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The effects of protein glycosylation on enzyme kinetics

Reference	B15285
Principal Investigator / Supervisor	Professor Rudolf Allemann
Co-Investigators / Co-Supervisors	Professor Sabine Flitsch
Institution	University of Birmingham
Department	School of Chemistry
Funding type	Research
Value (£)	371,028
Status	Completed
Type	Research Grant
Start date	01/10/2001
End date	01/10/2004
Duration	36 months

Abstract

The origin of the exquisite rate acceleration observed in enzyme catalysed reactions is not yet fully understood. In addition to contributions to the rate enhancement from transition state stabilisation/reactant destabilisation and enzyme conformational changes, contributions from enzyme dynamics can be significant. If atomic motions in a protein are essential for catalysis, then glycosylation should directly influence reaction rates. To study the effects of protein glycosylation, sugar chains will be attached in specific positions on the surface of the enzyme dihydrofolate reductase and the reaction kinetics studied as a function of the position and the nature of glycosylation. These studies will broaden our understanding of the relationship between structure and function of enzymes and together with the advances in protein design might eventually allow us to design artificial catalysts with tailor-made activities.

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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