ArticleBiophysical journal2009
Exploring local flexibility/rigidity in psychrophilic and mesophilic carbonic anhydrases.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.
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Who cites it
21 citing papers in PubMed, 1 synthesis or guideline pooled it, 62 citations in OpenAlex.
- A meta-analysis of the activity, stability, and mutational characteristics of temperature-adapted enzymes.Bioscience reports · 2021Pooled it
- Improving enzymatic properties of BlTDH fromFood chemistry. Molecular sciences · 2025Article
- Expression and characterization of Est2: a novel cold-adapted esterase from Antarctic bacterium defining the new esterase family XXII.Frontiers in microbiology · 2025Article
- Enzyme Engineering: Performance Optimization, Novel Sources, and Applications in the Food Industry.Foods (Basel, Switzerland) · 2024Review
- Biochemical and in silico structural characterization of a cold-active arginase from the psychrophilic yeast, Glaciozyma antarctica PI12.Extremophiles : life under extreme conditions · 2024Article
- A multi-functional genetic manipulation system and its use in high-level expression of a β-mannanase mutant with high specific activity in Pichia pastoris.Microbial biotechnology · 2021Article
- Characterization of SdGA, a cold-adapted glucoamylase fromBiotechnology reports (Amsterdam, Netherlands) · 2021Article
- Parallel molecular mechanisms for enzyme temperature adaptation.Science (New York, N.Y.) · 2021Article
- Exploring the Cold-Adaptation Mechanism of Serine Hydroxymethyltransferase by Comparative Molecular Dynamics Simulations.International journal of molecular sciences · 2021Article
- The high catalytic rate of the cold-active Vibrio alkaline phosphatase requires a hydrogen bonding network involving a large interface loop.FEBS open bio · 2021Article
- The Role of Surface Exposed Lysine in Conformational Stability and Functional Properties of Lipase fromMolecules (Basel, Switzerland) · 2020Article
- Deciphering the Structural Basis of High Thermostability of Dehalogenase from Psychrophilic BacteriumMicroorganisms · 2019Article
- A comparative study of cold- and warm-adapted Endonucleases A using sequence analyses and molecular dynamics simulations.PloS one · 2017Article
- Improving the Thermostability and Activity of a Thermophilic Subtilase by Incorporating Structural Elements of Its Psychrophilic Counterpart.Applied and environmental microbiology · 2015Article
- Psychrophilic enzymes: from folding to function and biotechnology.Scientifica · 2013Review
- Fluorescence studies on the stability, flexibility and substrate-induced conformational changes of acetate kinases from psychrophilic and mesophilic bacteria.The protein journal · 2012Article
- Optimization to low temperature activity in psychrophilic enzymes.International journal of molecular sciences · 2012Review
- Serine hydroxymethyltransferase from the cold adapted microorganism Psychromonas ingrahamii: a low temperature active enzyme with broad substrate specificity.International journal of molecular sciences · 2012Article
- Comparative void-volume analysis of psychrophilic and mesophilic enzymes: Structural bioinformatics of psychrophilic enzymes reveals sources of core flexibility.BMC structural biology · 2011Article
- Biotechnological uses of enzymes from psychrophiles.Microbial biotechnology · 2011Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Molecular flexibility and rigidity are required to determine the function and specificity of protein molecules. Some psychrophilic enzymes demonstrate a higher catalytic efficiency at low temperatures, compared to the efficiency demonstrated by their meso/thermophilic homologous. The emerging picture suggests that such enzymes have an improved flexibility of the structural catalytic components, whereas other protein regions far from functional sites may be even more rigid than those of their mesophilic counterparts. To gain a deeper insight in the analysis of the activity-flexibility/rigidity relationship in protein structure, psychrophilic carbonic anhydrase of the Antarctic teleost Chionodraco hamatus has been compared with carbonic anhydrase II of Bos taurus through fluorescence studies, three-dimensional modeling, and activity analyses. Data demonstrated that the cold-adapted enzyme exhibits an increased catalytic efficiency at low and moderate temperatures and, more interestingly, a local flexibility in the region that controls the correct folding of the catalytic architecture, as well as a rigidity in the hydrophobic core. The opposite result was observed in the mesophilic counterpart. These results suggest a clear relationship between the activity and the presence of flexible and rigid protein substructures that may be useful in rational molecular and drug design of a class of enzymes playing a key role in pathologic processes.
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