Entry |
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Name |
tryptophan 5-halogenase;
pyrH (gene name)
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Class |
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With oxidation of a pair of donors resulting in the reduction of O2 to two molecules of water
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Sysname |
L-tryptophan:FADH2 oxidoreductase (5-halogenating)
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Reaction(IUBMB) |
L-tryptophan + FADH2 + chloride + O2 + H+ = 5-chloro-L-tryptophan + FAD + 2 H2O [RN: R12031]
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Reaction(KEGG) |
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Substrate |
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Product |
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Comment |
A flavin-dependent halogenase. The enzyme from the bacterium Streptomyces rugosporus catalyses halogenation of the C-5 position of tryptophan during the biosynthesis of the antibiotic compound pyrroindomycin B. It utilizes molecular oxygen to oxidize the FADH2 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, tryptophan 6-halogenase and EC 1.14.19.9, tryptophan 7-halogenase.
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History |
EC 1.14.19.58 created 2018
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Orthology |
K22693 | tryptophan 5-halogenase |
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Genes |
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Reference |
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Authors |
Zehner S, Kotzsch A, Bister B, Sussmuth RD, Mendez C, Salas JA, van Pee KH |
Title |
A regioselective tryptophan 5-halogenase is involved in pyrroindomycin biosynthesis in Streptomyces rugosporus LL-42D005. |
Journal |
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Sequence |
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Reference |
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Authors |
Zhu X, De Laurentis W, Leang K, Herrmann J, Ihlefeld K, van Pee KH, Naismith JH |
Title |
Structural insights into regioselectivity in the enzymatic chlorination of tryptophan. |
Journal |
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Sequence |
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Other DBs |
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