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Domain organisation and catalytic efficiency in the mammalian pyruvate and 2-oxoglutarate multienzyme complexes

Reference	B10192
Principal Investigator / Supervisor	Professor John Lindsay
Co-Investigators / Co-Supervisors	Professor Richard Cogdell
Institution	University of Glasgow
Department	IBLS Division of Biochemistry & Molecula
Funding type	Research
Value (£)	171,239
Status	Completed
Type	Research Grant
Start date	01/04/1999
End date	15/11/2002
Duration	44 months

Abstract

Specific aims are as follows: a) to insert the high-affinity E3 binding domain of protein X at various sites in the E2 core enzyme of PDC: 1) to permit reconstitution of a modified PDC lacking its protein X subunit and 2) to assess the efficiencies of these mutant E2 cores in restoration of complex activity; b) to measure the stoichiometry and affinity of the E1 and E3 components for the E2 and protein X-derived peripheral subunit binding domains; c) to map critical regions in the N-terminal region of E1- OGDC involved in maintaining key subunit interactions and d) to initiate pilot crystallisation trials with the overexpressed subunit binding domains of E2 and protein X and the native E2/X and E1/E2 cores of PDC and OGDC.

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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