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Molecular mechanisms of amino acid recognition by A-domains of the Streptomyces coelicolor A3(2) coelichelin NRPS

ReferenceB16610
Principal Investigator / Supervisor Professor Gregory Challis
Co-Investigators /
Co-Supervisors
Institution University of Warwick
DepartmentChemistry
Funding typeResearch
Value (£) 182,084
StatusCompleted
TypeResearch Grant
Start date 01/08/2002
End date 31/07/2006
Duration48 months

Abstract

Non-ribosomal peptide synthetases (NRPSs) are a large family of modular multienzymes that catalyse the biosynthesis of many commercially important microbial natural products. Adenylation (A) domains within each NRPS module selectively bind and activate (by reaction with ATP) the amino acids constituting the peptide. Structure based models of A-domains have recently been developed, which identify potentially important residues from amino acid recognition and facilitate the prediction of new peptide natural product structures from genome sequence data. The accuracy of these structural predictions and the role played by putative recognition residues will be investigated using the Streptomyces coelicolor A3(2) coelichelin synthetase as a model.

Summary

unavailable
Committee Closed Committee - Biomolecular Sciences (BMS)
Research TopicsX – not assigned to a current Research Topic
Research PriorityX – Research Priority information not available
Research Initiative X - not in an Initiative
Funding SchemeX – not Funded via a specific Funding Scheme
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