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

Research output: Contribution to journalArticlepeer-review

20 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 languageEnglish (US)
Pages (from-to)842-844
Number of pages3
JournalJournal of the American Chemical Society
Volume130
Issue number3
DOIs
StatePublished - Jan 23 2008

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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