EC	1.14.19.59
Accepted name:	tryptophan 6-halogenase
Reaction:	(1) L-tryptophan + FADH2 + chloride + O2 + H+ = 6-chloro-L-tryptophan + FAD + 2 H2O (2) D-tryptophan + FADH2 + chloride + O2 + H+ = 6-chloro-D-tryptophan + FAD + 2 H2O
Other name(s):	sttH (gene name); thdH (gene name)
Systematic name:	L-tryptophan:FADH2 oxidoreductase (6-halogenating)
Comments:	The enzyme is a flavin-dependent halogenase that has been described from several bacterial species. 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 1.14.19.58, tryptophan 5-halogenase, and EC 1.14.19.9, tryptophan 7-halogenase.
References:	1.  Zeng, J. and Zhan, J. Characterization of a tryptophan 6-halogenase from Streptomyces toxytricini. Biotechnol. Lett. 33 (2011) 1607–1613. [PMID: 21424165] 2.  Milbredt, D., Patallo, E.P. and van Pee, K.H. A tryptophan 6-halogenase and an amidotransferase are involved in thienodolin biosynthesis. ChemBioChem 15 (2014) 1011–1020. [PMID: 24692213] 3.  Shepherd, S.A., Menon, B.R., Fisk, H., Struck, A.W., Levy, C., Leys, D. and Micklefield, J. A structure-guided switch in the regioselectivity of a tryptophan halogenase. ChemBioChem 17 (2016) 821–824. [PMID: 26840773]
[EC 1.14.19.59 created 2018]