The Library
Substrate recognition by nonribosomal peptide synthetase multi-enzymes
Tools
UNSPECIFIED (2004) Substrate recognition by nonribosomal peptide synthetase multi-enzymes. MICROBIOLOGY-SGM, 150 (Part 6). pp. 1629-1636.
Research output not available from this repository.
Request-a-Copy directly from author or use local Library Get it For Me service.
Abstract
Nonribosomal peptide synthetases (NRPSs) are giant multi-domain enzymes that catalyse the biosynthesis of many commercially important peptides produced by bacteria and fungi. Several studies over the last decade have shown that many of the individual domains within NRPSs exhibit significant substrate selectivity, which impacts on our ability to engineer NRPSs to produce new bioactive microbial peptides. Adenylation domains appear to be the primary determinants of substrate selectivity in NRPSs. Much progress has been made towards an empirical understanding of substrate selection by these domains over the last 5 years, but the molecular basis of substrate selectivity in these domains is not yet well understood. Perhaps surprisingly, condensation domains have also been reported to exhibit moderate to high substrate selectivity, although the generality of this observation and its potential impact on engineered biosynthesis experiments has yet to be fully elucidated. The situation is less clear for the thioesterase domains, which seem in certain cases to be dedicated to the hydrolysis/cyclization of their natural substrate, whereas in other cases they are largely permissive.
Item Type: | Journal Item | ||||
---|---|---|---|---|---|
Subjects: | Q Science > QR Microbiology | ||||
Journal or Publication Title: | MICROBIOLOGY-SGM | ||||
Publisher: | SOC GENERAL MICROBIOLOGY | ||||
ISSN: | 1350-0872 | ||||
Official Date: | June 2004 | ||||
Dates: |
|
||||
Volume: | 150 | ||||
Number: | Part 6 | ||||
Number of Pages: | 8 | ||||
Page Range: | pp. 1629-1636 | ||||
Publication Status: | Published |
Data sourced from Thomson Reuters' Web of Knowledge
Request changes or add full text files to a record
Repository staff actions (login required)
View Item |