L-enantiomers of transition state analogue inhibitors bound to human purine nucleoside phosphorylase

Agnes Rinaldo-Matthis; Andrew S. Murkin; Udupi A. Ramagopal; Keith Clinch; Simon P.H. Mee; Gary B. Evans; Peter C. Tyler; Richard H. Furneaux; Steven C. Almo; Vern L. Schramm

doi:10.1021/ja710733g

L-enantiomers of transition state analogue inhibitors bound to human purine nucleoside phosphorylase

Agnes Rinaldo-Matthis, Andrew S. Murkin, Udupi A. Ramagopal, Keith Clinch, Simon P.H. Mee, Gary B. Evans, Peter C. Tyler, Richard H. Furneaux, Steven C. Almo, Vern L. Schramm

Biochemistry

Research output: Contribution to journal › Article › peer-review

22 Scopus citations

Abstract

Human purine nucleoside phosphorylase (PNP) was crystallized with transition-state analogue inhibitors Immucillin-H and DADMe-Immucillin-H synthesized with ribosyl mimics of l-stereochemistry. The inhibitors demonstrate that major driving forces for tight binding of these analogues are the leaving group interaction and the cationic mimicry of the transition state, even though large geometric changes occur with d-Immucillins and l-Immucillins bound to human PNP.

Original language	English (US)
Pages (from-to)	842-844
Number of pages	3
Journal	Journal of the American Chemical Society
Volume	130
Issue number	3
DOIs	https://doi.org/10.1021/ja710733g
State	Published - Jan 23 2008

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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abstract = "Human purine nucleoside phosphorylase (PNP) was crystallized with transition-state analogue inhibitors Immucillin-H and DADMe-Immucillin-H synthesized with ribosyl mimics of l-stereochemistry. The inhibitors demonstrate that major driving forces for tight binding of these analogues are the leaving group interaction and the cationic mimicry of the transition state, even though large geometric changes occur with d-Immucillins and l-Immucillins bound to human PNP.",

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AU - Rinaldo-Matthis, Agnes

AU - Murkin, Andrew S.

AU - Ramagopal, Udupi A.

AU - Clinch, Keith

AU - Mee, Simon P.H.

AU - Evans, Gary B.

AU - Tyler, Peter C.

AU - Furneaux, Richard H.

AU - Almo, Steven C.

AU - Schramm, Vern L.

PY - 2008/1/23

Y1 - 2008/1/23

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AB - Human purine nucleoside phosphorylase (PNP) was crystallized with transition-state analogue inhibitors Immucillin-H and DADMe-Immucillin-H synthesized with ribosyl mimics of l-stereochemistry. The inhibitors demonstrate that major driving forces for tight binding of these analogues are the leaving group interaction and the cationic mimicry of the transition state, even though large geometric changes occur with d-Immucillins and l-Immucillins bound to human PNP.

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L-enantiomers of transition state analogue inhibitors bound to human purine nucleoside phosphorylase

Abstract

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