Characterization of the Ketosynthase and Acyl Carrier Protein Domains at the LnmI Nonribosomal Peptide Synthetase–Polyketide Synthase Interface for Leinamycin Biosynthesis | Zendy

Yong Huang | Zendy; Gong-Li Tang | Zendy; Guohui Pan | Zendy; ChinYuan Chang | Zendy; Ben Shen | Zendy

Open Access

Characterization of the Ketosynthase and Acyl Carrier Protein Domains at the LnmI Nonribosomal Peptide Synthetase–Polyketide Synthase Interface for Leinamycin Biosynthesis

Author(s) -

Yong Huang,

Gong-Li Tang,

Guohui Pan,

ChinYuan Chang,

Ben Shen

Publication year - 2016

Publication title -

organic letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.94

H-Index - 239

eISSN - 1523-7060

pISSN - 1523-7052

DOI - 10.1021/acs.orglett.6b02033

Subject(s) - nonribosomal peptide , polyketide synthase , acyl carrier protein , biosynthesis , polyketide , acyltransferase , chemistry , architecture domain , peptide , biochemistry , stereochemistry , enzyme , art , enterprise architecture management , architecture , visual arts , enterprise architecture

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.

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