ENZYME entry: EC 1.14.19.58
Accepted Name |
Tryptophan 5-halogenase.
|
Reaction catalysed |
L-tryptophan + FADH(2) + chloride + O(2) + H(+) <=> 5-chloro-L-tryptophan + FAD + 2 H(2)O |
Comment(s) |
- A flavin-dependent halogenase.
- The enzyme from the bacterium Streptomyces rugosporus catalyzes
halogenation of the C-5 position of tryptophan during the
biosynthesis of the antibiotic compound pyrroindomycin B.
- It utilizes molecular oxygen to oxidize the FADH(2) cofactor, giving
C4a-hydroperoxyflavin, which then reacts with chloride to produce a
hypochlorite ion.
- The latter reacts with an active site lysine to generate a
chloramine, which chlorinates the substrate.
- cf. EC 1.14.19.59 and EC 1.14.19.9.
|
Cross-references |
BRENDA | 1.14.19.58 |
EC2PDB | 1.14.19.58 |
ExplorEnz | 1.14.19.58 |
PRIAM enzyme-specific profiles | 1.14.19.58 |
KEGG Ligand Database for Enzyme Nomenclature | 1.14.19.58 |
IUBMB Enzyme Nomenclature | 1.14.19.58 |
IntEnz | 1.14.19.58 |
MEDLINE | Find literature relating to 1.14.19.58 |
MetaCyc | 1.14.19.58 |
Rhea expert-curated reactions | 1.14.19.58 |
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