Calorimetry of enzyme-catalyzed reactions.

This mini-review shows the valuable contributions of Professor Julian Sturtevant to the current applications of calorimetry to the study of enzyme-catalyzed reactions. The more recent applications of calorimetric techniques such as isothermal titration calorimetry and flow calorimetry to the study of enzyme kinetics, as well as the advantages on using calorimetric techniques in the determination of kinetic parameters of enzymes, is also discussed here.

[1]  D. Winzor,et al.  Further evidence for the reliance of catalysis by rabbit muscle pyruvate kinase upon isomerization of the ternary complex between enzyme and products. , 2003, Biophysical chemistry.

[2]  J F Brandts,et al.  Rapid measurement of binding constants and heats of binding using a new titration calorimeter. , 1989, Analytical biochemistry.

[3]  J. Sturtevant,et al.  The Heat of Hydrolysis of Inorganic Pyrophosphate1 , 1954 .

[4]  M. Cosgrove,et al.  On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. , 1998, Biochemistry.

[5]  J. Sturtevant,et al.  A New Calorimetric Method1,2 , 1951 .

[6]  G. Feller,et al.  Enzyme activity determination on macromolecular substrates by isothermal titration calorimetry: application to mesophilic and psychrophilic chitinases. , 2001, Biochimica et biophysica acta.

[7]  C. Asensio,et al.  Substrate specificity and some other properties of baker's yeast hexokinase. , 1958, Biochimica et biophysica acta.

[8]  A. Beezer,et al.  Sources of error, and their correction, in the analysis of isothermal heat conduction microcalorimetric data: applications of a newly developed test reaction , 2001 .

[9]  J. Gerlt,et al.  The enthalpies of hydrolysis of acyclic, monocyclic, and glycoside cyclic phosphate diesters. , 1975, The Journal of biological chemistry.

[10]  J. Sturtevant,et al.  Calorimetric studies of the activation of chymotrypsinogen A. , 1971, Biochemistry.

[11]  E. Freire,et al.  Direct calorimetric analysis of the enzymatic activity of yeast cytochrome c oxidase. , 1991, Biochemistry.

[12]  S. Kidokoro,et al.  Calorimetric evaluation of the activity and the mechanism of cellulases for the hydrolysis of cello-oligosaccharides accompanied by the mutarotation reaction of the hydrolyzed products , 2005 .

[13]  A. Galina,et al.  Subcellular distribution and kinetic properties of cytosolic and non-cytosolic hexokinases in maize seedling roots: implications for hexose phosphorylation. , 2001, Journal of experimental botany.

[14]  A. Beezer,et al.  Determination of Michaelis–Menten parameters obtained from isothermal flow calorimetric data , 2004 .

[15]  R. Lavecchia,et al.  Kinetic study of hydrogen peroxide decomposition by catalase in a flow-mix microcalorimetric system , 2003 .

[16]  L. Meis.  Uncoupled ATPase activity and heat production by the sarcoplasmic reticulum Ca2+-ATPase. Regulation by ADP. , 2001 .

[17]  J. Sturtevant,et al.  Application of flow calorimetry to the determination of the enthalpies of mixing of organic liquids , 1969 .

[18]  R. Biltonen,et al.  The application of flow microcalorimetry to the study of enzyme kinetics. , 1981, Analytical biochemistry.

[19]  G. Watt,et al.  A microcalorimetric procedure for evaluating the kinetic parameters of enzyme-catalyzed reactions: kinetic measurements of the nitrogenase system. , 1990, Analytical biochemistry.

[20]  A. Vercesi,et al.  A Highly Active ATP-Insensitive K+ Import Pathway in Plant Mitochondria , 2004, Journal of bioenergetics and biomembranes.

[21]  R. Woledge,et al.  Enthalpy changes for intermediate steps of the ATP hydrolysis catalyzed by myosin subfragment-1. , 1979, The Journal of biological chemistry.

[22]  R. Gilli,et al.  A flow microcalorimetric method for enzyme activity measurements: application to dihydrofolate reductase. , 1987, Analytical biochemistry.

[23]  M. L. Bianconi.  Titration Calorimetry as a Tool to Determine Thermodynamic and Kinetic Parameters of Enzymes , 2005 .

[24]  E. Toone,et al.  Calorimetric evaluation of enzyme kinetic parameters , 1993 .

[25]  M. L. Bianconi,et al.  Calorimetric Determination of Thermodynamic Parameters of Reaction Reveals Different Enthalpic Compensations of the Yeast Hexokinase Isozymes* , 2003, Journal of Biological Chemistry.

[26]  J. Sturtevant.  The Heat of Hydrolysis of p-Nitrophenylphosphate1 , 1955 .

[27]  J. Sturtevant,et al.  Action of rennin on casein: heat of reaction. , 1963, Biochimica et biophysica acta.

[28]  H. Levy,et al.  Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides: revised kinetic mechanism and kinetics of ATP inhibition. , 1983, Archives of biochemistry and biophysics.

[29]  J. Sturtevant.  The Heat of Hydrolysis of Poly-L-lysine1 , 1955 .

[30]  L. Lai,et al.  An isothermal titration calorimetric method to determine the kinetic parameters of enzyme catalytic reaction by employing the product inhibition as probe. , 2001, Analytical biochemistry.

[31]  J. Sturtevant,et al.  Heats of Hydrolysis of Peptide Bonds1 , 1961 .

[32]  J. Sturtevant,et al.  Heats of hydrolysis of amide and peptide bonds. , 1952, The Journal of biological chemistry.

[33]  P. Greengard,et al.  Enthalpy of hydrolysis of the 3' bond of adenosine 3',5'-monophosphate and guanosine 3',5'-monophosphate. , 1969, The Journal of biological chemistry.

[34]  J. Sturtevant,et al.  The enthalpy change on adenosine triphosphate hydrolysis. I. , 1955, The Journal of biological chemistry.

[35]  D. Winzor,et al.  A potential role for isothermal calorimetry in studies of the effects of thermodynamic non‐ideality in enzyme‐catalyzed reactions , 2004, Journal of molecular recognition : JMR.

[36]  J. Sturtevant.  Calorimetric Investigations of Organic Reactions. I. Apparatus and Method. The Inversion of Surcrose and the Decomposition of Diacetone Alcohol1 , 1937 .

[37]  Zhiquan Zhang,et al.  High Glucose Inhibits Glucose-6-phosphate Dehydrogenase via cAMP in Aortic Endothelial Cells* , 2000, The Journal of Biological Chemistry.

[38]  J. Sturtevant,et al.  Thermodynamics of hydrolysis of peptide bonds. , 1952, Journal of Biological Chemistry.

[39]  H. Fukada,et al.  Enthalpy and heat capacity changes for the proton dissociation of various buffer components in 0.1 M potassium chloride , 1998, Proteins.

[40]  M J Todd,et al.  Enzyme kinetics determined using calorimetry: a general assay for enzyme activity? , 2001, Analytical biochemistry.