Additional Possibility of Data Analysis of Enzyme Inhibition and Activation. 4. Criterion of Stability of the Mechanism of Proceeding of Enzymatic Reactions
Abstract:
Possible use of the criterion of stability of the mechanism of proceeding of enzymatic reactions for studying the effect of increasing concentration of inhibitors on the enzyme were analysed. It was shown that the constant of inhibition (Ki) characterizes the strength of binding of the inhibitor to the enzyme. The length of Li vectors for enzyme inhibition in three-dimensional K` mV` I coordinate system characterizes the intensity of inhibition. This opens up additional possibility of studying the mechanism of proceeding of enzymatic reactions at consecutive addition of inhibitors, activators and also under varying temperature conditions, etc., with the aim to increase the yield of a reaction product. Examples of using the dependencies of change in the length of Li vectors of enzyme inhibition for characterization of the dynamics of a stable and unstable inhibitory effect on calf alkaline phosphatase are given.
How to cite this article
V. I. Krupyanko and P. V. Krupyanko, 2005. Additional Possibility of Data Analysis of Enzyme Inhibition and Activation. 4. Criterion of Stability of the Mechanism of Proceeding of Enzymatic Reactions. Journal of Biological Sciences, 5: 292-296.
REFERENCES
Steinke, L., R. Bacon and S.M. Schuster, 1987. The effects of exchange-inert metal-nucleotide complexes on the kinetics of beef heart mitochondrial F1-ATPase. Arch. Bioch. Biophys., 258: 482-490.
Podshun, B., P.F. Cook and K.D. Schnackerz, 1990. Kinetic mechanism of dihydropyrimidine dehydrogenase from pig liver. J. Biol. Chem., 265: 12966-12972.
Gaudineau, C., R. Beckerman, S. Welbourn and K. Auclair, 2004. Inhibition of human P450 enzymes by multiple constituents of the Ginkgo biloba extract. Biochem. Biophys. Res. Com., 318: 1072-1078.
Makarov, A.A., G.I. Yakovlev, V.A. Mitkevich, J.J. Higgin and R.T. Raines, 2004. Zinc(II)-mediated inhibition of ribonuclease Sa by an N-hydroxyurea nucleotide and its basis. Biochem. Biophys. Res. Comm., 319: 152-156.
Wilson, J.E. and V. Chung, 1989. Rat brain hexokinase: Further studies on the specificity of the hexose and hexose 6-phosphate binding sites. Arch. Bioch. Biophys., 269: 517-525.
Smith, D.F., D.P. Kosow, C. Wu and G.A. Jamieson, 1977. Characterization of human platelet UDP-glucose-collagen glycosyltransferase using a new rapid assay. Biochim. Biophys. Acta, 483: 263-278.
Whitman, M., D. Kaplan, T. Roberts and L. Cantley, 1987. Evidence for two distinct phosphatidylinositol kinases in fibroblasts. Biochem. J., 247: 165-174.
Seubert, P.A., F. Renosto, P. Knudson and I.H. Segel, 1985. Adenosinetriphosphate sulfurase from Penicillium chrysogenum: Steady-state kinetics of the forward and reverse reactions, alternative substrate kinetics and equilibrium binding studies. Arch. Bioch. Biophys., 240: 509-523.
Bhaird, N.N.A., G. Kumaravel, R.D. Gandour, M.J. Krueger and R.R. Ramsay, 1993. Comparison of the active sites of the purified carnitine acyltransferases from peroxisomes and mitochondria by using a reaction-intermediate analogue. Biochem. J., 294: 645-651.
Rangarajan, M. and B.S. Hartley, 1992. Mechanism of D-fructose isomerization by Arthrobacter D-xylose isomerase. Biochem. J., 283: 223-233.
Garbers, D.L., 1978. Demonstration of 5N-methylthioadenosine phosphorylase activity in various rat tissues. Some properties of the enzyme from rat lung. Biochim. Biophys. Acta, 523: 82-93.
Kato, N., H. Sahm and F. Wagner, 1979. Steady-state kinetics of formaldehyde dehydrogenase and formate dehydrogenase from a methanol-utilizing yeast, Candida biodini. Biochem. Biophys. Acta, 556: 12-20.
Tian, G., C.D. Sobotka-Briner, J. Zysk, X. Liu and C. Birr et al., 2002. Linear non-competitive inhibition of solubilized human γ-secretase by pepstatin A methylester, L685456, sulfonamides and benzodiazepines. J. Biol. Chem., 277: 31499-31505.
Cuenllas, E., S. Gaitan, J.A. Bueren and C. Tejero, 1989. Pyruvate kinase during in vitro differentiation of GM-CFC haemopoietic precursor in mice: Modulation by L-alanine and L-phenylalanine. Biochimie, 71: 763-766.
Denicola-Seoane, A. and B.M. Anderson, 1990. Purification and characterization of Haemophilus influenzae D-lactate dehydrogenase. J. Biol. Chem., 265: 3691-3696.
Bhat, G.B., K. Iwase, B.C.W. Hummel and P.G. Walfish, 1989. Kinetic characteristics of a thioredoxin-activated rat hepatic and renal low-Km iodothyronine 5N-deiodinase. Biochem. J., 258: 785-792.
Andreassi, J.L. and R.G. Moran, 2002. Mouse folylpoly-γ-glutamate synthetase isoforms respond differently to feedback inhibition by folylpolyglutamate cofactors. Biochemistry, 41: 226-235.
Krupyanko, V.I., 1990. A Vector Method of Representation of Enzymatic Reactions. Nauka, Moscow, pp: 3-142
Krupyanko, V.I., 2004. Additional possibility of data analysis of enzyme inhibition and activation. 1. Equations for calculation of the Ka and Ki constants of enzyme activation and nontrivial types of enzyme inhibition. J. Biol. Sci., 5: 82-91.
Krupyanko, V.I., P.V. Krupyanko and I.N. Dorokhov, 2004. Additional possibility of data analysis of enzyme inhibition and activation. 2. Geometrical portraits of enzymatic reactions for data processing in enzyme inhibition. J. Biol. Sci., 5: 92-97.
Krupyanko, P.V., V.I. Krupyanko and I.N. Dorokhov, 2004. Additional possibility of data analysis of enzyme inhibition and activation. 3. Geometrical portraits of enzymatic reactions for data processing in enzyme temperature activation. J. Biol. Sci., 5: 98-102.
Krupyanko, V.I. and P.V. Krupyanko, 1999. Selection of substrate concentrations for determining the michaelis constant and maximum rate of an enzymatic reaction. Applied Biochem. Microbiol., 35: 133-136.
Krupyanko, V.I., 1996. Applicability of vector representation of enzymatic reactions to the analysis of enzyme activation and inhibition. Applied Biochem. Microbiol., 32: 144-152.
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