ArticleBiochemistry2012
Constrained bonding environment in the Michaelis complex of Trypanosoma cruzi uridine phosphorylase.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 8 citations in OpenAlex.
- Probing the Human 4-Oxo-l-proline Reductase-Catalyzed Reaction by Deuterium Kinetic and Equilibrium Isotope Effects.Biochemistry · 2026Article
- Kinetic isotope effects reveal early transition state of protein lysine methyltransferase SET8.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Binding Isotope Effects for para-Aminobenzoic Acid with Dihydropteroate Synthase from Staphylococcus aureus and Plasmodium falciparum.ACS chemical biology · 2015Article
- Ground state destabilization by anionic nucleophiles contributes to the activity of phosphoryl transfer enzymes.PLoS biology · 2013Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The transition state for the Trypanosoma cruzi uridine phosphorylase (TcUP) reaction has an expanded S(N)2 character. We used binding isotope effects (BIE's) to probe uridine distortion in the complex with TcUP and sulfate to mimic the Michaelis complex. Inverse 1'-(3)H and 5'-(3)H BIE's indicate a constrained bonding environment of these groups in the complex. Quantum chemical modeling identified a uridine conformer whose calculated BIE's match the experimental values. This conformer differs in sugar pucker and uracil orientation from the unbound conformer and the transition-state structure. These results support ground-state stabilization in the Michaelis complex.
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