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Org Lett. 2013 Jul 19;15(14):3774-7. doi: 10.1021/ol401723h. Epub 2013 Jul 9.

Expanding the structural diversity of polyketides by exploring the cofactor tolerance of an inline methyltransferase domain.

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1
Department of Chemical and Biomolecular Engineering, University of California, Los Angeles, California 90095, USA.

Abstract

A strategy for introducing structural diversity into polyketides by exploiting the promiscuity of an in-line methyltransferase domain in a multidomain polyketide synthase is reported. In vitro investigations using the highly-reducing fungal polyketide synthase CazF revealed that its methyltransferase domain accepts the nonnatural cofactor propargylic Se-adenosyl-l-methionine and can transfer the propargyl moiety onto its growing polyketide chain. This propargylated polyketide product can then be further chain-extended and cyclized to form propargyl-α pyrone or be processed fully into the alkyne-containing 4'-propargyl-chaetoviridin A.

PMID:
23837609
PMCID:
PMC3779521
DOI:
10.1021/ol401723h
[Indexed for MEDLINE]
Free PMC Article
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