Is rat skeletal muscle hexokinase an allosteric enzyme?
A recent report by M. Gregoriou, I. P. Trayer, and A. Cornish-Bowden (1986, Eur. J. Biochem. 161, 171-176) showed that the mechanism for rat skeletal muscle hexokinase contains two allosteric sites: one for ATP and one for glucose 6-phosphate. In this report, we show that the allosteric mechanism is at variance with a large amount of kinetic data for the skeletal muscle hexokinase reaction in the literature. In addition, the allosteric mechanism conflicts with isotope exchange at chemical equilibrium data reported by M. Gregoriou, I. P. Trayer, and A. Cornish-Bowden (1983, Eur. J. Biochem. 134, 283-288).
D000494:Allosteric Regulation; D000495:Allosteric Site; D000818:Animals; D006593:Hexokinase / Q000378:metabolism*; D007700:Kinetics; D008433:Mathematics; D008954:Models, Biological; D009132:Muscles / Q000201:enzymology*; D051381:Rats
D006593:Hexokinase