Award details

Structural and biochemical studies on pantothenate biosynthesis enzymes

Reference	B09676
Principal Investigator / Supervisor	Professor Alison Smith
Co-Investigators / Co-Supervisors	Professor Chris Abell, Professor Sir Tom Blundell
Institution	University of Cambridge
Department	Plant Sciences
Funding type	Research
Value (£)	161,086
Status	Completed
Type	Research Grant
Start date	01/10/1998
End date	01/10/2001
Duration	36 months

Abstract

The overall aim of our work is to develop a comprehensive biochemical and structural understanding of the four enzymes which constitute the biosynthetic pathway to pantothenate (vitamin B5). In this proposal we aim specifically to: (i) study the catalytic mechanism of E. coli L-aspartate-alpha decarboxylase (ADC), and the protein processing involved in forming the active site pyruvoyl group, using a combination of biochemical and crystallographic approaches. (ii) solve the crystal structures of KPHMT and pantothenate synthase. (iii) clone and overexpress ketopantoate reductase as a prelude to mechanistic and structural studies.

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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