Journal Article

Characterization of SgcE6, the flavin reductase component supporting FAD-dependent halogenation and hydroxylation in the biosynthesis of the enediyne antitumor antibiotic C-1027

Steven G. Van Lanen, Shuangjun Lin, Geoff P. Horsman and Ben Shen

in FEMS Microbiology Letters

Volume 300, issue 2, pages 237-241
Published in print November 2009 |
Published online October 2009 | e-ISSN: 1574-6968 | DOI: https://dx.doi.org/10.1111/j.1574-6968.2009.01802.x

Show Summary Details

Preview

Abstract

The C-1027 enediyne antitumor antibiotic from Streptomyces globisporus possesses an (S)-3-chloro-5-hydroxy-β-tyrosine moiety, the chloro- and hydroxy-substituents of which are installed by a flavin-dependent halogenase SgcC3 and monooxygenase SgcC, respectively. Interestingly, a single flavin reductase, SgcE6, can provide reduced flavin to both enzymes. Bioinformatics analysis reveals that, similar to other flavin reductases involved in natural product biosynthesis, SgcE6 belongs to the HpaC-like subfamily of the Class I flavin reductases. The present study describes the steady-state kinetic characterization of SgcE6 as a strictly NADH- and FAD-specific enzyme.

Keywords: C-1027; enediyne; flavin reductase; halogenase; monooxygenase; SgcE6

Journal Article.  2125 words.  Illustrated.

Full text: subscription required

How to subscribe Recommend to my Librarian

Users without a subscription are not able to see the full content. Please, subscribe or login to access all content.