Unusual Activities of the Thioesterase Domain for the Biosynthesis of the Polycyclic Tetramate Macrolactam HSAF in Lysobacter enzymogenes C3

Authors

Lili Lou, University of Nebraska-Lincoln
Haotong Chen, University of Nebraska-Lincoln
Ronald Cerny, University of Nebraska - LincolnFollow
Yaoyao Li, Shandong University
Yuemao Shen, Shandong University
Liangcheng Du, University of Nebraska-LincolnFollow

Date of this Version

2012

Citation

Biochemistry. 2012 January 10; 51(1): 4–6.

Comments

Copyright © 2011 American Chemical Society

Abstract

HSAF is an antifungal natural product with a new mode of action. A rare bacterial iterative PKSNRPS assembles the HSAF skeleton. The biochemical characterization of the NRPS revealed that the thioesterase (TE) domain possesses the activities of both a protease and a peptide ligase. Active site mutagenesis, circular dichroism spectra and homology modeling of the TE structure suggested that the TE may possess uncommon features that may lead to the unusual activities. The iterative PKS-NRPS is found in all polycyclic tetramate macrolactam gene clusters, and the unusual activities of the TE may be common to this type of hybrid PKS-NRPS.