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- W2022275498 abstract "The effects of temperature on the energy of activation, the enthalpy of binding, and the apparent equilibrium constant for the overall reaction catalyzed by L-histidine ammonia-lyase (EC 4.3.1.3) have been determined. A temperature-dependent transition (at approximately 30°) involving multiple forms of the enzyme is also discussed.The enthalpy of binding is exothermic above 30° and endothermic below this transition temperature. In addition, a bend is observed in the Arrhenius plots at approximately 34°. The combination of these effects suggests the existence of at least two forms of the enzyme." @default.
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- W2022275498 date "1973-05-01" @default.
- W2022275498 modified "2023-09-27" @default.
- W2022275498 title "Temperature-Dependent Transition in L-Histidine Ammonia-Lyase" @default.
- W2022275498 doi "https://doi.org/10.1139/o73-069" @default.
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