We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Reversible Product Release and Recapture by a Fungal Polyketide Synthase Using a Carnitine Acyltransferase Domain.
- Authors
Hang, Leibniz; Tang, Man ‐ Cheng; Harvey, Colin J. B.; Page, Claire G.; Li, Jian; Hung, Yiu ‐ Sun; Liu, Nicholas; Hillenmeyer, Maureen E.; Tang, Yi
- Abstract
Fungal polyketides have significant biological activities, yet the biosynthesis by highly reducing polyketide synthases (HRPKSs) remains enigmatic. An uncharacterized group of HRPKSs was found to contain a C-terminal domain with significant homology to carnitine O-acyltransferase (cAT). Characterization of one such HRPKS (Tv6-931) from Trichoderma virens showed that the cAT domain is capable of esterifying the polyketide product with polyalcohol nucleophiles. This process is readily reversible, as confirmed through the holo ACP-dependent transesterification of the released product. The methyltransferase (MT) domain of Tv6-931 can perform two consecutive α-methylation steps on the last β-keto intermediate to yield an α,α-gem-dimethyl product, a new programing feature among HRPKSs. Recapturing of the released product by cAT domain is suggested to facilitate complete gem-dimethylation by the MT.
- Subjects
POLYKETIDE synthases; CARNITINE acyltransferases; POLYKETIDES; BIOSYNTHESIS; CHEMICAL reactions
- Publication
Angewandte Chemie, 2017, Vol 129, Issue 32, p9684
- ISSN
0044-8249
- Publication type
Article
- DOI
10.1002/ange.201705237