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Evidence for a novel phosphopantetheinyl transferase domain in the polyketide synthase for enediyne biosynthesis
Author(s) -
Murugan Elavazhagan,
Liang Zhao-Xun
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.02.061
Subject(s) - polyketide synthase , polyketide , acyl carrier protein , enediyne , biosynthesis , biology , nonribosomal peptide , transferase , biochemistry , fatty acid synthase , stereochemistry , adenylylation , enzyme , chemistry
The polyketide synthase associated with the biosynthesis of enediyne‐containing calicheamicin contains a putative phosphopantetheinyl transferase (PPTase) domain. By cloning and expressing the C‐terminal region of the polyketide synthase and in vitro phosphopantetheinylation assay, we found that the PPTase domain exhibits preferred substrate specificity towards acyl and peptidyl carrier proteins in fatty acid and non‐ribosomal peptide synthesis over its cognate partner. We also found evidence suggesting that the PPTase domain adopts a pseudo‐trimeric structure, distinct from the pseudo‐dimeric structure of type II PPTases. The results revealed a novel type of PPTase with unique structure and substrate specificity, and suggested that the polyketide synthase probably acquired the PPTase domain from a primary metabolic pathway in evolution.