IUBMB Enzyme Nomenclature

EC 1.14.13.2

Accepted name: 4-hydroxybenzoate 3-monooxygenase

Reaction: 4-hydroxybenzoate + NADPH + H+ + O2 = protocatechuate + NADP+ + H2O

For diagram click here.

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, EXPASY, KEGG, Metacyc, PDB, UM-BBD, 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. [PMID: 8706756]

[EC 1.14.13.2 created 1972, modified 1999]


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