3-hydroxybenzoate 2-monooxygenase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC no. | 1.14.99.23 | ||||||||
CAS no. | 73507-96-7 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
|
In enzymology, a 3-hydroxybenzoate 2-monooxygenase (EC 1.14.99.23) is an enzyme that catalyzes the chemical reaction
- 3-hydroxybenzoate + AH2 + O2 2,3-dihydroxybenzoate + A + H2O
The 3 substrates of this enzyme are 3-hydroxybenzoate, an electron acceptor AH2, and O2, whereas its 3 products are 2,3-dihydroxybenzoate, the reduction product A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is 3-hydroxybenzoate,hydrogen-donor:oxygen oxidoreductase (2-hydroxylating). Other names in common use include 3-hydroxybenzoate 2-hydroxylase, and 3-HBA-2-hydroxylase. This enzyme participates in benzoate degradation via hydroxylation.
References
- Daumy GO, McColl AS (1982). "Induction of 3-hydroxybenzoate 2-hydroxylase in a Pseudomonas testosteroni mutant". J. Bacteriol. 149 (1): 384–5. PMC 216637. PMID 7054148.
Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14) | |
---|---|
1.14.11: 2-oxoglutarate | |
1.14.13: NADH or NADPH | |
1.14.14: reduced flavin or flavoprotein | |
1.14.15: reduced iron–sulfur protein | |
1.14.16: reduced pteridine (BH4 dependent) | |
1.14.17: reduced ascorbate | |
1.14.18-19: other | |
1.14.99 - miscellaneous |
Enzymes | |
---|---|
Activity | |
Regulation | |
Classification | |
Kinetics | |
Types |
|
This EC 1.14 enzyme-related article is a stub. You can help Misplaced Pages by expanding it. |