Biology:2-aminobenzenesulfonate 2,3-dioxygenase
| 2-aminobenzenesulfonate 2,3-dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.14.12.14 | ||||||||
| CAS number | 156621-16-8 | ||||||||
| 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 | ||||||||
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In enzymology, a 2-aminobenzenesulfonate 2,3-dioxygenase (EC 1.14.12.14) is an enzyme that catalyzes the chemical reaction
- 2-aminobenzenesulfonate + NADH + H+ + O2 [math]\displaystyle{ \rightleftharpoons }[/math] 2,3-dihydroxybenzenesulfonate + NH3 + NAD+
The 4 substrates of this enzyme are 2-aminobenzenesulfonate, NADH, H+, and O2, whereas its 3 products are 2,3-dihydroxybenzenesulfonate, NH3, and NAD+.
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 derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms o oxygen into the other donor. The systematic name of this enzyme class is 2-aminobenzenesulfonate,NADH:oxygen oxidoreductase (2,3-hydroxylating, ammonia-forming). This enzyme is also called 2-aminosulfobenzene 2,3-dioxygenase. This enzyme participates in benzoate degradation via hydroxylation.
References
- "Oxygenation and spontaneous deamination of 2-aminobenzenesulphonic acid in Alcaligenes sp. strain O-1 with subsequent meta ring cleavage and spontaneous desulphonation to 2-hydroxymuconic acid". Biochem. J. 300: 429–36. June 1, 1994. PMID 8002948.
- "3-Sulphocatechol 2,3-dioxygenase and other dioxygenases (EC 1.13.11.2 and EC 1.14.12.-) in the degradative pathways of 2-aminobenzenesulphonic, benzenesulphonic and 4-toluenesulphonic acids in Alcaligenes sp. strain O-1". Microbiology 140 (7): 1713–22. July 1994. doi:10.1099/13500872-140-7-1713. PMID 8075807.
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