Refining and expanding nonribosomal peptide synthetase function and mechanism

Matt McErlean; Jonathan Overbay; Steven Van Lanen

doi:10.1007/s10295-018-02130-w

Refining and expanding nonribosomal peptide synthetase function and mechanism

Matt McErlean, Jonathan Overbay, Steven Van Lanen

Research output: Contribution to journal › Review article › peer-review

34 Scopus citations

Abstract

Nonribosomal peptide synthetases (NRPSs) are involved in the biosynthesis of numerous peptide and peptide-like natural products that have been exploited in medicine, agriculture, and biotechnology, among other fields. As a consequence, there have been considerable efforts aimed at understanding how NRPSs orchestrate the assembly of these natural products. This review highlights several recent examples that continue to expand upon the fundamental knowledge of NRPS mechanism and includes (1) the discovery of new NRPS substrates and the mechanism by which these sometimes structurally complex substrates are made, (2) the characterization of new NRPS activities and domains that function during the process of peptide assembly, and (3) the various catalytic strategies that are utilized to release the NRPS product. These findings continue to strengthen the predictive power for connecting genes to products, thereby facilitating natural product discovery and development in the Genomics Era.

Original language	English
Pages (from-to)	493-513
Number of pages	21
Journal	Journal of Industrial Microbiology and Biotechnology
Volume	46
Issue number	3-4
DOIs	https://doi.org/10.1007/s10295-018-02130-w
State	Published - Mar 29 2019

Bibliographical note

Funding Information:
Pharmaceutical Sciences, University of Kentucky). Natural product-inspired research in the Van Lanen laboratory is supported in part by National Institutes of Health Grants AI128862, AI087849, and CA217255.

Funding Information:
We appreciate the in depth discussions with Dr. Sylvie Garneau-Tsodikova and Taylor Lundy (Department of Pharmaceutical Sciences, University of Kentucky). Natural product-inspired research in the Van Lanen laboratory is supported in part by National Institutes of Health Grants AI128862, AI087849, and CA217255.

Publisher Copyright:
© 2019, Society for Industrial Microbiology and Biotechnology.

Keywords

Bioinformatics
Discovery
Domain
Mechanism
NRPS
Natural products

ASJC Scopus subject areas

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology

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10.1007/s10295-018-02130-w

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abstract = "Nonribosomal peptide synthetases (NRPSs) are involved in the biosynthesis of numerous peptide and peptide-like natural products that have been exploited in medicine, agriculture, and biotechnology, among other fields. As a consequence, there have been considerable efforts aimed at understanding how NRPSs orchestrate the assembly of these natural products. This review highlights several recent examples that continue to expand upon the fundamental knowledge of NRPS mechanism and includes (1) the discovery of new NRPS substrates and the mechanism by which these sometimes structurally complex substrates are made, (2) the characterization of new NRPS activities and domains that function during the process of peptide assembly, and (3) the various catalytic strategies that are utilized to release the NRPS product. These findings continue to strengthen the predictive power for connecting genes to products, thereby facilitating natural product discovery and development in the Genomics Era.",

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Refining and expanding nonribosomal peptide synthetase function and mechanism

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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