| Entry |
|
|---|
| Name |
4-hydroxybenzoate 3-monooxygenase [NAD(P)H];
4-hydroxybenzoate 3-monooxygenase (reduced nicotinamide adenine
dinucleotide (phosphate));
4-hydroxybenzoate-3-hydroxylase;
4-hydroxybenzoate 3-hydroxylase |
|---|
| Class |
Oxidoreductases;
Acting on paired donors, with O2 as oxidant and incorporation or
reduction of oxygen. The oxygen incorporated need not be derived
from O2;
With NADH or NADPH as one donor, and incorporation of one atom of
oxygen into the other donor
 |
|---|
| Sysname |
4-hydroxybenzoate,NAD(P)H:oxygen oxidoreductase (3-hydroxylating) |
|---|
| Reaction(IUBMB) |
4-hydroxybenzoate + NAD(P)H + H+ + O2 = 3,4-dihydroxybenzoate +
NAD(P)+ + H2O [RN:R01296 R01298] |
|---|
| Reaction(KEGG) |
R01296 R01298
 |
|---|
| Substrate |
4-hydroxybenzoate [CPD:C00156];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080];
O2 [CPD:C00007] |
|---|
| Product |
3,4-dihydroxybenzoate [CPD:C00230];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006];
H2O [CPD:C00001] |
|---|
| Cofactor |
FAD [CPD:C00016] |
|---|
| Comment |
A flavoprotein (FAD). The enzyme from Corynebacterium cyclohexanicum
is highly specific for 4-hydroxybenzoate, but uses NADH and NADPH at
approximately equal rates (cf. EC 1.14.13.2 4-hydroxybenzoate
3-monooxygenase). It is less specific for NADPH than EC 1.14.13.2. |
|---|
| Pathway |
PATH: ec00362 Benzoate degradation via hydroxylation
PATH: ec00623 2,4-Dichlorobenzoate degradation
PATH: ec01100 Metabolic pathways |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:3971979]
Fujii T, Kaneda T.
Purification and properties of NADH/NADPH-dependent
p-hydroxybenzoate hydroxylase from Corynebacterium cyclohexanicum.
Eur. J. Biochem. 147 (1985) 97-104.
Corynebacterium cyclohexanicum |
|---|
Reference
Authors
Title
Journal
Organism
|
2 [PMID:8706756]
Seibold B, Matthes M, Eppink MH, Lingens F, Van Berkel WJ, 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) 469-78.
Pseudomonas sp. |
|---|
| Other DBs |
ExplorEnz - The Enzyme Database: 1.14.13.33
IUBMB Enzyme Nomenclature: 1.14.13.33
ExPASy - ENZYME nomenclature database: 1.14.13.33
BRENDA, the Enzyme Database: 1.14.13.33
CAS: 95471-33-3 |
|---|
