ReviewThe Journal of biological chemistry2020
A global analysis of function and conservation of catalytic residues in enzymes.
Review in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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Who cites it
72 citing papers in PubMed, 149 citations in OpenAlex.
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- Trypsinogen Pro-Region as a Molecular Scaffold for the Design of Competitive Peptide Inhibitors of Trypsin-Like Proteases.Archives of insect biochemistry and physiology · 2026Article
- Toward understanding the catalytic mechanism for two classes of bacterial phospholipid N-methyltransferases.The FEBS journal · 2026Article
- Subcellular photochemistry for precision spatial protein targeting.Nature reviews. Chemistry · 2026Review
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- Methods for the establishment of enzymatic mechanisms - from QM to ML.Chemical science · 2026Review
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- Protein folds and catalytic strategies at the origin of biological CO2 fixation.FEMS microbiology ecology · 2026Article
- Structural and mechanistic insights into the divergence of pterin deaminase and sepiapterin deaminase.Applied microbiology and biotechnology · 2026Review
- Review
- Evolutionary Dynamics of Matrix Metalloproteases with Collagenolytic Activity in Teleosts.Animals : an open access journal from MDPI · 2025Article
- Understanding Biases in Liquid-Liquid Phase Separation: Investigating Amino Acid Enrichments in Phase-Separating Proteins toward Peptide Design.Biomacromolecules · 2025Article
- Reduced Amino Acid Substitution Matrices Find Traces of Ancient Coding Alphabets in Modern Day Proteins.Molecular biology and evolution · 2025Article
- Sequence and taxonomic feature evaluation facilitated the discovery of alcohol oxidases.Synthetic and systems biotechnology · 2025Article
- Measuring catalytic mechanism similarity - a new approach to study enzyme function and evolution.The FEBS journal · 2025Article
- Fermi calculations enable quick downselection of target genes and process optimization in photosynthetic systems.Plant physiology · 2025Review
- Advances in sulfonyl exchange chemical biology: expanding druggable target space.Chemical science · 2025Review
- Purine Chemistry in the Early RNA World at the Origins of Life: From RNA and Nucleobases Lesions to Current Key Metabolic Routes.Chembiochem : a European journal of chemical biology · 2025Review
- Unraveling the trisubstrate-triproduct reaction mechanisms of wine grape VvCYP76F14 to improve wine bouquet.Food chemistry · 2025Article
12 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The catalytic residues of an enzyme comprise the amino acids located in the active center responsible for accelerating the enzyme-catalyzed reaction. These residues lower the activation energy of reactions by performing several catalytic functions. Decades of enzymology research has established general themes regarding the roles of specific residues in these catalytic reactions, but it has been more difficult to explore these roles in a more systematic way. Here, we review the data on the catalytic residues of 648 enzymes, as annotated in the Mechanism and Catalytic Site Atlas (M-CSA), and compare our results with those in previous studies. We structured this analysis around three key properties of the catalytic residues: amino acid type, catalytic function, and sequence conservation in homologous proteins. As expected, we observed that catalysis is mostly accomplished by a small set of residues performing a limited number of catalytic functions. Catalytic residues are typically highly conserved, but to a smaller degree in homologues that perform different reactions or are nonenzymes (pseudoenzymes). Cross-analysis yielded further insights revealing which residues perform particular functions and how often. We obtained more detailed specificity rules for certain functions by identifying the chemical group upon which the residue acts. Finally, we show the mutation tolerance of the catalytic residues based on their roles. The characterization of the catalytic residues, their functions, and conservation, as presented here, is key to understanding the impact of mutations in evolution, disease, and enzyme design. The tools developed for this analysis are available at the M-CSA website and allow for user specific analysis of the same data.
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