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Protein-protein interaction substrate channelling and post-translational modification in multienzyme complexes
Reference
B09560
Principal Investigator / Supervisor
Professor Richard Perham
Co-Investigators /
Co-Supervisors
Institution
University of Cambridge
Department
Biochemistry
Funding type
Research
Value (£)
175,597
Status
Completed
Type
Research Grant
Start date
01/08/1998
End date
01/08/2001
Duration
36 months
Abstract
High-expression systems for the E1 components of 2-oxo acid dehydrogenase complexes will be perfected and the interaction of E1 with the lipoyl domains of the E2 components will be studied using directed mutagenesis, SPR and NMR spectroscopy. This interaction forms the molecular basis of substrate channelling and will be distinguished from subsequent catalytic events, notably reductive acylation of the pendant lipoyl group. Similar experiments will be carried out on post-translational modification of the E2 lipoyl domains and the structurally homologous biotinyl domain of acetylCoA carboxylase by their respective ligases. This will explain how target lysine residues are selected for attachment of the catalytically essential swinging arms.
Summary
unavailable
Committee
Closed Committee - Biomolecular Sciences (BMS)
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
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