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Biochemistry of Acyl CoA dependent proteins in plants: a targeted proteomics approach
Reference
C17862
Principal Investigator / Supervisor
Professor Antony Slabas
Co-Investigators /
Co-Supervisors
Professor Robert Edwards
Institution
Durham University
Department
Biological and Biomedical Sciences
Funding type
Research
Value (£)
156,792
Status
Completed
Type
Research Grant
Start date
06/05/2003
End date
06/05/2006
Duration
36 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 Topics
X – not assigned to a current Research Topic
Research Priority
X – Research Priority information not available
Research Initiative
X - not in an Initiative
Funding Scheme
X – not Funded via a specific Funding Scheme
Associated awards:
C18065 Biochemistry of plant AcylCoA binding proteins using a targeted proteomics approach
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