Temperature compensation for hybrid devices: Kinesin's K<inf>m</inf> is temperature independent

Detailed measurements of the temperature dependence of kinesin motor protein activity at sub-saturating substrate concentrations from 19 to 34 °C for Drosophila kinesin-1 and thermomyces kinesin-3 was presented. These measurement were carried out based on the assumption that the Km of the kinesin increased with the increasing temperature. Velocity measurements for microtubules gliding on Drosophila kinesin-1 revealed an expected Arrhenius-type increase with increase in temperature for a saturating ATP concentration. Significant changes in the properties of Thermomyces kinesin-3 were observed at temperatures above 45 °C. Another preparation of Thermomyces kinesin-3 indicated altered motility and a km of 175 μM at 23 ° C. It was concluded that the design of a suitable enzymatic network was essential for stabilization against temperature changes.