Binding of histidinal to histidinol dehydrogenase
- 1 July 1985
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 150 (2) , 305-308
- https://doi.org/10.1111/j.1432-1033.1985.tb09021.x
Abstract
One molecule of the enzymatic intermediate histidinal is firmly bound per subunit of histidinol dehydrogenase (EC 1.1.1.23) and protected against decomposition. The dissociation rate constant of the histidinal--histidinol dehydrogenase complex is estimated as 2.5 X 10(-5) S-1. Steady-state kinetic measurements studying the oxidation of histidinal to histidine and the reduction of histidinal to histidinol allow to calculate the association rate constants for histidinal. For both reactions the association rate constant is found as 1.9 X 10(6) M-1 S-1. Thus the dissociation constant of the histidinal--histidinol dehydrogenase complex is estimated to be of the order of 1.4 X 10(-11) M.Keywords
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