The Enzyme Database

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EC 1.13.11.35     
Accepted name: pyrogallol 1,2-oxygenase
Reaction: 1,2,3-trihydroxybenzene + O2 = (2Z,4E)-2-hydroxyhexa-2,4-dienedioate
Glossary: (2Z,4E)-2-hydroxyhexa-2,4-dienedioate = (2Z,4E)-2-hydroxymuconate
1,2,3-trihydroxybenzene = pyrogallol
Other name(s): pyrogallol 1,2-dioxygenase; 1,2,3-trihydroxybenzene:oxygen 1,2-oxidoreductase (decyclizing)
Systematic name: 1,2,3-trihydroxybenzene:oxygen 1,2-oxidoreductase (ring-opening)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 78310-68-6
References:
1.  Groseclose, E.E. and Ribbons, D.W. Metabolism of resorcinylic compounds by bacteria: new pathway for resorcinol catabolism in Azotobacter vinelandii. J. Bacteriol. 146 (1981) 460–466. [PMID: 7217008]
[EC 1.13.11.35 created 1984, modified 2012]
 
 
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 1.14.14.20     
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 1.14.14.27     
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]
 
 
EC 4.1.1.103     
Accepted name: γ-resorcylate decarboxylase
Reaction: 2,6-dihydroxybenzoate = 1,3-dihydroxybenzene + CO2
Glossary: 2,6-dihydroxybenzoate = γ-resorcylate
1,3-dihydroxybenzene = resorcinol
Other name(s): graF (gene name); tsdA (gene name)
Systematic name: 2,6-dihydroxybenzoate carboxy-lyase
Comments: The enzyme, characterized from several bacterial strains, is involved in the degradation of γ-resorcylate. It contains a zinc ion and a water molecule at the active site. The reaction is reversible, but equilibrium greatly favors the decarboxylation reaction.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Yoshida, M., Fukuhara, N. and Oikawa, T. Thermophilic, reversible γ-resorcylate decarboxylase from Rhizobium sp. strain MTP-10005: purification, molecular characterization, and expression. J. Bacteriol. 186 (2004) 6855–6863. [DOI] [PMID: 15466039]
2.  Ishii, Y., Narimatsu, Y., Iwasaki, Y., Arai, N., Kino, K. and Kirimura, K. Reversible and nonoxidative γ-resorcylic acid decarboxylase: characterization and gene cloning of a novel enzyme catalyzing carboxylation of resorcinol, 1,3-dihydroxybenzene, from Rhizobium radiobacter. Biochem. Biophys. Res. Commun. 324 (2004) 611–620. [DOI] [PMID: 15474471]
3.  Matsui, T., Yoshida, T., Yoshimura, T. and Nagasawa, T. Regioselective carboxylation of 1,3-dihydroxybenzene by 2,6-dihydroxybenzoate decarboxylase of Pandoraea sp. 12B-2. Appl. Microbiol. Biotechnol. 73 (2006) 95–102. [DOI] [PMID: 16683134]
4.  Goto, M., Hayashi, H., Miyahara, I., Hirotsu, K., Yoshida, M. and Oikawa, T. Crystal structures of nonoxidative zinc-dependent 2,6-dihydroxybenzoate (γ-resorcylate) decarboxylase from Rhizobium sp. strain MTP-10005. J. Biol. Chem. 281 (2006) 34365–34373. [DOI] [PMID: 16963440]
5.  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 4.1.1.103 created 2016]
 
 


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