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The gene cluster for fluorometabolite biosynthesis in Streptomyces cattleya: A thioesterase confers resistance to fluoroacetyl-coenzyme A

Author(s): F. L. Huang, S. F. Haydock, D. Spiteller, T. Mironenko, T. L. Li, D. O'Hagan, P. F. Leadlay, J. B. Spencer

A genomic library of Streptomyces cattleya was screened to isolate a gene cluster encoding enzymes responsible for the production of fluorine-containing metabolites. In addition to the previously described fluorinase FIA which catalyzes the formation of 5'-fluoro-5'-deoxyadenosine from S-adenosylmethionine and fluoride, 11 other putative open reading frames have been identified. Three of the proteins encoded by these genes have been characterized. FIB was determined to be the second enzyme in the pathway, catalyzing the phosphorolytic cleavage of 5'-fluoro-5'-deoxyadenosine to produce 5-fluoro-5-deoxy-D-ribose-1-phosphate. The enzyme Fill was found to be an S-adenosylhomocysteine hydrolase, which may act to relieve S-adenosylhomocysteine inhibition of the fluorinase. Finally, flK encodes a thioesterase which catalyzes the selective breakdown of fluoroacetyl-CoA but not acetyl-CoA, suggesting that it provides the producing strain with a mechanism for resistance to fluoroacetate.

Full version: Available here

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ISBN: 1074-5521
Publication Year: 2006
Periodical: Chemistry & Biology
Periodical Number: 5
Volume: 13
Pages: 475-484
Author Address: