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Binding of histidinal to histidinol dehydrogenase.

Authors :
Görisch H
Hölke W
Source :
European journal of biochemistry [Eur J Biochem] 1985 Jul 15; Vol. 150 (2), pp. 305-8.
Publication Year :
1985

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.

Details

Language :
English
ISSN :
0014-2956
Volume :
150
Issue :
2
Database :
MEDLINE
Journal :
European journal of biochemistry
Publication Type :
Academic Journal
Accession number :
3894023
Full Text :
https://doi.org/10.1111/j.1432-1033.1985.tb09021.x