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.
| Identifer | oai:union.ndltd.org:bl.uk/oai:ethos.bl.uk:490456 |
| Date | January 2008 |
| Creators | Coles, Steven John |
| Publisher | University of the West of England, Bristol |
| Source Sets | Ethos UK |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
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