| EC |
1.14.13.35 |
| Accepted name: |
anthranilate 3-monooxygenase (deaminating) |
| Reaction: |
anthranilate + NADPH + H+ + O2 = 2,3-dihydroxybenzoate + NADP+ + NH3 |
| Other name(s): |
anthranilate hydroxylase; anthranilate 2,3-dioxygenase (deaminating); anthranilate hydroxylase (deaminating); anthranilic hydroxylase; anthranilate 2,3-hydroxylase (deaminating) |
| Systematic name: |
anthranilate,NADPH:oxygen oxidoreductase (3-hydroxylating, deaminating) |
| Comments: |
The enzyme from Aspergillus niger is an iron protein; that from the yeast Trichosporon cutaneum is a flavoprotein (FAD). |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-68-1 |
| References: |
| 1. |
Powlowski, J.B., Dagley, S., Massey, V. and Ballou, D.P. Properties of anthranilate hydroxylase (deaminating), a flavoprotein from Trichosporon cutaneum. J. Biol. Chem. 262 (1987) 69–74. [PMID: 3793735] |
| 2. |
Subramanian, V. and Vaidyanathan, C.S. Anthranilate hydroxylase from Aspergillus niger: new type of NADPH-linked nonheme iron monooxygenase. J. Bacteriol. 160 (1984) 651–655. [PMID: 6501219] |
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| [EC 1.14.13.35 created 1972 as EC 1.14.12.2, transferred 1990 to EC 1.14.13.35] |
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