Activation of Brain Hexokinase by Magnesium Ions and by Magnesium Ion--adenosine Triphosphate Complex
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1. An alternative explanation for the kinetic data obtained by Bachelard (1971) for the brain hexokinase reaction is presented. 2. Apparently sigmoidal saturation curves for MgATP(2-) based upon Bachelard's (1971) studies can be corrected to hyperbolic curves by use of a stability constant for MgATP(2-) complex formation. 3. A number of other effects related to the concentration-dependent stability of the MgATP(2-) complex and to the presence of the inhibitory free uncomplexed ATP(4-) concentration are also explained in terms of a non-allosteric role for either Mg(2+) or MgATP(2-) fully consistent with a number of previous reports on this enzyme. 4. A brief discussion of the validity of Hill plots in studies of multisubstrate co-operative enzymes is presented. 5. A simple model is presented that demonstrates how enzymes obeying Michaelis-Menten kinetics can demonstrate sigmoidal velocity responses if the true substrate of the reaction is the metal-substrate complex.
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Umekawa M, Hamada K, Isono N, Karita S J Appl Glycosci (1999). 2021; 67(4):103-109.
PMID: 34354536 PMC: 8119236. DOI: 10.5458/jag.jag.JAG-2020_0007.
Microcalorimetric study of magnesium-adenosine triphosphate ternary complex.
Sari J, Hadida M, Crevat A J Bioenerg Biomembr. 1982; 14(3):171-9.
PMID: 6980221 DOI: 10.1007/BF00745018.
Kamikashi T, Kizaki H, Murakami K, Ishibashi S Biochem J. 1974; 137(1):139-42.
PMID: 4463972 PMC: 1166094. DOI: 10.1042/bj1370139.
Differences in catalytic properties between cerebral cytoplasmic and mitochondrial hexokinases.
Thompson M, Bachelard H Biochem J. 1977; 161(3):593-8.
PMID: 851431 PMC: 1164545. DOI: 10.1042/bj1610593.