temperature optimum very low

Edge evidence

• cold environment selects for psychrophile cold-adapted machinery METPO:2007401

  Cold environments select for cold-adapted enzymes and lipids.

  • DOI:10.1038/sj.embor.7400662 growing well at temperatures around the freezing point of water Supports cold habitats as the context for psychrophile machinery.
• psychrophile cold-adapted machinery produces temperature optimum very low METPO:2000202

  Psychrophile cold-adapted machinery yields a very-low temperature optimum.

  • DOI:10.1146/annurev-micro-091313-103612 more unsaturated fatty acids Supports homoviscous adaptation as the mechanism setting the psychrophile optimum.
• temperature optimum very low is a temperature optimum rdfs:subClassOf

  Temperature optimum very low is a quantitative bin of the temperature-optimum phenotype.

  • DOI:10.1038/sj.embor.7400662 growing well at temperatures around the freezing point of water Supports a ≤10 °C optimum as a value within the temperature-optimum distribution.
• fatty acid desaturase activity increases abundance of unsaturated fatty acids

  Fatty acid desaturase activity increases unsaturated acyl chains.

  • DOI:10.17159/sajs.2018/20170254 activation of desaturases, increased unsaturated acyl chains
• unsaturated fatty acids maintains membrane fluidity at low temperature

  Increased unsaturated fatty acids maintain membrane fluidity at low temperature.

  • DOI:10.1128/AEM.01928-22 maintain membrane fluidity by improving the ratio of unsaturated fatty acids
• membrane fluidity at low temperature supports psychrophile cold-adapted machinery

  Maintained membrane fluidity supports cold-adapted cellular machinery.

  • DOI:10.1128/AEM.01928-22 maintained membrane fluidity sustains function at low temperature
• cold shock proteins / RNA chaperones supports translation at low temperature

  Cold shock proteins / RNA chaperones support transcription and translation in the cold.

  • DOI:10.17159/sajs.2018/20170254 Cold-shock proteins are major cold responses, functioning in regulation of transcription/translation
• glycine betaine stabilizes protein and membrane stabilization under cold stress

  Glycine betaine prevents protein aggregation and stabilizes membranes during cold stress.

  • DOI:10.17159/sajs.2018/20170254 including glycine betaine and trehalose - prevent protein aggregation and stabilize membranes
• trehalose acts as cryoprotection

  Trehalose acts as a cryoprotectant.

  • DOI:10.1038/sj.embor.7400662 Compatible solutes (trehalose) and extracellular polysaccharides act as cryoprotectants
• antifreeze / ice-binding proteins causes thermal hysteresis / lowered freezing point biolink:causes

  Antifreeze proteins lower the freezing point via thermal hysteresis.

  • DOI:10.1007/s42770-023-01057-4 AFPs lower freezing point via thermal hysteresis
• increased enzyme structural flexibility increases catalytic activity at low temperature RO:0002213

  Increased enzyme structural flexibility increases catalytic activity at low temperature.

  • DOI:10.17159/sajs.2018/20170254 Cold-adapted enzymes display increased structural flexibility and higher catalytic efficiency