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Characterization of SgcE6, the flavin reductase component supporting FAD-dependent halogenation and hydroxylation in the biosynthesis of the enediyne antitumor antibiotic C-1027.
- Source :
-
FEMS Microbiology Letters . Nov2009, Vol. 300 Issue 2, p237-241. 5p. 2 Diagrams, 3 Graphs. - Publication Year :
- 2009
-
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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 03781097
- Volume :
- 300
- Issue :
- 2
- Database :
- Academic Search Index
- Journal :
- FEMS Microbiology Letters
- Publication Type :
- Academic Journal
- Accession number :
- 44685181
- Full Text :
- https://doi.org/10.1111/j.1574-6968.2009.01802.x