KEGG   ENZYME: 1.14.13.35Help
Entry
EC 1.14.13.35               Enzyme                                 
Name
anthranilate 3-monooxygenase (deaminating);
anthranilate hydroxylase;
anthranilate 2,3-dioxygenase (deaminating);
anthranilate hydroxylase (deaminating);
anthranilic hydroxylase;
anthranilate 2,3-hydroxylase (deaminating)
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
BRITE hierarchy
Sysname
anthranilate,NADPH:oxygen oxidoreductase (3-hydroxylating, deaminating)
Reaction(IUBMB)
anthranilate + NADPH + H+ + O2 = 2,3-dihydroxybenzoate + NADP+ + NH3 [RN:R00980]
Reaction(KEGG)
Substrate
anthranilate [CPD:C00108];
NADPH [CPD:C00005];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product
2,3-dihydroxybenzoate [CPD:C00196];
NADP+ [CPD:C00006];
NH3 [CPD:C00014]
Comment
The enzyme from Aspergillus niger is an iron protein; that from the yeast Trichosporon cutaneum is a flavoprotein (FAD).
Pathway
Aminobenzoate degradation
Reference
1  [PMID:3793735]
  Authors
Powlowski JB, Dagley S, Massey V, Ballou DP.
  Title
Properties of anthranilate hydroxylase (deaminating), a flavoprotein from Trichosporon cutaneum.
  Journal
J. Biol. Chem. 262 (1987) 69-74.
  Organism
Trichosporon cutaneum
Reference
2  [PMID:6501219]
  Authors
Subramanian V, Vaidyanathan CS.
  Title
Anthranilate hydroxylase from Aspergillus niger: new type of NADPH-linked nonheme iron monooxygenase.
  Journal
J. Bacteriol. 160 (1984) 651-5.
  Organism
Aspergillus niger [GN:ang]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 
CAS: 
37256-68-1
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