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Bioorg Med Chem Lett. 2007 Jun 1;17(11):3034-7. Epub 2007 Mar 23.

The thioesterase domain from the pimaricin and erythromycin biosynthetic pathways can catalyze hydrolysis of simple thioester substrates.

Author information

1
Department of Chemistry, Syracuse University, Syracuse, NY 13244-4100, USA.

Abstract

The recombinant polyketide synthase thioesterase domains from the pimaricin and 6-deoxyerythronolide B biosynthetic pathways catalyze hydrolysis of a number of simple N-acetylcysteamine thioester derivatives. This study demonstrates that thioesterases are not highly substrate selective in formation of the acyl-enzyme intermediate, in contrast to non-ribosomal peptide synthase thioesterase domains that show very high specificity for substrate loading. This observation has important implications for the engineering of biosynthetic pathways to produce polyketide products.

PMID:
17428661
DOI:
10.1016/j.bmcl.2007.03.060
[Indexed for MEDLINE]

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