ArticleBiochemistry2011
Arsenate and phosphate as nucleophiles at the transition states of human purine nucleoside phosphorylase.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Vanadate as a new substrate for nucleoside phosphorylases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Article
- Allosteric Activation Shifts the Rate-Limiting Step in a Short-Form ATP Phosphoribosyltransferase.Biochemistry · 2018Article
- Inverse enzyme isotope effects in human purine nucleoside phosphorylase with heavy asparagine labels.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Catalytic-site design for inverse heavy-enzyme isotope effects in human purine nucleoside phosphorylase.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Are rice (Oryza sativa L.) phosphate transporters regulated similarly by phosphate and arsenate? A comprehensive study.Plant molecular biology · 2014Article
- Transition states of native and drug-resistant HIV-1 protease are the same.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Femtosecond dynamics coupled to chemical barrier crossing in a Born-Oppenheimer enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Article
- Transition-state analysis of Trypanosoma cruzi uridine phosphorylase-catalyzed arsenolysis of uridine.Journal of the American Chemical Society · 2011Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Purine nucleoside phosphorylase (PNP) catalyzes the reversible phosphorolysis of 6-oxypurine (2'-deoxy)ribonucleosides, generating (2-deoxy)ribose 1-phosphate and the purine base. Transition-state models for inosine cleavage have been proposed with bovine, human, and malarial PNPs using arsenate as the nucleophile, since kinetic isotope effects (KIEs) are obscured on phosphorolysis due to high commitment factors. The Phe200Gly mutant of human PNP has low forward and reverse commitment factors in the phosphorolytic reaction, permitting the measurement of competitive intrinsic KIEs on both arsenolysis and phosphorolysis of inosine. The intrinsic 1'-(14)C, 1'-(3)H, 2'-(2)H, 9-(15)N, and 5'-(3)H(2) KIEs for inosine were measured for arsenolysis and phosphorolysis. Except for the remote 5'-(3)H(2), and some slight difference between the 2'-(2)H KIEs, all isotope effects originating in the reaction coordinate are the same within experimental error. Hence, arsenolysis and phosphorolysis proceed through closely related transition states. Although electrostatically similar, the volume of arsenate is greater than phosphate and supports a steric influence to explain the differences in the 5'-(3)H(2) KIEs. Density functional theory calculations provide quantitative models of the transition states for Phe200Gly human PNP-catalyzed arsenolysis and phosphorolysis, selected upon matching calculated and experimental KIEs. The models confirm the striking resemblance between the transition states for the two reactions.
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Registered trials
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