ArticleBiochemistry2022
Structure and Mechanism of a Cold-Adapted Bacterial Lipase.
Article in Biochemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers, 1 of them a synthesis that pooled it.
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Who cites it
10 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Cold-adapted enzymes: mechanisms, engineering and biotechnological application.Bioprocess and biosystems engineering · 2023Pooled it
- Thermodynamic Activation Parameters for Chemical Reactions in Enzymes and Solution from Computer Simulations at a Single Temperature.Journal of chemical theory and computation · 2026Article
- A CALB-like Cold-Active Lipolytic Enzyme fromMarine drugs · 2025Article
- Structural Insights into Cold-Active Lipase from Glaciozyma antarctica PI12: Alphafold2 Prediction and Molecular Dynamics Simulation.Journal of molecular evolution · 2024Article
- Molecular Evolution and Adaptation Strategies in Marine Ciliates: An Inspiration for Cold-Adapted Enzyme Engineering and Drug Binding Analysis.Marine drugs · 2024Review
- Computational studies on the catalytic potential of the double active site for enzyme engineering.Scientific reports · 2024Article
- Helping proteins come in from the cold: 5 burning questions about cold-active enzymes.BBA advances · 2024Review
- Computational design of the temperature optimum of an enzyme reaction.Science advances · 2023Article
- Biochemical Properties of a Cold-Active Chitinase from MarineMarine drugs · 2023Article
- Cold-Active Lipases and Esterases: A Review on Recombinant Overexpression and Other Essential Issues.International journal of molecular sciences · 2022Review
Corrections and comments
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Authors and funding
9 authors.
Funding
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Abstract
The structural origin of enzyme cold-adaptation has been the subject of considerable research efforts in recent years. Comparative studies of orthologous mesophilic-psychrophilic enzyme pairs found in nature are an obvious strategy for solving this problem, but they often suffer from relatively low sequence identity of the enzyme pairs. Small bacterial lipases adapted to distinctly different temperatures appear to provide an excellent model system for these types of studies, as they may show a very high degree of sequence conservation. Here, we report the first crystal structures of lipase A from the psychrophilic bacterium
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