ReviewBiochemistry2013
Fundamental challenges in mechanistic enzymology: progress toward understanding the rate enhancements of enzymes.
Review in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 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
37 citing papers in PubMed.
- Understanding how enzymes work: the journey to ensemble-function studies.The FEBS journal · 2026Review
- Bifunctional Catalysis of Aldol Reactions by Foldamer Dihydrazides: Assessment of Conformational Preorganization.Journal of the American Chemical Society · 2025Article
- Conformation-Dependent Hydrogen-Bonding Interactions in a Switchable Artificial Metalloprotein.Biochemistry · 2024Article
- Interplay of structural preorganization and conformational sampling in UDP-glucuronic acid 4-epimerase catalysis.Nature communications · 2024Article
- Substrate promiscuity of Dicer toward precursors of the let-7 family and their 3'-end modifications.Cellular and molecular life sciences : CMLS · 2024Article
- Reactivity Tracking of an Enzyme Progress Coordinate.The journal of physical chemistry letters · 2023Article
- Engineering a Conformationally Switchable Artificial Metalloprotein.Journal of the American Chemical Society · 2022Article
- The mechanisms of catalysis and ligand binding for the SARS-CoV-2 NSP3 macrodomain from neutron and x-ray diffraction at room temperature.Science advances · 2022Article
- Essential Functional Interplay of the Catalytic Groups in Acid Phosphatase.ACS catalysis · 2022Article
- The mechanisms of catalysis and ligand binding for the SARS-CoV-2 NSP3 macrodomain from neutron and X-ray diffraction at room temperature.bioRxiv : the preprint server for biology · 2022Article
- Resolution and characterization of confinement- and temperature-dependent dynamics in solvent phases that surround proteins in frozen aqueous solution by using spin-probe EPR spectroscopy.Methods in enzymology · 2022Article
- Resolution and characterization of contributions of select protein and coupled solvent configurational fluctuations to radical rearrangement catalysis in coenzyme BMethods in enzymology · 2022Article
- Revealing enzyme functional architecture via high-throughput microfluidic enzyme kinetics.Science (New York, N.Y.) · 2021Article
- 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
- A Preorganized Electric Field Leads to Minimal Geometrical Reorientation in the Catalytic Reaction of Ketosteroid Isomerase.Journal of the American Chemical Society · 2020Article
- Article
- Carbon Acidity in Enzyme Active Sites.Frontiers in bioengineering and biotechnology · 2019Article
- Promoting Vibrations and the Function of Enzymes. Emerging Theoretical and Experimental Convergence.Biochemistry · 2018Review
- Enzyme Architecture: The Role of a Flexible Loop in Activation of Glycerol-3-phosphate Dehydrogenase for Catalysis of Hydride Transfer.Biochemistry · 2018Article
- Shuffling Active Site Substate Populations Affects Catalytic Activity: The Case of Glucose Oxidase.ACS catalysis · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Enzymes are remarkable catalysts that lie at the heart of biology, accelerating chemical reactions to an astounding extent with extraordinary specificity. Enormous progress in understanding the chemical basis of enzymatic transformations and the basic mechanisms underlying rate enhancements over the past decades is apparent. Nevertheless, it has been difficult to achieve a quantitative understanding of how the underlying mechanisms account for the energetics of catalysis, because of the complexity of enzyme systems and the absence of underlying energetic additivity. We review case studies from our own work that illustrate the power of precisely defined and clearly articulated questions when dealing with such complex and multifaceted systems, and we also use this approach to evaluate our current ability to design enzymes. We close by highlighting a series of questions that help frame some of what remains to be understood, and we encourage the reader to define additional questions and directions that will deepen and broaden our understanding of enzymes and their catalysis.
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.