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

L-tryptophan:FADH2 oxidoreductase (5-halogenating)

L-tryptophan + FADH2 + chloride + O2 + H+ = 5-chloro-L-tryptophan + FAD + 2 H2O [RN:R12031]

R12031

L-tryptophan [CPD:C00078];
FADH2 [CPD:C01352];
chloride [CPD:C00698];
O2 [CPD:C00007];
H+ [CPD:C00080]

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.

EC 1.14.19.58 created 2018

1  [PMID:15850981]

Zehner S, Kotzsch A, Bister B, Sussmuth RD, Mendez C, Salas JA, van Pee KH

A regioselective tryptophan 5-halogenase is involved in pyrroindomycin biosynthesis in Streptomyces rugosporus LL-42D005.

Chem Biol 12:445-52 (2005)
DOI:10.1016/j.chembiol.2005.02.005

[ag:AAU95674]

2  [PMID:19501593]

Zhu X, De Laurentis W, Leang K, Herrmann J, Ihlefeld K, van Pee KH, Naismith JH

Structural insights into regioselectivity in the enzymatic chlorination of tryptophan.

J Mol Biol 391:74-85 (2009)
DOI:10.1016/j.jmb.2009.06.008

[ag:AAU95674]