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Characterization of the Ketosynthase and Acyl Carrier Protein Domains at the LnmI Nonribosomal Peptide Synthetase-Polyketide Synthase Interface for Leinamycin Biosynthesis.
- Source :
-
Organic Letters . Sep2016, Vol. 18 Issue 17, p4288-4291. 4p. - Publication Year :
- 2016
-
Abstract
- Leinamycin (LNM) is biosynthesized by a hybrid nonribosomal peptide synthetase (NRPS)-acyltransferase (AT)-less type I polyketide synthase (PKS). Characterization of LnmI revealed ketosynthase (KS)-acyl carrier protein (ACP)-KS domains at the NRPS-PKS interface. Inactivation of the KS domain or ACP domain in vivo abolished LNM production, and the ACP domain can be phosphopantetheinylated in vitro. The LnmI KS-ACP-KS architecture represents a new mechanism for functional crosstalk between NRPS and AT-less type I PKS in the biosynthesis of hybrid peptide-polyketide natural products. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 15237060
- Volume :
- 18
- Issue :
- 17
- Database :
- Academic Search Index
- Journal :
- Organic Letters
- Publication Type :
- Academic Journal
- Accession number :
- 117975842
- Full Text :
- https://doi.org/10.1021/acs.orglett.6b02033