ArticleBiophysical journal2005
Specificity of trypsin and chymotrypsin: loop-motion-controlled dynamic correlation as a determinant.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed.
- Evaluation of recombinant trypsinogen and chymotrypsinogen production in Komagataella phaffii through co-expression of HAC1 and PDI1.Microbial cell factories · 2026Article
- The FAM111A Gene: Genetic, Epigenetic, and Pharmacological Targets and Mechanistic Insights with Clinical Relevance.Pharmaceuticals (Basel, Switzerland) · 2026Article
- Structural and Catalytic Roles of the Disulfide Bonds Cys19-Cys154 and Cys134-Cys199 in Trypsin-like Proteases: Evolutionary Insights for Disulfide Bond Acquisition.Molecules (Basel, Switzerland) · 2026Article
- An in silico approach to peptide-based dual-receptor targeting for IL13RA2 and VEGFR-2 extracellular domain.Journal of molecular modeling · 2026Article
- Advances in Microbial Alkaline Proteases: Addressing Industrial Bottlenecks Through Genetic and Enzyme Engineering.Applied biochemistry and biotechnology · 2025Review
- Enzyme-Based Anti-Inflammatory Therapeutics for Inflammatory Diseases.Pharmaceutics · 2025Review
- Biochemical and physiological characterization of Aedes aegypti midgut chymotrypsin.Scientific reports · 2025Article
- Comprehensive proteolytic profiling of Aedes aegypti mosquito midgut extracts: Unraveling the blood meal protein digestion system.PLoS neglected tropical diseases · 2025Article
- In Silico Strategies for Characterizing Inner Cavities of Lipid-Binding Proteins.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Article
- Kunitz-type trypsin inhibitor from durian (Durio zibethinus) employs a distinct loop for trypsin inhibition.Protein science : a publication of the Protein Society · 2024Article
- Homology-based identification and structural analysis ofComputational and structural biotechnology journal · 2024Article
- Characterizing the amyloid core region of the tumor suppressor protein p16The Journal of biological chemistry · 2024Article
- cFLIP - An interacting partner and a novel substrate for pro-apoptotic serine protease HtrA2.Biochemistry and biophysics reports · 2024Article
- Population-specific responses to pollution exposure suggest local adaptation of invasive red swamp crayfish Procambarus clarkii along the Mediterranean French coastline.Environmental science and pollution research international · 2024Article
- Remote loop evolution reveals a complex biological function for chitinase enzymes beyond the active site.Nature communications · 2024Article
- Surface Proteome of Extracellular Vesicles and Correlation Analysis Reveal Breast Cancer Biomarkers.Cancers · 2024Article
- Ligand-Based Design of Selective Peptidomimetic uPA and TMPRSS2 Inhibitors with Arg Bioisosteres.International journal of molecular sciences · 2024Article
- Insufficiency of collagenases in establishment of primary chondrocyte culture from cartilage of elderly patients receiving total joint replacement.Cell and tissue banking · 2023Article
- The genome of Anoplarchus purpurescens (Stichaeidae) reflects its carnivorous diet.Molecular genetics and genomics : MGG · 2023Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Trypsin and chymotrypsin are both serine proteases with high sequence and structural similarities, but with different substrate specificity. Previous experiments have demonstrated the critical role of the two loops outside the binding pocket in controlling the specificity of the two enzymes. To understand the mechanism of such a control of specificity by distant loops, we have used the Gaussian network model to study the dynamic properties of trypsin and chymotrypsin and the roles played by the two loops. A clustering method was introduced to analyze the correlated motions of residues. We have found that trypsin and chymotrypsin have distinct dynamic signatures in the two loop regions, which are in turn highly correlated with motions of certain residues in the binding pockets. Interestingly, replacing the two loops of trypsin with those of chymotrypsin changes the motion style of trypsin to chymotrypsin-like, whereas the same experimental replacement was shown necessary to make trypsin have chymotrypsin's enzyme specificity and activity. These results suggest that the cooperative motions of the two loops and the substrate-binding sites contribute to the activity and substrate specificity of trypsin and chymotrypsin.
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