Original Research Paper

Biotechnology Letters

, Volume 33, Issue 8, pp 1607-1613

First online:

Characterization of a tryptophan 6-halogenase from Streptomyces toxytricini

  • Jia ZengAffiliated withDepartment of Biological Engineering, Utah State University
  • , Jixun ZhanAffiliated withDepartment of Biological Engineering, Utah State University Email author 

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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 k cat /K M 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