Abstract
Computational studies have been conducted to built a closed form of TPase and to characterize the transition state of the phosphorylisis reaction catalyzed by TPase. The results obtained point to a crucial role of His-85 and the O2 of thymine in the catalysis. This modelled transition state forms the basis for the design of new TPase inhibitors.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding Sites
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Catalysis
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Crystallography, X-Ray
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / pharmacology*
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Histidine
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Kinetics
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Protein Conformation
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Thymidine Phosphorylase / antagonists & inhibitors*
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Thymidine Phosphorylase / chemistry*
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Thymine
Substances
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Enzyme Inhibitors
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Histidine
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Thymidine Phosphorylase
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Thymine