Anthranilate 3-monooxygenase (FAD)
| Anthranilate 3-monooxygenase (FAD) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.14.8 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Anthranilate 3-monooxygenase (FAD) (EC 1.14.14.8, anthranilate 3-hydroxylase, anthranilate hydroxylase) is an enzyme with systematic name anthranilate,FAD:oxygen oxidoreductase (3-hydroxylating).[1] This enzyme catalyses the following chemical reaction
The three substrates of this enzyme are anthranilic acid, reduced flavin adenine dinucleotide (FADH2), and oxygen. It products are 3-hydroxyanthranilic acid, FAD, and water.[2] The bacterial enzyme from Geobacillus thermodenitrificans participates in tryptophan degradation.[1]
References
- 1 2 Liu X, Dong Y, Li X, Ren Y, Li Y, Wang W, Wang L, Feng L (February 2010). "Characterization of the anthranilate degradation pathway in Geobacillus thermodenitrificans NG80-2". Microbiology. 156 (Pt 2): 589–95. doi:10.1099/mic.0.031880-0. PMID 19942660.
- ↑ Enzyme 1.14.14.8 at KEGG Pathway Database.
External links
- Anthranilate+3-monooxygenase+(FAD) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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