ExplorEnz: EC 1.14.13.2

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1.14.13.2

Accepted name:

4-hydroxybenzoate 3-monooxygenase

Reaction:

4-hydroxybenzoate + NADPH + H⁺ + O₂ = 3,4-dihydroxybenzoate + NADP⁺ + H₂O

For diagram of benzoate metabolism, click here

Glossary:

3,4-dihydroxybenzoate = protocatechuate

Other name(s):

p-hydroxybenzoate hydrolyase; p-hydroxybenzoate hydroxylase; 4-hydroxybenzoate 3-hydroxylase; 4-hydroxybenzoate monooxygenase; 4-hydroxybenzoic hydroxylase; p-hydroxybenzoate-3-hydroxylase; p-hydroxybenzoic acid hydrolase; p-hydroxybenzoic acid hydroxylase; p-hydroxybenzoic hydroxylase

Systematic name:

4-hydroxybenzoate,NADPH:oxygen oxidoreductase (3-hydroxylating)

Comments:

A flavoprotein (FAD). Most enzymes from Pseudomonas are highly specific for NADPH (cf. EC 1.14.13.33 4-hydroxybenzoate 3-monooxygenase [NAD(P)H]).

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9059-23-8

References:

1.	Hosokawa, K. and Stanier, R.Y. Crystallization and properties of p-hydroxybenzoate hydroxylase from Pseudomonas putida. J. Biol. Chem. 241 (1966) 2453–2460. [PMID: 4380381]
2.	Howell, L.G., Spector, T. and Massey, V. Purification and properties of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. J. Biol. Chem. 247 (1972) 4340–4350. [PMID: 4402514]
3.	Spector, T. and Massey, V. Studies on the effector specificity of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. J. Biol. Chem. 247 (1972) 4679–4687. [PMID: 4402938]
4.	Spector, T. and Massey, V. p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Evidence for an oxygenated flavin intermediate. J. Biol. Chem. 247 (1972) 5632–5636. [PMID: 4403446]
5.	Spector, T. and Massey, V. p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Reactivity with oxygen. J. Biol. Chem. 247 (1972) 7123–7127. [PMID: 4404745]
6.	Seibold, B., Matthes, M., Eppink, M.H., Lingens, F., Van Berkel, W.J. and Muller, R. 4-Hydroxybenzoate hydroxylase from Pseudomonas sp. CBS3. Purification, characterization, gene cloning, sequence analysis and assignment of structural features determining the coenzyme specificity. Eur. J. Biochem. 239 (1996) 469–478. [DOI] [PMID: 8706756]

[EC 1.14.13.2 created 1972, modified 1999]