ArticleProceedings of the National Academy of Sciences of the United States of America2009
Determining the catalytic role of remote substrate binding interactions in ketosteroid isomerase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
36 citing papers in PubMed, 61 citations in OpenAlex.
- Towards next generation enzyme mimics through local electric field control in organic cage catalysts.Chemical science · 2026Article
- Emergence of specific binding and catalysis from a designed generalist binding protein.Nature chemistry · 2026Article
- Binding memory of liquid molecules.Nature communications · 2025Article
- Ensemble-function relationships to dissect mechanisms of enzyme catalysis.Science advances · 2022Article
- Distal Ionic Substrate-Catalyst Interactions Enable Long-Range Stereocontrol: Access to Remote Quaternary Stereocenters through a Desymmetrizing Suzuki-Miyaura Reaction.Journal of the American Chemical Society · 2022Article
- Assessment of enzyme active site positioning and tests of catalytic mechanisms through X-ray-derived conformational ensembles.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- BIMP-Catalyzed 1,3-Prototropic Shift for the Highly Enantioselective Synthesis of Conjugated Cyclohexenones.Angewandte Chemie (International ed. in English) · 2020Article
- Enzyme-Substrate-Cofactor Dynamical Networks Revealed by High-Resolution Field Cycling Relaxometry.Biochemistry · 2020Article
- Protein Flexibility and Stiffness Enable Efficient Enzymatic Catalysis.Journal of the American Chemical Society · 2019Article
- Dynamic Characteristics of Guanosine-5'-monophosphate Reductase Complexes Revealed by High-ResolutionBiochemistry · 2018Article
- Engineering the "Missing Link" in Biosynthetic (-)-Menthol Production: Bacterial Isopulegone Isomerase.ACS catalysis · 2018Article
- Electric Fields and Fast Protein Dynamics in Enzymes.The journal of physical chemistry letters · 2017Article
- Ability of T1 Lipase to Degrade Amorphous P(3HB): Structural and Functional Study.Molecular biotechnology · 2017Article
- Electric Fields and Enzyme Catalysis.Annual review of biochemistry · 2017Review
- A Critical Test of the Electrostatic Contribution to Catalysis with Noncanonical Amino Acids in Ketosteroid Isomerase.Journal of the American Chemical Society · 2016Article
- Dissecting Proton Delocalization in an Enzyme's Hydrogen Bond Network with Unnatural Amino Acids.Biochemistry · 2015Article
- Single-molecule spectroscopy reveals how calmodulin activates NO synthase by controlling its conformational fluctuation dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Prediction of distal residue participation in enzyme catalysis.Protein science : a publication of the Protein Society · 2015Article
- Computer aided enzyme design and catalytic concepts.Current opinion in chemical biology · 2014Review
- Enzyme architecture: on the importance of being in a protein cage.Current opinion in chemical biology · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
A fundamental difference between enzymes and small chemical catalysts is the ability of enzymes to use binding interactions with nonreactive portions of substrates to accelerate chemical reactions. Remote binding interactions can localize substrates to the active site, position substrates relative to enzymatic functional groups and other substrates, trigger conformational changes, induce local destabilization, and modulate an active site environment by solvent exclusion. We investigated the role of remote substrate binding interactions in the reaction catalyzed by the enzyme ketosteroid isomerase (KSI), which catalyzes a double bond migration of steroid substrates through a dienolate intermediate that is stabilized in an oxyanion hole. Comparison of a single-ring and multiple-ring substrate allowed the catalytic contribution of binding interactions with the distal substrate rings to be determined. The value of k(cat)/K(M) for a single-ring substrate is reduced 27,000-fold relative to a multiple-ring steroid substrate, suggesting that remote binding interactions with the steroid substrate contribute substantially to the KSI reaction. Nevertheless, the reaction rates for KSI-bound single- and multiple-ring substrates (k(cat)) are within 2-fold. Further, oxyanion hole mutations have the same effect on reactions of the single- and multiple-ring substrates. These results suggest that remote binding interactions contribute >5 kcal/mol to catalysis by KSI but that local rather than remote interactions dictate the catalytic contributions from KSI's general base and oxyanion hole.
Indexed as
Identifiers
What OpenQuestion holds
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.