The Gene Cluster for Fluorometabolite Biosynthesis in Streptomyces cattleya: A Thioesterase Confers Resistance to Fluoroacetyl-Coenzyme A

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2006
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Huang, Fanglu
Stephen F., Haydock,
Mironenko, Tatiana
Li, Tsung-Lin
O'Hagan, David
Leadlay, Peter F.
Spencer, Jonathan B.
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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 FlA 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. FlB 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 FlI 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.

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570 Biowissenschaften, Biologie
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MICROBIO, CHEMBIO
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ISO 690HUANG, Fanglu, Haydock STEPHEN F., Dieter SPITELLER, Tatiana MIRONENKO, Tsung-Lin LI, David O'HAGAN, Peter F. LEADLAY, Jonathan B. SPENCER, 2006. The Gene Cluster for Fluorometabolite Biosynthesis in Streptomyces cattleya: A Thioesterase Confers Resistance to Fluoroacetyl-Coenzyme A. In: Chemistry & Biology. 2006, 13(5), pp. 475-484. ISSN 1074-5521. Available under: doi: 10.1016/j.chembiol.2006.02.014
BibTex
@article{Huang2006-05Clust-15500,
  year={2006},
  doi={10.1016/j.chembiol.2006.02.014},
  title={The Gene Cluster for Fluorometabolite Biosynthesis in Streptomyces cattleya: A Thioesterase Confers Resistance to Fluoroacetyl-Coenzyme A},
  number={5},
  volume={13},
  issn={1074-5521},
  journal={Chemistry & Biology},
  pages={475--484},
  author={Huang, Fanglu and Stephen F., Haydock, and Spiteller, Dieter and Mironenko, Tatiana and Li, Tsung-Lin and O'Hagan, David and Leadlay, Peter F. and Spencer, Jonathan B.}
}
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    <dcterms:abstract xml:lang="eng">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 FlA 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. FlB 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 FlI 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.</dcterms:abstract>
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