ReviewInternational journal of molecular sciences2012
Optimization to low temperature activity in psychrophilic enzymes.
Review in International journal of molecular sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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Who cites it
73 citing papers in PubMed.
- Structural Adaptations of Bacterial Grx3 to Temperature: Pro29 Is Essential for Cold Adaptation inACS omega · 2025Article
- A structural perspective on the temperature-dependent activity of enzymes.bioRxiv : the preprint server for biology · 2024Article
- Low-temperature features of the psychrophilic chaperonin from Pseudoalteromonas haloplanktis.Archives of microbiology · 2024Article
- Cold-active microbial enzymes and their biotechnological applications.Microbial biotechnology · 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
- Quantifying thermal adaptation of soil microbial respiration.Nature communications · 2023Article
- A general overview of the multifactorial adaptation to cold: biochemical mechanisms and strategies.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023Review
- A Cold-Active Flavin-Dependent Monooxygenase fromACS catalysis · 2023Article
- A bacterial cold-active dye-decolorizing peroxidase from an Antarctic Pseudomonas strain.Applied microbiology and biotechnology · 2023Article
- Tyr76 is essential for the cold adaptation of a class II glutaredoxin 4 with a heat-labile structure from the Arctic bacterium Sphingomonas sp.FEBS open bio · 2023Article
- Discrimination of psychrophilic enzymes using machine learning algorithms with amino acid composition descriptor.Frontiers in microbiology · 2023Article
- Characterization ofMicrobiology spectrum · 2022Article
- Cold-Active Lipases and Esterases: A Review on Recombinant Overexpression and Other Essential Issues.International journal of molecular sciences · 2022Review
- Antarctic aldehyde dehydrogenase from Flavobacterium PL002 as a potent catalyst for acetaldehyde determination in wine.Scientific reports · 2022Article
- Cold-Active Enzymes and Their Potential Industrial Applications-A Review.Molecules (Basel, Switzerland) · 2022Review
- Some Clues about Enzymes from Psychrophilic Microorganisms.Microorganisms · 2022Review
- Genome Functional Analysis of the Psychrotrophic Lignin-Degrading BacteriumFrontiers in microbiology · 2022Article
- Bacterial diversity and their metabolic profiles in the sedimentary environments of Ny-Ålesund, Arctic.Antonie van Leeuwenhoek · 2021Article
- Article
- Cold-Active β-Galactosidases: Insight into Cold Adaption Mechanisms and Biotechnological Exploitation.Marine drugs · 2021Review
13 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Psychrophiles, i.e., organisms thriving permanently at near-zero temperatures, synthesize cold-active enzymes to sustain their cell cycle. These enzymes are already used in many biotechnological applications requiring high activity at mild temperatures or fast heat-inactivation rate. Most psychrophilic enzymes optimize a high activity at low temperature at the expense of substrate affinity, therefore reducing the free energy barrier of the transition state. Furthermore, a weak temperature dependence of activity ensures moderate reduction of the catalytic activity in the cold. In these naturally evolved enzymes, the optimization to low temperature activity is reached via destabilization of the structures bearing the active site or by destabilization of the whole molecule. This involves a reduction in the number and strength of all types of weak interactions or the disappearance of stability factors, resulting in improved dynamics of active site residues in the cold. Considering the subtle structural adjustments required for low temperature activity, directed evolution appears to be the most suitable methodology to engineer cold activity in biological catalysts.
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