ExplorEnz: EC 1.14.19.58

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1.14.19.58

Accepted name:

tryptophan 5-halogenase

Reaction:

L-tryptophan + FADH₂ + chloride + O₂ + H⁺ = 5-chloro-L-tryptophan + FAD + 2 H₂O

For diagram of chlorotryptophan biosynthesis, click here

Other name(s):

pyrH (gene name)

Systematic name:

L-tryptophan:FADH₂ oxidoreductase (5-halogenating)

Comments:

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.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Zehner, S., Kotzsch, A., Bister, B., Sussmuth, R.D., Mendez, C., Salas, J.A. and van Pee, K.H. A regioselective tryptophan 5-halogenase is involved in pyrroindomycin biosynthesis in Streptomyces rugosporus LL-42D005. Chem. Biol. 12 (2005) 445–452. [DOI] [PMID: 15850981]
2.	Zhu, X., De Laurentis, W., Leang, K., Herrmann, J., Ihlefeld, K., van Pee, K.H. and Naismith, J.H. Structural insights into regioselectivity in the enzymatic chlorination of tryptophan. J. Mol. Biol. 391 (2009) 74–85. [DOI] [PMID: 19501593]

[EC 1.14.19.58 created 2018]