Structural highlights
Function
PNPH_BOVIN The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
In an effort to develop potent multisubstrate-analog inhibitors of purine nucleoside phosphorylase (PNP), three nucleoside phosphonates were designed utilizing structural information from the previously reported structures of complexes of bovine PNP with substrates and products. The nucleoside phosphonates contain an acetal linkage at the O2' and O3' positions and a two-C-atom spacer between the ribose and phosphate moieties. The linkage enables the compounds to simultaneously occupy the purine-, ribose- and phosphate-binding sites. The chemical syntheses, inhibition profiles and structural characterization of these novel multisubstrate analog inhibitors with bovine PNP are described.
Novel multisubstrate inhibitors of mammalian purine nucleoside phosphorylase.,Toms AV, Wang W, Li Y, Ganem B, Ealick SE Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1449-58. Epub 2005, Oct 19. PMID:16239721[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Toms AV, Wang W, Li Y, Ganem B, Ealick SE. Novel multisubstrate inhibitors of mammalian purine nucleoside phosphorylase. Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1449-58. Epub 2005, Oct 19. PMID:16239721 doi:http://dx.doi.org/10.1107/S0907444905025503
