ArticleProtein science : a publication of the Protein Society2022
Electrostatic fingerprints of catalytically active amino acids in enzymes.
Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Molecular Basis of pH-Dependent Activity in T7 RNA Polymerase Revealed by Constant pH Replica Exchange Molecular Dynamics.ACS physical chemistry Au · 2026Article
- Exploring the GM-CSF histidine triad as a modulator of structure, molecular motion, and ligand binding.RSC chemical biology · 2026Article
- MEDOC: A Fast, Scalable, and Mathematically Exact Algorithm for the Site-Specific Prediction of the Protonation Degree in Large Disordered Proteins.Journal of chemical information and modeling · 2025Article
- Article
- Biochemical Activity of 17 Cancer-Associated Variants of DNA Polymerase Kappa Predicted by Electrostatic Properties.Chemical research in toxicology · 2023Article
- Electrostatic fingerprints of catalytically active amino acids in enzymes.Protein science : a publication of the Protein Society · 2022Article
- Identification and characterization of alternative sites and molecular probes for SARS-CoV-2 target proteins.Frontiers in chemistry · 2022Article
Corrections and comments
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Authors and funding
5 authors.
Funding
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Abstract
The computed electrostatic and proton transfer properties are studied for 20 enzymes that represent all six major enzyme commission classes and a variety of different folds. The properties of aspartate, glutamate, and lysine residues that have been previously experimentally determined to be catalytically active are reported. The catalytic aspartate and glutamate residues studied here are strongly coupled to at least one other aspartate or glutamate residue and often to multiple other carboxylate residues with intrinsic pK
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