In vivo characterization of nonribosomal peptide synthetases NocA and NocB in the biosynthesis of nocardicin A

17Citations
Citations of this article
34Readers
Mendeley users who have this article in their library.

Abstract

Two nonribosomal peptide synthetases (NRPS), NocA and NocB, together comprising five modules, are essential for the biosynthesis of the D,L,D configured tripeptide backbone of the monocyclic β-lactam nocardicin A. We report a double replacement gene strategy in which point mutations were engineered in the two encoding NRPS genes without disruption of the nocABC operon by placing selective markers in adjacent genes. A series of mutants was constructed to inactivate the thiolation (T) domain of each module and to evaluate an HHxxxDR catalytic motif in NocA and an atypical extended histidine motif in NocB. The loss of nocardicin A production in each of the T domain mutants indicates that all five modules are essential for its biosynthesis. Conversely, production of nocardicin A was not affected by mutation of the NocB histidine motif or the R828G mutation in NocA. © 2012 Elsevier Ltd. All rights reserved.

Cite

CITATION STYLE

APA

Davidsen, J. M., & Townsend, C. A. (2012). In vivo characterization of nonribosomal peptide synthetases NocA and NocB in the biosynthesis of nocardicin A. Chemistry and Biology, 19(2), 297–306. https://doi.org/10.1016/j.chembiol.2011.10.020

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free