Biotechnology Letters

, Volume 33, Issue 8, pp 1607–1613

Characterization of a tryptophan 6-halogenase from Streptomyces toxytricini

Original Research Paper

DOI: 10.1007/s10529-011-0595-7

Cite this article as:
Zeng, J. & Zhan, J. Biotechnol Lett (2011) 33: 1607. doi:10.1007/s10529-011-0595-7


Tryptophan (Trp) halogenases are found in various bacteria and play an important role in natural product biosynthesis. Analysis of the genome of Streptomyces toxytricini NRRL 15443 revealed an ORF, stth, encoding a putative Trp halogenase within a non-ribosomal peptide synthetase gene cluster. This gene was cloned into pET28a and functionally overexpressed in Escherichia coli. The enzyme halogenated both l- and d-Trp to yield the corresponding 6-chlorinated derivatives. The optimum activity was at 40°C and pH 6 giving kcat/KM value of STTH of 72,000 min−1 M−1. The enzyme also used bromide to yield 6-bromo-Trp.


Brominase Chlorinase Streptomyces toxytricini Tryptophan Tryptophan 6-halogenase 

Supplementary material

10529_2011_595_MOESM1_ESM.doc (347 kb)
Supplementary material 1 (DOC 347 kb)

Copyright information

© Springer Science+Business Media B.V. 2011

Authors and Affiliations

  1. 1.Department of Biological EngineeringUtah State UniversityLoganUSA

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