Journal
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
Volume 18, Issue 22, Pages 5900-5903Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmcl.2008.08.047
Keywords
PNP; Immucillin; ImmH; Mutant; Binding; Transition-state analogue
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Funding
- NIGMS NIH HHS [R37 GM041916-19, R37 GM041916] Funding Source: Medline
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Neighboring-group participation in the reaction catalyzed by purine nucleoside phosphorylase involves a compression mode between the 5'- and 4'-ribosyl oxygens, facilitated by His257. The His257Gly mutant opens a space in the catalytic site. Hydrophobic 5'-substituted Immucillins are transition-state analogue inhibitors of this mutant enzyme. Dissociation constants as low as 2 pM are achieved, with K-m/K-d as high as 400,000,000. (C) 2008 Elsevier Ltd. All rights reserved.
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