ArticleJournal of chemical information and modeling2022
Role of Enzyme and Active Site Conformational Dynamics in the Catalysis by α-Amylase Explored with QM/MM Molecular Dynamics.
Article in Journal of chemical information and modeling, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 35 citations in OpenAlex.
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- Mechanism of Polyester Hydrolysis by Marine Bacterium PE-H Enzyme: an Atomistic and Thermodynamic Characterization.Journal of chemical information and modeling · 2026Article
- A Multienzyme Magnetic Nanocatalyst for Efficient, Sustainable Hydrolysis of Wastewater-Grown Microalgae Consortia.ACS sustainable chemistry & engineering · 2026Article
- Molecular insights of acarbose metabolization catalyzed by acarbose-preferred glucosidase.Nature communications · 2025Article
- Special Issue: "Advanced Research on Molecular Modeling of Protein Structure and Functions".International journal of molecular sciences · 2025Article
- Accurate Free Energy Calculation via Multiscale Simulations Driven by Hybrid Machine Learning and Molecular Mechanics Potentials.Journal of chemical theory and computation · 2025Article
- Correlating enzymatic reactivity for different substrates using transferable data-driven collective variables.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Current status and emerging frontiers in enzyme engineering: An industrial perspective.Heliyon · 2024Review
- The Anti-Diabetic Effects of Medicinal Plants Belonging to the Liliaceae Family: Potential Alpha Glucosidase Inhibitors.Drug design, development and therapy · 2024Review
- The Enzymatic Hydrolysis of Human Milk Oligosaccharides and Prebiotic Sugars from LAB Isolated from Breast Milk.Microorganisms · 2023Article
- Drug Design in the Exascale Era: A Perspective from Massively Parallel QM/MM Simulations.Journal of chemical information and modeling · 2023Review
- Unraveling the catalytic mechanism of SARS-CoV-2 papain-like protease with allosteric modulation of C270 mutation using multiscale computational approaches.Chemical science · 2023Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We assessed enzyme:substrate conformational dynamics and the rate-limiting glycosylation step of a human pancreatic α-amylase:maltopentose complex. Microsecond molecular dynamics simulations suggested that the distance of the catalytic Asp197 nucleophile to the anomeric carbon of the buried glucoside is responsible for most of the enzyme active site fluctuations and that both Asp197 and Asp300 interact the most with the buried glucoside unit. The buried glucoside binds either in a
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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.