The Enzyme Database

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EC 1.14.19.9     
Accepted name: tryptophan 7-halogenase
Reaction: tryptophan + FADH2 + chloride + O2 + H+ = 7-chloro-L-tryptophan + FAD + 2 H2O
For diagram of rebeccamycin biosynthesis, click here
Other name(s): PrnA; RebH
Systematic name: L-tryptophan:FADH2 oxidoreductase (7-halogenating)
Comments: In the bacterium Lechevalieria aerocolonigenes the enzyme catalyses the initial step in the biosynthesis of rebeccamycin [2]. Also acts on bromide ion.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Dong, C., Kotzsch, A., Dorward, M., van Pee, K.H. and Naismith, J.H. Crystallization and X-ray diffraction of a halogenating enzyme, tryptophan 7-halogenase, from Pseudomonas fluorescens. Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 1438–1440. [PMID: 15272170]
2.  Yeh, E., Garneau, S. and Walsh, C.T. Robust in vitro activity of RebF and RebH, a two-component reductase/halogenase, generating 7-chlorotryptophan during rebeccamycin biosynthesis. Proc. Natl. Acad. Sci. USA 102 (2005) 3960–3965. [PMID: 15743914]
3.  Bitto, E., Huang, Y., Bingman, C.A., Singh, S., Thorson, J.S. and Phillips Jr., G.N. The structure of flavin-dependent tryptophan 7-halogenase RebH. Proteins Struct. Funct. Genet. 70 (2008) 289–293.
[EC 1.14.19.9 created 2009 as EC 1.14.14.7, transferred 2014 to EC 1.14.19.9]
 
 


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