Mechanistic Origin of the Sigmoidal Rate Behaviour of Rat Liver Hexokinase D ('glucokinase')

Overview

Journal Biochem J

Specialty Biochemistry

Date 1986 Nov 15

PMID 3493769

Citations 10

Authors

A Cornish-Bowden

A C Storer

Affiliations

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Abstract

Two recent proposals to account for the kinetic co-operativity of hexokinase D ('glucokinase') from rat liver are examined. A model in which the deviations from Michaelis-Menten kinetics result from a random order of binding of the substrates [Pettersson (1986) Biochem. J. 233, 347-350] accounts satisfactorily for the behaviour as a function of glucose concentrations, but it also predicts observable substrate inhibition by MgATP, which is in fact not observed. An alternative proposal in which the deviations arise from recycling of an enzyme-MgADP complex [Pettersson (1986) Eur. J. Biochem. 154, 167-170] also accounts satisfactorily for some of the data, but the required enzyme-MgADP complex could not be detected in isotope-exchange measurements. Thus the mnemonical mechanism proposed originally [Storer & Cornish-Bowden (1977) Biochem. J. 165, 61-69], which explains the deviations in terms of a relatively slow interconversion between two forms of free enzyme, remains the most parsimonious explanation of the behavior of hexokinase D.

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References

Ricard J, Meunier J, Buc J . Regulatory behavior of monomeric enzymes. 1. The mnemonical enzyme concept. Eur J Biochem. 1974; 49(1):195-208. DOI: 10.1111/j.1432-1033.1974.tb03825.x. View

Pettersson G . Mechanistic origin of the sigmoidal rate behaviour of glucokinase. Biochem J. 1986; 233(2):347-50. PMC: 1153034. DOI: 10.1042/bj2330347. View

Niemeyer H, de la Luz Cardenas M, RABAJILLE E, URETA T, CLARK-TURRI L, Penaranda J . Sigmoidal kinetics of glucokinase. Enzyme. 1975; 20(6):321-33. DOI: 10.1159/000458957. View

Holroyde M, Allen M, Storer A, Warsy A, Chesher J, Trayer I . The purification in high yield and characterization of rat hepatic glucokinase. Biochem J. 1976; 153(2):363-73. PMC: 1172582. DOI: 10.1042/bj1530363. View

Storer A, Cornish-Bowden A . Kinetics of rat liver glucokinase. Co-operative interactions with glucose at physiologically significant concentrations. Biochem J. 1976; 159(1):7-14. PMC: 1164031. DOI: 10.1042/bj1590007. View

Storer A, Cornish-Bowden A . Kinetic evidence for a 'mnemonical' mechanism for rat liver glucokinase. Biochem J. 1977; 165(1):61-9. PMC: 1164869. DOI: 10.1042/bj1650061. View

Connolly B, Trayer I . Reaction of rat hepatic glucokinase with substrate-related and other alkylating agents. Eur J Biochem. 1979; 99(2):299-308. DOI: 10.1111/j.1432-1033.1979.tb13257.x. View

Cardenas M, RABAJILLE E, Niemeyer H . Kinetic cooperativity of glucokinase with glucose. Arch Biol Med Exp. 1979; 12(5):571-80. View

Gregoriou M, Trayer I, Cornish-Bowden A . Isotope-exchange evidence for an ordered mechanism for rat-liver glucokinase, a monomeric cooperative enzyme. Biochemistry. 1981; 20(3):499-506. DOI: 10.1021/bi00506a009. View

10.

Tippett P, NEET K . An allosteric model for the inhibition of glucokinase by long chain acyl coenzyme A. J Biol Chem. 1982; 257(21):12846-52. View

11.

Andersson P, Kvassman J, Olden B, Pettersson G . Catalytic significance of binary enzyme-aldehyde complexes in the liver alcohol dehydrogenase reaction. Eur J Biochem. 1984; 139(3):519-27. DOI: 10.1111/j.1432-1033.1984.tb08036.x. View

12.

Cornish-Bowden A . Solvent isotope effects on the glucokinase reaction. Negative co-operativity and a large inverse isotope effect in 2H2O. Eur J Biochem. 1984; 141(1):157-63. DOI: 10.1111/j.1432-1033.1984.tb08170.x. View

13.

Cardenas M, RABAJILLE E, Niemeyer H . Suppression of kinetic cooperativity of hexokinase D (glucokinase) by competitive inhibitors. A slow transition model. Eur J Biochem. 1984; 145(1):163-71. DOI: 10.1111/j.1432-1033.1984.tb08536.x. View

14.

Pettersson G . Mechanistic origin of the kinetic cooperativity of hexokinase type L1 from wheat germ. Eur J Biochem. 1986; 154(1):167-70. DOI: 10.1111/j.1432-1033.1986.tb09374.x. View

15.

Meunier J, Buc J, Navarro A, Ricard J . Regulatory behavior of monomeric enzymes. 2. A wheat-germ hexokinase as a mnemonical enzyme. Eur J Biochem. 1974; 49(1):209-23. DOI: 10.1111/j.1432-1033.1974.tb03826.x. View