Expanding the Chemical Space of Nonribosomal Peptide Synthetase-like Enzymes by Domain and Tailoring Enzyme Recombination

Johannes W A van Dijk; Clay C C Wang

doi:10.1021/acs.orglett.8b01581

Expanding the Chemical Space of Nonribosomal Peptide Synthetase-like Enzymes by Domain and Tailoring Enzyme Recombination

Org Lett. 2018 Sep 7;20(17):5082-5085. doi: 10.1021/acs.orglett.8b01581. Epub 2018 Aug 14.

Authors

Johannes W A van Dijk¹, Clay C C Wang^{1

2}

Affiliations

¹ Department of Pharmacology and Pharmaceutical Sciences , University of Southern California, School of Pharmacy , Los Angeles , California 90089 , United States.
² Department of Chemistry, College of Letters, Arts, and Sciences , University of Southern California , Los Angeles , California 90089 , United States.

PMID: 30106305
DOI: 10.1021/acs.orglett.8b01581

Abstract

The potential of tailoring enzymes in combination with engineered hybrid nonribosomal peptide synthetase-like enzymes was explored and resulted in methylated and prenylated forms of novel natural products, highlighting the possibilities and limitations of this approach.

Publication types

Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Aspergillus / enzymology
Peptide Synthases / chemistry*
Peptide Synthases / genetics
Peptide Synthases / metabolism*
Protein Domains
Protein Engineering*

Substances

Peptide Synthases
non-ribosomal peptide synthase

Grants and funding

P01 GM084077/GM/NIGMS NIH HHS/United States