ArticleBMC structural biology2011
Comparative void-volume analysis of psychrophilic and mesophilic enzymes: Structural bioinformatics of psychrophilic enzymes reveals sources of core flexibility.
Article in BMC structural biology, 2011. 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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Who cites it
27 citing papers in PubMed.
- Structural and biochemical insights into the thermostable esterase Ta0887 from Thermoplasma acidophilum.FEBS open bio · 2026Article
- Adaptation of Folding and Function of a Nuclease from the Cold Deep Sea.Journal of molecular biology · 2026Article
- Catalytic His-loop flexibility drives high activity in hyperthermophilic esterase EstE1 while preserving structural stability.Microbiology spectrum · 2025Article
- Expression and characterization of Est2: a novel cold-adapted esterase from Antarctic bacterium defining the new esterase family XXII.Frontiers in microbiology · 2025Article
- Molecular Biology Applications of Psychrophilic Enzymes: Adaptations, Advantages, Expression, and Prospective.Applied biochemistry and biotechnology · 2024Review
- Kinetic and dynamical properties of truncated hemoglobins of the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125.Protein science : a publication of the Protein Society · 2024Article
- Helping proteins come in from the cold: 5 burning questions about cold-active enzymes.BBA advances · 2024Review
- Cold-Active Lipases and Esterases: A Review on Recombinant Overexpression and Other Essential Issues.International journal of molecular sciences · 2022Review
- Some Clues about Enzymes from Psychrophilic Microorganisms.Microorganisms · 2022Review
- Comparative Proteomic Analysis of Psychrophilic vs. Mesophilic Bacterial Species Reveals Different Strategies to Achieve Temperature Adaptation.Frontiers in microbiology · 2022Article
- Structure andOpen biology · 2021Article
- Current Status of Mining, Modification, and Application of Cellulases in Bioactive Substance Extraction.Current issues in molecular biology · 2021Review
- Psychrophilic enzymes: structural adaptation, pharmaceutical and industrial applications.Applied microbiology and biotechnology · 2021Review
- Mesophilic Pyrophosphatase Function at High Temperature: A Molecular Dynamics Simulation Study.Biophysical journal · 2020Article
- Parallel Strategy Increases the Thermostability and Activity of Glutamate Decarboxylase.Molecules (Basel, Switzerland) · 2020Article
- A Novel Cold-Adapted Leucine Dehydrogenase from Antarctic Sea-Ice BacteriumMarine drugs · 2018Article
- A general and efficient strategy for generating the stable enzymes.Scientific reports · 2016Article
- Comparing Residue Clusters from Thermophilic and Mesophilic Enzymes Reveals Adaptive Mechanisms.PloS one · 2016Article
- Low Temperature Adaptation Is Not the Opposite Process of High Temperature Adaptation in Terms of Changes in Amino Acid Composition.Genome biology and evolution · 2015Article
- Role of Internal Water on Protein Thermal Stability: The Case of Homologous G Domains.The journal of physical chemistry. B · 2015Article
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5 authors.
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Abstract
backgroundPsychrophiles, cold-adapted organisms, have adapted to live at low temperatures by using a variety of mechanisms. Their enzymes are active at cold temperatures by being structurally more flexible than mesophilic enzymes. Even though, there are some indications of the possible structural mechanisms by which psychrophilic enzymes are catalytic active at cold temperatures, there is not a generalized structural property common to all psychrophilic enzymes.
resultsWe examine twenty homologous enzyme pairs from psychrophiles and mesophiles to investigate flexibility as a key characteristic for cold adaptation. B-factors in protein X-ray structures are one way to measure flexibility. Comparing psychrophilic to mesophilic protein B-factors reveals that psychrophilic enzymes are more flexible in 5-turn and strand secondary structures. Enzyme cavities, identified using CASTp at various probe sizes, indicate that psychrophilic enzymes have larger average cavity sizes at probe radii of 1.4-1.5 Å, sufficient for water molecules. Furthermore, amino acid side chains lining these cavities show an increased frequency of acidic groups in psychrophilic enzymes.
conclusionsThese findings suggest that embedded water molecules may play a significant role in cavity flexibility, and therefore, overall protein flexibility. Thus, our results point to the important role enzyme flexibility plays in adaptation to cold environments.
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