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Enzyme thermostability and thermoactivity subunit interactions catalytic mechanisms and conformation changes at extreme temperature

Reference	B10059
Principal Investigator / Supervisor	Professor Michael Danson
Co-Investigators / Co-Supervisors	Dr David Hough, Professor Garry Taylor
Institution	University of Bath
Department	Biology and Biochemistry
Funding type	Research
Value (£)	154,143
Status	Completed
Type	Research Grant
Start date	16/02/1999
End date	16/08/2002
Duration	42 months

Abstract

At Bath we have cloned, sequenced and expressed the genes encoding citrate synthase from Pyrococcus furiosus (100 degrees centigrade), Sulfolobus solfataricus (80 degrees centigrade), Thermoplasma acidophilum (55 degrees centigrade) and a psychrophilic bacterium (10 degrees centigrade), and have determined the crystal structures of all the recombinant enzymes [the pig (37 degrees centigrade) enzyme structure was already available]. From comparative analyses, we have identified features that may be involved in hyperstability and cold-activity, and have preliminary evidence that the subunit interactions may be crucial to maintaining polypeptide integrity. This homologous series of enzymes, spanning the biological range over which life exists, puts us in a unique position to ask: 1) What is the role of inter- subunit interactions in determining the stability of oligomeric, hyperthermostable enzymes? 2) What are the quantitative contributions of the features identified to the overall thermostability of the enzyme? 3) How do enzymes from hyperthermophiles catalyse their reactions at temperatures approaching 100 degrees centigrade? 4) How do psychophilic enzymes maintain their high catalytic rates at low temperatures?

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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