Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.490456
Title: Redox regulation through S-thiolation and S-nitrosylation of the BCAT proteins with insights in to the role these systems play in neuronal cells
Author: Coles, Steven John
Awarding Body: University of West of England, Bristol
Current Institution: University of the West of England, Bristol
Date of Award: 2008
Availability of Full Text:
Access through EThOS:
Abstract:
The human mitochondrial and cytosolic branched chain aminotransferases (hBCATm and hBCATc, respectively) are key metabolic enzymes that catalyse the reversible transamination of the nutritionally essential branched-chain amino acids. Both isozymes have a conserved redox active CXXC motif, unique among the mammalian aminotransferases. In the present study the effect of ^S-nitrosylation, iS-thiolation or disulphide bond formation on the functionality of the BCAT proteins was investigated.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.490456  DOI: Not available
Share: