Open AccessKinetic Properties of Triokinase from Rat Liver
Author(s) -
Frandsen Erik K.,
Grunnet Niels
Publication year - 1971
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1971.tb01658.x
Subject(s) - dihydroxyacetone , fructose , glyceraldehyde , dihydroxyacetone phosphate , chemistry , biochemistry , non competitive inhibition , magnesium , glycerol , enzyme , kinetics , metabolism , glyceraldehyde 3 phosphate dehydrogenase , dehydrogenase , organic chemistry , physics , quantum mechanics
Kinetic measurements of the reaction catelyzed by triokinase were carried out with a purified preparation of the enzyme from rat liver. The kinetics with regard to d ‐glyceraldehyde and dihydroxyacetone were of the Michaelis type. The rate of reaction was dependent on the concentration of ATP‐Mg 2− rather than the total ATP or magnesium‐ion concentration. Free ATP and ADP‐Mg − were found to be competitive inhibitors with regard to ATP‐Mg 2− and non‐competitive inhibitors with regard to d ‐glyceraldehyde. Inhibition experiments showed no effect of AMP, L‐glyceraldehyde, inorganic phosphate, fructose, fructose‐1‐ P , fructose‐1,6‐ P 2 , glycerol or glycerate. The possible physiological role of triokinase in relation to the metabolism of fructose is discussed.