ArticleChemistry & biology2009
Ribocation transition state capture and rebound in human purine nucleoside phosphorylase.
Article in Chemistry & biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 14 citations in OpenAlex.
- Structural basis for substrate selectivity and nucleophilic substitution mechanisms in human adenine phosphoribosyltransferase catalyzed reaction.The Journal of biological chemistry · 2019Article
- Chemo-enzymatic synthesis of the exocyclic olefin isomer of thymidine monophosphate.Bioorganic & medicinal chemistry · 2018Article
- A conserved threonine prevents self-intoxication of enoyl-thioester reductases.Nature chemical biology · 2017Article
- Transition States and transition state analogue interactions with enzymes.Accounts of chemical research · 2015Article
- Catalytic site conformations in human PNP by 19F-NMR and crystallography.Chemistry & biology · 2013Article
- A complex of methylthioadenosine/S-adenosylhomocysteine nucleosidase, transition state analogue, and nucleophilic water identified by mass spectrometry.Journal of the American Chemical Society · 2012Article
- Structure of RiVax: a recombinant ricin vaccine.Acta crystallographica. Section D, Biological crystallography · 2011Article
- Arsenate and phosphate as nucleophiles at the transition states of human purine nucleoside phosphorylase.Biochemistry · 2011Article
- Enzymatic transition states, transition-state analogs, dynamics, thermodynamics, and lifetimes.Annual review of biochemistry · 2011Review
- Transition state analysis of thymidine hydrolysis by human thymidine phosphorylase.Journal of the American Chemical Society · 2010Article
- Transition States.The Journal of biological chemistry · 2009Article
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
Purine nucleoside phosphorylase (PNP) catalyzes the phosphorolysis of 6-oxy-purine nucleosides to the corresponding purine base and alpha-D-ribose 1-phosphate. Its genetic loss causes a lethal T cell deficiency. The highly reactive ribocation transition state of human PNP is protected from solvent by hydrophobic residues that sequester the catalytic site. The catalytic site was enlarged by replacing individual catalytic site amino acids with glycine. Reactivity of the ribocation transition state was tested for capture by water and other nucleophiles. In the absence of phosphate, inosine is hydrolyzed by native, Y88G, F159G, H257G, and F200G enzymes. Phosphorolysis but not hydrolysis is detected when phosphate is bound. An unprecedented N9-to-N3 isomerization of inosine is catalyzed by H257G and F200G in the presence of phosphate and by all PNPs in the absence of phosphate. These results establish a ribocation lifetime too short to permit capture by water. An enlarged catalytic site permits ribocation formation with relaxed geometric constraints, permitting nucleophilic rebound and N3-inosine isomerization.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.