Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.495651
Title: Structural studies of the human glyoxylate reductase/hydroxypyruvate reductase (GRHPR) and other proteins
Author: Booth, Michael P. S.
Awarding Body: UNIVERSITY OF BRISTOL
Current Institution: University of Bristol
Date of Award: 2008
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Abstract:
Human glyoxylate reductase/hydroxypyruvate reductase (GRHPR) is a D-2-hydroxyacid dehydrogenase found predominantly within the liver, and is essential for the removal of the reactive metabolic product glyoxylate. Primary hyperoxaluria type 2 (PH2) disease, which is characterised by increased urinary oxalate and L-glycerate levels leading to calcium oxalate deposition and decreased renal function, is caused by mutations in the gene for GRHPR. In this study the first crystal structures of the human GRHPR enzyme are reported. Structures of apo, binary and ternary forms of GRHPR are reported, the latter being the first structure of a true ternary complex of an enzyme from the D-2-hydroxyacid dehydrogenase family.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.495651  DOI: Not available
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