| Entry |
|
|---|
| 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
 |
|---|
| Sysname |
anthranilate,NADPH:oxygen oxidoreductase (3-hydroxylating,
deaminating) |
|---|
| Reaction(IUBMB) |
anthranilate + NADPH + H+ + O2 = 2,3-dihydroxybenzoate + NADP+ + NH3
[RN:R00980] |
|---|
| Reaction(KEGG) |
R00980
 |
|---|
| 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 |
PATH: ec00362 Benzoate degradation via hydroxylation
PATH: ec00629 Carbazole degradation
PATH: ec00910 Nitrogen metabolism |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:3793735]
Powlowski JB, Dagley S, Massey V, Ballou DP.
Properties of anthranilate hydroxylase (deaminating), a flavoprotein
from Trichosporon cutaneum.
J. Biol. Chem. 262 (1987) 69-74.
Trichosporon cutaneum |
|---|
Reference
Authors
Title
Journal
Organism
|
2 [PMID:6501219]
Subramanian V, Vaidyanathan CS.
Anthranilate hydroxylase from Aspergillus niger: new type of
NADPH-linked nonheme iron monooxygenase.
J. Bacteriol. 160 (1984) 651-5.
Aspergillus niger [GN:ang] |
|---|
| Other DBs |
ExplorEnz - The Enzyme Database: 1.14.13.35
IUBMB Enzyme Nomenclature: 1.14.13.35
ExPASy - ENZYME nomenclature database: 1.14.13.35
UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.35
BRENDA, the Enzyme Database: 1.14.13.35
CAS: 37256-68-1 |
|---|
