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Journal of Biological Sciences

Year: 2005 | Volume: 5 | Issue: 5 | Page No.: 633-636
DOI: 10.3923/jbs.2005.633.636
Additional Possibility of Data Analysis of Enzyme Inhibition and Activation. 7. Analysis of Multiparameter Data in Enzyme Kinetics Using N-dimensional Coordinate Systems
V. I. Krupyanko

Abstract: Possible use of a vector method of representation of enzymatic reactions is considered in the four and five-dimensional (K mV E ani) and (K mV E aA ni) coordinate systems for data processing of a simultaneous course of change in four K m, V , E a, ni and five K m, V , E a, A , ni) parameters of inhibition of the mutant forms of Escherichia coli E15 alkaline phosphatase modified by substitution of neutral amino acid residues in two N-terminal peptides by positively charged lysine residues (Lys, Lys) in the positions (+2+3), (+5+6), (+13+14), (+19+20) and arginine ones (Arg, Arg) in the positions (+5+6), (+13+14), (+19+20). It is established that at transfer of positive charges to the enzyme active centre the maximum inhibitory effect of enzyme activity occurs at substitution in the position (+13+14) from the N-terminus. This effect intensifies with increasing charge of amino acid residues (Lys Arg ).

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How to cite this article
V. I. Krupyanko , 2005. Additional Possibility of Data Analysis of Enzyme Inhibition and Activation. 7. Analysis of Multiparameter Data in Enzyme Kinetics Using N-dimensional Coordinate Systems. Journal of Biological Sciences, 5: 633-636.

Keywords: Mutant forms of E. coli E15 alkaline phosphates, a vector method of data processing in the four and five-dimensional coordinate systems

REFERENCES
  • Krupyanko, V.I., 2004. A Vector Method of Representation of Enzymatic Reactions. 3. Three-dimensional system of the (K!mV!I) coordinates convenient for representation of enzyme inhibition and activation. Process Biochem., 39: 825-832.

  • 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, 2005. 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: 98-102.

  • Krupyanko, P.V., V.I. Krupyanko and I.N. Dorokhov, 2005. Additional possibility of data analysis of enzyme inhibition and activation 3. Geometrical portraits of enzymatic reactions for data processing in enzyme temperature activation. J. Biological Sci., 5: 98-102.
    CrossRef    Direct Link    

  • Kononova, S.V., C.N. Zolov, V.I. Krupyanko and M.A. Nesmeyanova, 2000. The primary structure of the N-terminal region of mature alkaline phosphatase is important for secretion and functioning of the enzyme. J. Applied Biochem. Microbiol., 65: 1270-1277.

  • Nesmeyanova, M.A., A.E. Kalinin, A.L. Karamyshev, N.I. Michaleva and V.I. Krupyanko, 1997. Overproduction, secretion, isolation and properties of recombinant alkaline phosphatase encoded in Escherichia coli. Process Biochem., 32: 1-7.

  • 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: 116-119.
    Direct Link    

  • Lazdunski C. and M. Lazdunski, 1996. Etude cinetigue du mecanisme action catalytigue de la phosphatase alcaline Escherichia coli. Biochim. Biophys. Acta, 113: 551-566.

  • Lazdunski, M., C. Petitclerc, D. Chappelet and C. Lazdunski, 1971. Flip-flop mechanisms in enzymology. A model: The alkaline phosphatase Escherichia coli. Eur. J. Biochem., 20: 124-139.

  • Garen A. and C. Levinthal, 1960. A fine-structure genetic and chemical study of the enzyme alkaline phosphatase of E. coli. Biochim. Biophys. Acta, 38: 470-483.

  • Sowadski, J.M., M.D. Handschumacher, H.M. Murthy, B.A. Foster and H.W. Wyckoff, 1985. Refined structure of alkaline phosphatase from Escherichia coli at 2.8 A resolution. J. Mol. Biol., 186: 417-433.

  • Krupyanko, V.I., 1990. A Vector Method of Representation of Enzymatic Reactions. Nauka, Moscow

  • Robert B. McComb, G.N. Bowers and S. Posen, 1979. Alkaline Phosphatase. Plenum Press, New York

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