174573]
3.  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.
4.  Kita, H., Kamimoto, M., Senoh, S., Adachi, T. and Takeda, Y. Cystallization and some properties of 3,4-dihydroxyphenylacetate-2,3-oxygenase. Biochem. Biophys. Res. Commun. 18 (1965) 66–70. [DOI] [PMID: 14265758]
5.  Knox, W.E. and Edwards, S.W. Homogentisate oxidase of liver. J. Biol. Chem. 216 (1955) 479–487. [PMID: 13271328]
6.  Ravdin, R.G. and Crandall, D.I. The enzymatic conversion of homogentisic acid to 4-fumarylacetoacetic acid. J. Biol. Chem. 189 (1951) 137–149. [PMID: 14832225]
[EC 1.13.11.5 created 1961 as EC 1.99.2.5, transferred 1965 to EC 1.13.1.5, transferred 1972 to EC 1.13.11.5]
 
 
EC 1.13.11.27     
Accepted name: 4-hydroxyphenylpyruvate dioxygenase
Reaction: 4-hydroxyphenylpyruvate + O2 = homogentisate + CO2
For diagram of 4-hydroxyphenylpyruvate metabolites, click here
Other name(s): p-hydroxyphenylpyruvic hydroxylase; p-hydroxyphenylpyruvate hydroxylase; p-hydroxyphenylpyruvate oxidase; p-hydroxyphenylpyruvic oxidase; p-hydroxyphenylpyruvate dioxygenase; p-hydroxyphenylpyruvic acid hydroxylase; 4-hydroxyphenylpyruvic acid dioxygenase
Systematic name: 4-hydroxyphenylpyruvate:oxygen oxidoreductase (hydroxylating, decarboxylating)
Comments: The Pseudomonas enzyme contains one Fe3+ per mole of enzyme; the enzymes from other sources may contain essential iron or copper.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 9029-72-5
References:
1.  Lindstedt, S. and Rundgren, M. Blue color, metal content, and substrate binding in 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. strain P. J. 874. J. Biol. Chem. 257 (1982) 11922–11931. [PMID: 7118918]
2.  Roche, P.A., Moorehead, T.J. and Hamilton, G.A. Purification and properties of hog liver 4-hydroxyphenylpyruvate dioxygenase. Arch. Biochem. Biophys. 216 (1982) 62–73. [DOI] [PMID: 7103516]
[EC 1.13.11.27 created 1961 as EC 1.99.1.14, transferred 1965 to EC 1.14.2.2, transferred 1972 to EC 1.13.11.27]
 
 
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 1.14.13.18     
Accepted name: 4-hydroxyphenylacetate 1-monooxygenase
Reaction: 4-hydroxyphenylacetate + NAD(P)H + H+ + O2 = homogentisate + NAD(P)+ + H2O
For diagram of the homogentisate pathways, click here
Other name(s): 4-hydroxyphenylacetate 1-hydroxylase; 4-hydroxyphenylacetic 1-hydroxylase; 4-HPA 1-hydroxylase
Systematic name: 4-hydroxyphenylacetate,NAD(P)H:oxygen oxidoreductase (1-hydroxylating)
Comments: A flavoprotein (FAD). Also acts on 4-hydroxyhydratropate (forming 2-methylhomogentisate) and on 4-hydroxyphenoxyacetate (forming hydroquinone and glycolate).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 55326-44-8
References:
1.  Hareland, W.A., Crawford, R.L., Chapman, P.J. and Dagley, S. Metabolic function and properties of 4-hydroxyphenylacetic acid 1-hydroxylase from Pseudomonas acidovorans. J. Bacteriol. 121 (1975) 272–285. [PMID: 234937]
[EC 1.14.13.18 created 1976]
 
 
EC 1.14.13.58     
Accepted name: benzoyl-CoA 3-monooxygenase
Reaction: benzoyl-CoA + NADPH + H+ + O2 = 3-hydroxybenzoyl-CoA + NADP+ + H2O
Other name(s): benzoyl-CoA 3-hydroxylase
Systematic name: benzoyl-CoA,NADPH: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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 151616-61-4
References:
1.  Niemetz, R., Altenschmidt, U., Herrmann, H. and 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 1.14.13.58 created 1999]
 
 
EC 1.14.13.63     
Accepted name: 3-hydroxyphenylacetate 6-hydroxylase
Reaction: 3-hydroxyphenylacetate + NAD(P)H + H+ + O2 = 2,5-dihydroxyphenylacetate + NAD(P)+ + H2O
For diagram of the homogentisate pathways, click here
Glossary: homogentisate = 2,5-dihydroxyphenylacetate
Other name(s): 3-hydroxyphenylacetate 6-monooxygenase
Systematic name: 3-hydroxyphenylacetate,NAD(P)H:oxygen oxidoreductase (6-hydroxylating)
Comments: 3-hydroxyphenylacetate 6-hydroxylase from Flavobacterium sp. is highly specific for 3-hydroxyphenylacetate and uses NADH and NADPH as electron donors with similar efficiency.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 114705-01-0
References:
1.  van Berkel, W.H.J. and 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. [DOI] [PMID: 1935954]
[EC 1.14.13.63 created 1999]
 
 
EC 1.14.13.172     
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 1.18.1.7, ferredoxin—NAD(P)+ reductase), an iron-sulfur oxygenase, and ferredoxin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD
References:
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 1.14.13.172 created 2013]
 
 
EC 1.14.13.209     
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 1.14.13.172, salicylate 5-hydroxylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
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 1.14.13.209 created 2015]
 
 
EC 1.99.2.4      
Transferred entry: Now EC 1.13.11.4, gentisate 1,2-dioxygenase
[EC 1.99.2.4 created 1961, deleted 1965]
 
 
EC 1.99.2.5      
Transferred entry: Now EC 1.13.11.5, homogentisate 1,2-dioxygenase
[EC 1.99.2.5 created 1961, deleted 1965]
 
 
EC 2.5.1.42     
Accepted name: geranylgeranylglycerol-phosphate geranylgeranyltransferase
Reaction: geranylgeranyl diphosphate + 3-(O-geranylgeranyl)-sn-glycerol 1-phosphate = diphosphate + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
For diagram of archaetidylserine biosynthesis, click here and for diagram of archaetidylserine biosynthesis, click here
Other name(s): geranylgeranyloxyglycerol phosphate geranylgeranyltransferase; geranylgeranyltransferase II; (S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; DGGGP synthase; DGGGPS; geranylgeranyl diphosphate:sn-3-O-(geranylgeranyl)glycerol 1-phosphate geranylgeranyltransferase
Systematic name: geranylgeranyl diphosphate:3-(O-geranylgeranyl)-sn-glycerol 1-phosphate geranylgeranyltransferase
Comments: This enzyme is an integral-membrane protein that carries out the second prenyltransfer reaction involved in the formation of polar membrane lipids in Archaea. Requires a divalent metal cation, such as Mg2+ or Mn2+, for activity [2]. 4-Hydroxybenzoate, 1,4-dihydroxy 2-naphthoate, homogentisate and α-glycerophosphate cannot act as prenyl-acceptor substrates [2]. The other enzymes involved in the biosynthesis of polar lipids in Archaea are EC 1.1.1.261 (sn-glycerol-1-phosphate dehydrogenase), EC 2.5.1.41 (phosphoglycerol geranylgeranyltransferase), which, together with this enzyme, alkylates the hydroxy groups of glycerol 1-phosphate to yield unsaturated archaetidic acid, which is acted upon by EC 2.7.7.67 (CDP-archaeol synthase) to form CDP-unsaturated archaeol. The final step in the pathway involves the addition of L-serine, with concomitant removal of CMP, leading to the production of unsaturated archaetidylserine [3]. Belongs in the UbiA prenyltransferase family [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 124650-68-6
References:
1.  Zhang, D.-L., Daniels, L. and Poulter, C.D. Biosynthesis of archaebacterial membranes. Formation of isoprene ethers by a prenyl transfer reaction. J. Am. Chem. Soc. 112 (1990) 1264–1265.
2.  Hemmi, H., Shibuya, K., Takahashi, Y., Nakayama, T. and Nishino, T. (S)-2,3-Di-O-geranylgeranylglyceryl phosphate synthase from the thermoacidophilic archaeon Sulfolobus solfataricus. Molecular cloning and characterization of a membrane-intrinsic prenyltransferase involved in the biosynthesis of archaeal ether-linked membrane lipids. J. Biol. Chem. 279 (2004) 50197–50203. [DOI] [PMID: 15356000]
3.  Morii, H., Nishihara, M. and Koga, Y. CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase in the methanogenic archaeon Methanothermobacter thermoautotrophicus. J. Biol. Chem. 275 (2000) 36568–36574. [DOI] [PMID: 10960477]
[EC 2.5.1.42 created 1992, modified 2009]
 
 
EC 2.5.1.115     
Accepted name: homogentisate phytyltransferase
Reaction: phytyl diphosphate + homogentisate = diphosphate + 2-methyl-6-phytylbenzene-1,4-diol + CO2
For diagram of the homogentisate pathways, click here
Glossary: 2-methyl-6-phytylbenzene-1,4-diol = MPBQ
Other name(s): HPT; VTE2 (gene name)
Systematic name: phytyl diphosphate:homogentisate phytyltransferase
Comments: Requires Mg2+ for activity [3]. Involved in the biosynthesis of the vitamin E tocopherols. While the enzyme from the cyanobacterium Synechocystis PCC 6803 has an appreciable activity with geranylgeranyl diphosphate (EC 2.5.1.116, homogentisate geranylgeranyltransferase), the enzyme from the plant Arabidopsis thaliana has only a low activity with that substrate [1,3,4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Collakova, E. and DellaPenna, D. Isolation and functional analysis of homogentisate phytyltransferase from Synechocystis sp. PCC 6803 and Arabidopsis. Plant Physiol. 127 (2001) 1113–1124. [PMID: 11706191]
2.  Savidge, B., Weiss, J.D., Wong, Y.H., Lassner, M.W., Mitsky, T.A., Shewmaker, C.K., Post-Beittenmiller, D. and Valentin, H.E. Isolation and characterization of homogentisate phytyltransferase genes from Synechocystis sp. PCC 6803 and Arabidopsis. Plant Physiol. 129 (2002) 321–332. [DOI] [PMID: 12011362]
3.  Sadre, R., Gruber, J. and Frentzen, M. Characterization of homogentisate prenyltransferases involved in plastoquinone-9 and tocochromanol biosynthesis. FEBS Lett. 580 (2006) 5357–5362. [DOI] [PMID: 16989822]
4.  Yang, W., Cahoon, R.E., Hunter, S.C., Zhang, C., Han, J., Borgschulte, T. and Cahoon, E.B. Vitamin E biosynthesis: functional characterization of the monocot homogentisate geranylgeranyl transferase. Plant J. 65 (2011) 206–217. [DOI] [PMID: 21223386]
[EC 2.5.1.115 created 2014]
 
 
EC 2.5.1.116     
Accepted name: homogentisate geranylgeranyltransferase
Reaction: geranylgeranyl diphosphate + homogentisate = diphosphate + 6-geranylgeranyl-2-methylbenzene-1,4-diol + CO2
For diagram of the homogentisate pathways, click here
Glossary: 6-geranylgeranyl-2-methylbenzene-1,4-diol = MGGBQ
Other name(s): HGGT; slr1736 (gene name)
Systematic name: geranylgeranyl diphosphate:homogentisate geranylgeranyltransferase
Comments: Requires Mg2+ for activity. Involved in the biosynthesis of the vitamin E, tocotrienols. While the enzyme from the bacterium Synechocystis PCC 6803 has higher activity with phytyl diphosphate (EC 2.5.1.115, homogentisate phytyltransferase), the enzymes from barley, rice and wheat have only a low activity with that substrate [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Collakova, E. and DellaPenna, D. Isolation and functional analysis of homogentisate phytyltransferase from Synechocystis sp. PCC 6803 and Arabidopsis. Plant Physiol. 127 (2001) 1113–1124. [PMID: 11706191]
2.  Cahoon, E.B., Hall, S.E., Ripp, K.G., Ganzke, T.S., Hitz, W.D. and Coughlan, S.J. Metabolic redesign of vitamin E biosynthesis in plants for tocotrienol production and increased antioxidant content. Nat. Biotechnol. 21 (2003) 1082–1087. [DOI] [PMID: 12897790]
3.  Yang, W., Cahoon, R.E., Hunter, S.C., Zhang, C., Han, J., Borgschulte, T. and Cahoon, E.B. Vitamin E biosynthesis: functional characterization of the monocot homogentisate geranylgeranyl transferase. Plant J. 65 (2011) 206–217. [DOI] [PMID: 21223386]
[EC 2.5.1.116 created 2014]
 
 
EC 2.5.1.117     
Accepted name: homogentisate solanesyltransferase
Reaction: all-trans-nonaprenyl diphosphate + homogentisate = diphosphate + 2-methyl-6-all-trans-nonaprenylbenzene-1,4-diol + CO2
For diagram of the homogentisate pathways, click here
Glossary: 2-methyl-6-all-trans-nonaprenylbenzene-1,4-diol = 2-methyl-6-solanesylbenzene-1,4-diol = MSBQ
Other name(s): HST; PDS2 (gene name)
Systematic name: all-trans-nonaprenyl diphosphate:homogentisate nonaprenyltransferase
Comments: Requires Mg2+ for activity. Part of the biosynthesis pathway of plastoquinol-9. The enzymes purified from the plant Arabidopsis thaliana and the alga Chlamydomonas reinhardtii are also active in vitro with unsaturated C10-C20 prenyl diphosphates, producing main products that are not decarboxylated [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sadre, R., Gruber, J. and Frentzen, M. Characterization of homogentisate prenyltransferases involved in plastoquinone-9 and tocochromanol biosynthesis. FEBS Lett. 580 (2006) 5357–5362. [DOI] [PMID: 16989822]
2.  Sadre, R., Frentzen, M., Saeed, M. and Hawkes, T. Catalytic reactions of the homogentisate prenyl transferase involved in plastoquinone-9 biosynthesis. J. Biol. Chem. 285 (2010) 18191–18198. [DOI] [PMID: 20400515]
[EC 2.5.1.117 created 2014]
 
 
EC 3.7.1.2     
Accepted name: fumarylacetoacetase
Reaction: 4-fumarylacetoacetate + H2O = acetoacetate + fumarate
Other name(s): β-diketonase; fumarylacetoacetate hydrolase
Systematic name: 4-fumarylacetoacetate fumarylhydrolase
Comments: Also acts on other 3,5- and 2,4-dioxo acids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 9032-59-1
References:
1.  Connors, W.M. and Stotz, E. The purification and properties of a triacetic acid-hydrolyzing enzyme. J. Biol. Chem. 178 (1949) 881–890. [PMID: 18117010]
2.  Edwards, S.W. and Knox, W.E. Homogentisate metabolism: the isomerization of maleylacetoacetate by an enzyme which requires glutathione. J. Biol. Chem. 220 (1956) 79–91. [PMID: 13319328]
3.  Meister, A. and Greenstein, J.P. Enzymatic hydrolysis of 2,4-diketo acids. J. Biol. Chem. 175 (1948) 573–588. [PMID: 18880754]
[EC 3.7.1.2 created 1961]
 
 
EC 3.7.1.20     
Accepted name: 3-fumarylpyruvate hydrolase
Reaction: 3-fumarylpyruvate + H2O = fumarate + pyruvate
Other name(s): nagK (gene name); naaD (gene name)
Systematic name: 3-fumarylpyruvate hydrolase
Comments: The enzyme is involved in bacterial degradation of 5-substituted salicylates, including gentisate (5-hydroxysalicylate), 5-nitrosalicylate and 5-halosalicylates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Zhou, N.Y., Fuenmayor, S.L. and Williams, P.A. nag genes of Ralstonia (formerly Pseudomonas) sp. strain U2 encoding enzymes for gentisate catabolism. J. Bacteriol. 183 (2001) 700–708. [DOI] [PMID: 11133965]
2.  Qu, Y. and Spain, J.C. Molecular and biochemical characterization of the 5-nitroanthranilic acid degradation pathway in Bradyrhizobium sp. strain JS329. J. Bacteriol. 193 (2011) 3057–3063. [DOI] [PMID: 21498645]
[EC 3.7.1.20 created 2012]
 
 
EC 3.7.1.23     
Accepted name: maleylpyruvate hydrolase
Reaction: 3-maleylpyruvate + H2O = maleate + pyruvate
Glossary: 3-maleylpyruvate = (2Z)-4,6-dioxohept-2-enedioate
Other name(s): hbzF (gene name)
Systematic name: (2Z)-4,6-dioxohept-2-enedioate acylhydrolase
Comments: The enzyme, characterized from the bacterium Pseudomonas alcaligenes NCIMB 9867, catalyses the hydrolysis of 3-maleylpyruvate, the ring-cleavage product of gentisate. The enzyme can also act on a number of maleylpyruvate derivatives, such as (2E)-2-methyl-4,6-dioxohept-2-enedioate and (2E)-3-methyl-4,6-dioxohept-2-enedioate. Activated by Mn2+. May be identical to EC 3.7.1.5, acylpyruvate hydrolase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hopper, D.J., Chapman, P.J. and Dagley, S. The enzymic degradation of alkyl-substituted gentisates, maleates and malates. Biochem. J. 122 (1971) 29–40. [PMID: 5124802]
2.  Bayly, R.C., Chapman, P.J., Dagley, S. and Di Berardino, D. Purification and some properties of maleylpyruvate hydrolase and fumarylpyruvate hydrolase from Pseudomonas alcaligenes. J. Bacteriol. 143 (1980) 70–77. [PMID: 7400101]
3.  Liu, K., Liu, T.T. and Zhou, N.Y. HbzF catalyzes direct hydrolysis of maleylpyruvate in the gentisate pathway of Pseudomonas alcaligenes NCIMB 9867. Appl. Environ. Microbiol. 79 (2013) 1044–1047. [DOI] [PMID: 23204427]
[EC 3.7.1.23 created 2016]
 
 
EC 4.1.1.62     
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
References:
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 4.1.1.62 created 1972]
 
 
EC 5.2.1.2     
Accepted name: maleylacetoacetate isomerase
Reaction: 4-maleylacetoacetate = 4-fumarylacetoacetate
Other name(s): maleylacetoacetic isomerase; maleylacetone isomerase; maleylacetone cis-trans-isomerase
Systematic name: 4-maleylacetoacetate cis-trans-isomerase
Comments: Also acts on maleylpyruvate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 9023-75-0
References:
1.  Edwards, S.W. and Knox, W.E. Homogentisate metabolism: the isomerization of maleylacetoacetate by an enzyme which requires glutathione. J. Biol. Chem. 220 (1956) 79–91. [PMID: 13319328]
2.  Lack, L. Enzymic cis-trans isomerization of maleylpyruvic acid. J. Biol. Chem. 236 (1961) 2835–2840. [PMID: 14461395]
3.  Seltzer, S. Purification and properties of maleylacetone cis-trans isomerase from Vibrio 01. J. Biol. Chem. 248 (1973) 215–222. [PMID: 4692831]
[EC 5.2.1.2 created 1961]
 
 


Data © 2001–2020 IUBMB
Web site © 2005–2020 Andrew McDonald