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Biochemistry of Acyl CoA dependent proteins in plants: a targeted proteomics approach

ReferenceC17862
Principal Investigator / Supervisor Professor Antony Slabas
Co-Investigators /
Co-Supervisors
Professor Robert Edwards
Institution Durham University
DepartmentBiological and Biomedical Sciences
Funding typeResearch
Value (£) 156,792
StatusCompleted
TypeResearch Grant
Start date 06/05/2003
End date 06/05/2006
Duration36 months

Abstract

Acyl CoA dependent enzymes serve essential roles in cellular metabolism, however, many of the enzymes remain to be identified and isolated. We aim to combine expertise in chemistry and enzymology to build a generic technology, using photoaffinity labelling and proteomic analysis, aimed at identification of acyl CoA dependent enzymes and their substrate binding sites. We will use this to: (1) identify the acyl binding site of soluble glycerol-3-phospate acyltransferase (G3PAT), (2) identify and clone the plant membrane bound G3PAT and the anthocyanin 6-aromatic acyltransferaese, and (3) isolate binding site peptides of acyl CoA-utilising enzymes using new affinity tags and investigate their application to complex mixtures of proteins. (Joint with grant 18065)

Summary

unavailable
Committee Closed Committee - Biochemistry & Cell Biology (BCB)
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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