Broad substrate specificity of the loading didomain of the lipomycin polyketide synthase.
Satoshi Yuzawa, Clara H Eng, Leonard Katz, Jay D Keasling
QB3 Institute, University of California, Berkeley, California 94270, United States.
Biochemistry 2013 Jun 4LipPks1, a polyketide synthase subunit of the lipomycin synthase, is believed to catalyze the polyketide chain initiation reaction using isobutyryl-CoA as a substrate, followed by an elongation reaction with methylmalonyl-CoA to start the biosynthesis of antibiotic α-lipomycin in Streptomyces aureofaciens Tü117. Recombinant LipPks1, containing the thioesterase domain from the 6-deoxyerythronolide B synthase, was produced in Escherichia coli, and its substrate specificity was investigated in vitro. Surprisingly, several different acyl-CoAs, including isobutyryl-CoA, were accepted as the starter substrates, while no product was observed with acetyl-CoA. These results demonstrate the broad substrate specificity of LipPks1 and may be applied to producing new antibiotics.
Citation
Satoshi Yuzawa, Clara H Eng, Leonard Katz, Jay D Keasling. Broad substrate specificity of the loading didomain of the lipomycin polyketide synthase. Biochemistry. 2013 Jun 4;52(22):3791-3
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PMID: 23692164
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