KEGG   ENZYME: 1.14.12.14
Entry
EC 1.14.12.14               Enzyme                                 
Name
2-aminobenzenesulfonate 2,3-dioxygenase;
2-aminosulfobenzene 2,3-dioxygenase
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and incorporation of two atoms of oxygen into the other donor
Sysname
2-aminobenzenesulfonate,NADH:oxygen oxidoreductase (2,3-hydroxylating, ammonia-forming)
Reaction(IUBMB)
2-aminobenzenesulfonate + NADH + H+ + O2 = 2,3-dihydroxybenzenesulfonate + NH3 + NAD+ [RN:R05156]
Reaction(KEGG)
R05156;
(other) R05294
Substrate
2-aminobenzenesulfonate [CPD:C06333];
NADH [CPD:C00004];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product
2,3-dihydroxybenzenesulfonate [CPD:C06336];
NH3 [CPD:C00014];
NAD+ [CPD:C00003]
History
EC 1.14.12.14 created 1999
Pathway
ec00362  Benzoate degradation
ec00623  Toluene degradation
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K15766  2-aminobenzenesulfonate 2,3-dioxygenase subunit alpha
K15767  2-aminobenzenesulfonate 2,3-dioxygenase subunit beta
Reference
1  [PMID:8002948]
  Authors
Junker F, Field JA, Bangerter F, Ramsteiner K, Kohler HP, Joannou CL, Mason JR, Leisinger T, Cook AM.
  Title
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.
  Journal
Biochem J 300 ( Pt 2):429-36 (1994)
DOI:10.1042/bj3000429
Reference
2  [PMID:8075807]
  Authors
Junker F, Leisinger T, Cook AM
  Title
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.
  Journal
Microbiology 140 ( Pt 7):1713-22 (1994)
DOI:10.1099/13500872-140-7-1713
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.14.12.14
IUBMB Enzyme Nomenclature: 1.14.12.14
ExPASy - ENZYME nomenclature database: 1.14.12.14
UM-BBD (Biocatalysis/Biodegradation Database): 1.14.12.14
BRENDA, the Enzyme Database: 1.14.12.14
CAS: 156621-16-8

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