Abstract
AT physiological substrate concentrations, the rates of enzymatic reactions of poikilotherms may be highly independent of temperature1–5. The basis of this effect has recently been clarified: for all enzymes from poikilotherms which we have examined, enzyme-substrate (E-S) affinity varies inversely with temperature over a large portion of the species' range of habitat temperatures. In addition, E-S affinity frequently reaches a maximum at temperatures near the lower extreme of the species' habitat temperatures3–5.
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References
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SOMERO, G., HOCHACHKA, P. Isoenzymes and Short-term Temperature Compensation in Poikilotherms: Activation of Lactate Dehydrogenase Isoenzymes by Temperature Decreases. Nature 223, 194–195 (1969). https://doi.org/10.1038/223194a0
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DOI: https://doi.org/10.1038/223194a0
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