Use this URL to cite or link to this record in EThOS: https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.750313
Title: Protein-carbohydrate recognition
Author: McMahon, Stephen Andrew
Awarding Body: University of St Andrews
Current Institution: University of St Andrews
Date of Award: 1999
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Abstract:
Protein-carbohydrate recognition is an important target for inhibitor development. Improved inhibitor design requires a fundamental molecular basis of these interactions. This thesis describes the preliminary structural studies on three carbohydrate processing enzymes, UDP-galactopyranose mutase, alpha-D-glucose-1-phosphate thymidylyltransferase and TDP-glucose 4,6-dehydratase. These enzymes are found in important human pathogens such as Mycobacterium tuberculosis and Salmonella typhimurium. The major focus of the thesis has been on UDP-galactopyranose mutase, the enzyme responsible for catalysing synthesis of the thermodynamically unfavourable 5 membered ring form of galactose, UDP-galactofuranose from the thermodynamically favoured 6 membered ring form, UDP-galactopyranose. UDP-galactofuranose plays a key role in mycobacterial cell walls. This thesis also describes work with concanavalin A. This legume lectin is an invaluable model for the study of protein-carbohydrate interactions. Two concanavalin A complexes are discussed. Both structures clear up misunderstandings in the literature and provide an insight into designing enzyme inhibitors.
Supervisor: Naismith, James H. Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.750313  DOI: Not available
Keywords: QR77.3M7 ; Bacterial cell walls
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