The Enzyme Database

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EC 1.6.5.7     
Accepted name: 2-hydroxy-1,4-benzoquinone reductase
Reaction: 2-hydroxy-1,4-benzoquinone + NADH + H+ = hydroxyquinol + NAD+
For diagram of 4-nitrophenol metabolism, click here
Glossary: hydroxyquinol = 1,2,4-trihydroxybenzene
Other name(s): hydroxybenzoquinone reductase; 1,2,4-trihydroxybenzene:NAD oxidoreductase
Systematic name: NADH:2-hydroxy-1,4-benzoquinone oxidoreductase
Comments: A flavoprotein (FMN) that differs in substrate specificity from other quinone reductases. The enzyme in Burkholderia cepacia is inducible by 2,4,5-trichlorophenoxyacetate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 214466-94-1
References:
1.  Zaborina, O., Daubaras, D.L., Zago, A., Xun, L., Saido, K. , Klem,T., Nikolic, D. and Chakrabarty, A.M. Novel pathway for conversion of chlorohydroxyquinol to maleylacetate in Burkholderia cepacia AC1100. J. Bacteriol. 180 (1998) 4667–4675. [PMID: 9721310]
[EC 1.6.5.7 created 2000, modified 2004]
 
 
EC 1.12.99.5      
Deleted entry:  3,4-dihydroxyquinoline 2,4-dioxygenase. Identical to EC 1.13.11.47, 3-hydroxy-4-oxoquinoline 2,4-dioxygenase
[EC 1.12.99.5 created 1999, deleted 2001]
 
 
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 1.14.12.16     
Accepted name: 2-hydroxyquinoline 5,6-dioxygenase
Reaction: quinolin-2-ol + NADH + H+ + O2 = 2,5,6-trihydroxy-5,6-dihydroquinoline + NAD+
For diagram of reaction, click here
Other name(s): 2-oxo-1,2-dihydroquinoline 5,6-dioxygenase; quinolin-2-ol 5,6-dioxygenase; quinolin-2(1H)-one 5,6-dioxygenase
Systematic name: quinolin-2-ol,NADH:oxygen oxidoreductase (5,6-hydroxylating)
Comments: 3-Methylquinolin-2-ol, quinolin-8-ol and quinolin-2,8-diol are also substrates. Quinolin-2-ols exist largely as their quinolin-2(1H)-one tautomers
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 172399-50-7
References:
1.  Schach, S.B., Tshisuaka, B., Fetzner, S. and Lingens, F. Quinoline 2-oxidoreductase and 2-oxo-1,2-dihydroquinoline 5,6-dioxygenase from Comamonas testosteroni 63. The first two enzymes in quinoline and 3-methylquinoline degradation. Eur. J. Biochem. 232 (1995) 536–544. [DOI] [PMID: 7556204]
[EC 1.14.12.16 created 1999]
 
 
EC 1.14.13.61     
Accepted name: 2-hydroxyquinoline 8-monooxygenase
Reaction: quinolin-2-ol + NADH + H+ + O2 = quinolin-2,8-diol + NAD+ + H2O
Other name(s): 2-oxo-1,2-dihydroquinoline 8-monooxygenase
Systematic name: quinolin-2(1H)-one,NADH:oxygen oxidoreductase (8-oxygenating)
Comments: Requires iron. Quinolin-2-ol exists largely as the quinolin-2(1H)-one tautomer.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 166799-89-9
References:
1.  Rosche, B., Tshisuaka, B., Fetzner, S. and Lingens, F. 2-Oxo-1,2-dihydroquinoline 8-monooxygenase, a two-component enzyme system from Pseudomonas putida 86. J. Biol. Chem. 270 (1995) 17836–17842. [DOI] [PMID: 7629085]
[EC 1.14.13.61 created 1999]
 
 
EC 1.14.13.62     
Accepted name: 4-hydroxyquinoline 3-monooxygenase
Reaction: quinolin-4-ol + NADH + H+ + O2 = quinolin-3,4-diol + NAD+ + H2O
Other name(s): quinolin-4(1H)-one 3-monooxygenase
Systematic name: quinolin-4(1H)-one,NADH:oxygen oxidoreductase (3-oxygenating)
Comments: Quinolin-4-ol exists largely as the quinolin-4(1H)-one tautomer.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 144378-37-0
References:
1.  Block, D.W. and Lingens, F. Microbial metabolism of quinoline and related compounds. XIV. Purification and properties of 1H-3-hydroxy-4-oxoquinoline oxygenase, a new estradiol cleavage enzyme from Pseudomonas putida strain 33/1. Biol. Chem. Hoppe Seyler 373 (1992) 249–254. [PMID: 1627263]
[EC 1.14.13.62 created 1999]
 
 
EC 1.14.13.65      
Deleted entry:  2-hydroxyquinoline 8-monooxygenase
[EC 1.14.13.65 created 1999, deleted 2006]
 
 
EC 1.14.13.182     
Accepted name: 2-heptyl-3-hydroxy-4(1H)-quinolone synthase
Reaction: 2-heptyl-4(1H)-quinolone + NADH + H+ + O2 = 2-heptyl-3-hydroxy-4(1H)-quinolone + NAD+ + H2O
Glossary: 2-heptyl-4(1H)-quinolone = 2-heptyl-4-hydroxyquinoline
2-heptyl-3-hydroxy-4(1H)-quinolone = 2-heptyl-3,4-dihydroxyquinoline
Other name(s): PqsH; 2-heptyl-3,4-dihydroxyquinoline synthase
Systematic name: 2-heptyl-4(1H)-quinolone,NADH:oxygen oxidoreductase (3-hydroxylating)
Comments: The enzyme from the bacterium Pseudomonas aeruginosa catalyses the terminal step in biosynthesis of the signal molecule 2-heptyl-3,4-dihydroxyquinoline that plays a role in regulation of virulence genes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Schertzer, J.W., Brown, S.A. and Whiteley, M. Oxygen levels rapidly modulate Pseudomonas aeruginosa social behaviours via substrate limitation of PqsH. Mol. Microbiol. 77 (2010) 1527–1538. [DOI] [PMID: 20662781]
[EC 1.14.13.182 created 2013]
 
 
EC 1.14.13.219     
Accepted name: resorcinol 4-hydroxylase (NADPH)
Reaction: resorcinol + NADPH + H+ + O2 = hydroxyquinol + NADP+ + H2O
Glossary: resorcinol = benzene-1,3-diol
hydroxyquinol = benzene-1,2,4-triol
Systematic name: resorcinol,NADPH:oxygen oxidoreductase (4-hydroxylating)
Comments: The enzyme, characterized from the bacterium Corynebacterium glutamicum, is a single-component hydroxylase. The enzyme has no activity with NADH. cf. EC 1.14.13.220, resorcinol 4-hydroxylase (NADH), and EC 1.14.14.27, resorcinol 4-hydroxylase (FADH2).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Huang, Y., Zhao, K.X., Shen, X.H., Chaudhry, M.T., Jiang, C.Y. and Liu, S.J. Genetic characterization of the resorcinol catabolic pathway in Corynebacterium glutamicum. Appl. Environ. Microbiol. 72 (2006) 7238–7245. [DOI] [PMID: 16963551]
[EC 1.14.13.219 created 2016]
 
 
EC 1.14.13.220     
Accepted name: resorcinol 4-hydroxylase (NADH)
Reaction: resorcinol + NADH + H+ + O2 = hydroxyquinol + NAD+ + H2O
Glossary: resorcinol = benzene-1,3-diol
hydroxyquinol = benzene-1,2,4-triol
Other name(s): tsdB (gene name)
Systematic name: resorcinol,NADH:oxygen oxidoreductase (4-hydroxylating)
Comments: The enzyme, characterized from the bacterium Rhodococcus jostii RHA1, is a single-component hydroxylase. The enzyme has no activity with NADPH. cf. EC 1.14.13.219, resorcinol 4-hydroxylase (NADPH), and EC 1.14.14.27, resorcinol 4-hydroxylase (FADH2).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kasai, D., Araki, N., Motoi, K., Yoshikawa, S., Iino, T., Imai, S., Masai, E. and Fukuda, M. γ-Resorcylate catabolic-pathway genes in the soil actinomycete Rhodococcus jostii RHA1. Appl. Environ. Microbiol. 81 (2015) 7656–7665. [DOI] [PMID: 26319878]
[EC 1.14.13.220 created 2016]
 
 
EC 1.14.14.27     
Accepted name: resorcinol 4-hydroxylase (FADH2)
Reaction: resorcinol + FADH2 + O2 = hydroxyquinol + FAD + H2O
Glossary: resorcinol = benzene-1,3-diol
hydroxyquinol = benzene-1,2,4-triol
Other name(s): graA (gene name)
Systematic name: resorcinol,FADH2:oxygen oxidoreductase (4-hydroxylating)
Comments: The enzyme, characterized from the bacterium Rhizobium sp. strain MTP-10005, uses FADH2 as a substrate rather than a cofactor. FADH2 is provided by a dedicated EC 1.5.1.36, flavin reductase (NADH). The enzyme participates in the degradation of γ-resorcylate and resorcinol. cf. EC 1.14.13.220, resorcinol 4-hydroxylase (NADH), and EC 1.14.13.219, resorcinol 4-hydroxylase (NADPH).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ohta, Y. and Ribbons, D.W. Bacterial metabolism of resorcinylic compounds: purification and properties of orcinol hydroxylase and resorcinol hydroxylase from Pseudomonas putida ORC. Eur. J. Biochem. 61 (1976) 259–269. [DOI] [PMID: 1280]
2.  Yoshida, M., Oikawa, T., Obata, H., Abe, K., Mihara, H. and Esaki, N. Biochemical and genetic analysis of the γ-resorcylate (2,6-dihydroxybenzoate) catabolic pathway in Rhizobium sp. strain MTP-10005: identification and functional analysis of its gene cluster. J. Bacteriol. 189 (2007) 1573–1581. [DOI] [PMID: 17158677]
[EC 1.14.14.27 created 2016]
 
 


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