ArticleProtein science : a publication of the Protein Society2001
Analysis of crystal structures of aspartic proteinases: on the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes.
Article in Protein science : a publication of the Protein Society, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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27 citing papers in PubMed, 98 citations in OpenAlex.
- Identification of a Novel 1,3,4-Thiadiazole-Based Scaffold as a Plasmepsin V Inhibitor.ACS omega · 2026Article
- Bidirectional effects of cuminaldehyde-pepsin interaction on enzymatic and antioxidant activity: Potential implications for gastrointestinal health and disorder modulation.Food chemistry: X · 2026Article
- Structural Catalytic Core of the Members of the Superfamily of Acid Proteases.Molecules (Basel, Switzerland) · 2024Review
- Structures of plasmepsin X from Plasmodium falciparum reveal a novel inactivation mechanism of the zymogen and molecular basis for binding of inhibitors in mature enzyme.Protein science : a publication of the Protein Society · 2022Article
- Exploring the pH- and Ligand-Dependent Flap Dynamics of Malarial Plasmepsin II.Journal of chemical information and modeling · 2022Article
- Exploring the pH-Dependent Structure-Dynamics-Function Relationship of Human Renin.Journal of chemical information and modeling · 2021Article
- Barley Nepenthesin-Like Aspartic ProteaseFrontiers in plant science · 2021Article
- Structural basis for the specificity of renin-mediated angiotensinogen cleavage.The Journal of biological chemistry · 2019Article
- Modeling and resistant alleles explain the selectivity of antimalarial compound 49c towards apicomplexan aspartyl proteases.The EMBO journal · 2018Article
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- pH Dependence of Chitosan Enzymolysis.Polymers · 2017Article
- Understanding the structural basis of substrate recognition by Plasmodium falciparum plasmepsin V to aid in the design of potent inhibitors.Scientific reports · 2016Article
- N-Glycosylation Improves the Pepsin Resistance of Histidine Acid Phosphatase Phytases by Enhancing Their Stability at Acidic pHs and Reducing Pepsin's Accessibility to Its Cleavage Sites.Applied and environmental microbiology · 2016Article
- Conformational Dynamics and Binding Free Energies of Inhibitors of BACE-1: From the Perspective of Protonation Equilibria.PLoS computational biology · 2015Article
- Computational Insights into Substrate and Site Specificities, Catalytic Mechanism, and Protonation States of the Catalytic Asp Dyad of β -Secretase.Scientifica · 2014Review
- Crystal structure of a putative aspartic proteinase domain of the Mycobacterium tuberculosis cell surface antigen PE_PGRS16.FEBS open bio · 2013Article
- Exploring the binding of BACE-1 inhibitors using comparative binding energy analysis (COMBINE).BMC structural biology · 2012Article
- Structure and activity of the Pseudomonas aeruginosa hotdog-fold thioesterases PA5202 and PA2801.The Biochemical journal · 2012Article
- Structural studies of vacuolar plasmepsins.Biochimica et biophysica acta · 2012Review
- Structural insights into the activation and inhibition of histo-aspartic protease from Plasmodium falciparum.Biochemistry · 2011Article
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Authors and funding
2 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
To elucidate the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes, we analyzed and compared the crystal structures of these enzymes, their complexes with inhibitors, and zymogens in the active site area (a total of 82 structures). In addition to the water molecule (W1) located between the active carboxyls and playing a role of the nucleophile during catalytic reaction, another water molecule (W2) at the vicinity of the active groups was found to be completely conserved. This water molecule plays an essential role in formation of a chain of hydrogen-bonded residues between the active site flap and the active carboxyls on ligand binding. These data suggest a new approach to understanding the role of residues around the catalytic site, which can assist the development of the catalytic reaction. The influence of groups adjacent to the active carboxyls is manifested by pepsin activity at pH 1.0. Some features of pepsin-like enzymes and their mutants are discussed in the framework of the approach.
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