Submit Manuscript

Journal of Biological Sciences

Year: 2005 | Volume: 5 | Issue: 1 | Page No.: 98-102
Facebook Twitter Digg Reddit Linkedin StumbleUpon E-mail
Research Article

Additional Possibility of Data Analysis of Enzyme Inhibition and Activation 3. Geometrical Portraits of Enzymatic Reactions for Data Processing in Enzyme Temperature Activation

P.V. Krupyanko, V.I. Krupyanko and I.N. Dorokhov

ABSTRACT

When calculating enzyme energy activation (Eα), researchers tend to only plot a temperature dependence of the course of change in the logarithm (lg V) of maximum reaction rate upon (1/T�K) and determine these thermodynamic parameters by the slope angle (tg α) of experimental lines in the (lg V;1/T) coordinates of Arrhenius. Yet, the course of change in the Michaelis constant (Km), the second important parameter of enzyme activation, is not taken into consideration as there is no this parameter in the Arrhenius equation. In practice, simultaneous account of temperature dependence in the course of change of both V and Km parameters allows additional analysis of the dynamics of enzyme temperature activation. A vector method of representation of such data in the three-dimensional KmVt coordinate system is proposed. Examples of data processing in temperature activation of bovine pyrimidine-specific RNases A and B using conventional methods and the proposed one are given.
PDF References Citation

How to cite this article

P.V. Krupyanko, 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. Journal of Biological Sciences, 5: 98-102.

DOI: 10.3923/jbs.2005.98.102

URL: https://scialert.net/abstract/?doi=jbs.2005.98.102

Search

REFERENCES

  1. Sim, E. and P.M. Vignais, 1979. Comparsion of the membrane-bound and detergent-solubilized hydrogenase from Paraccoccus dinitrificans. Biochim. Biophys. Acta, 570: 43-53.
  2. Miyairi, S., 1979. An enzyme-polymer film prepeared with the use of poly vinyl-alcohol) bearing photosensitive aromatic azido groups. Biochim. Biophys. Acta, 571: 374-377.
  3. Norling, A. and O. Hanninen, 1974. Activation energy of glucuronide biosynthesis. Biochem. Biophys. Acta, 350: 183-192.
  4. Burgos, J., R. Martin and V. Diez, 1974. Pigeon liver diacetyl reductase kinetic and thermodynamic studies with NADH as coenzyme. Biochim. Biophys. Acta, 364: 9-16.
  5. Guranowski, A. and P. Kiewicz, 1977. Adenosylhomocysteinase from yellow lupin seeds. Eur. J. Biochem., 80: 517-523.
  6. Lazdunski C. and M. Lazdunski, 1996. Etude cinetigue du mecanisme action catalytigue de la phosphatase alcaline Escherichia coli. Biochim. Biophys. Acta, 113: 551-566.
  7. 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.
  8. Kilsheimer, G.S. and B. Axelrod, 1957. Inhibition of prostatic acid phosphatase by α-hydroxycarboxylic acids. J. Biol. Chem., 227: 879-889.
  9. Baldijao, C.E.M., E. Guila, H.M.S. Bittencourt and H. Chaimovich, 1975. Steady state kinetics and effect of SH inhibitors on acid phosphatase from bovine brain. Biochim. Biophys. Acta, 391: 316-325.
  10. Saini, M.N. and R.L. Etten, 1978. A homogeneous isoenzyme of human liver acid phosphatase. Arch. Biochem. Biophys., 191: 613-624.
  11. Lazdunski, C. and M. Lazdunski, 1969. Zn2+ and Co2+-alkaline phosphatases of E. coli. A comparative kinetic study. Eur. J. Biochem., 7: 294-300.
  12. Yang, Y., S. Cun, L. Peng, X. Xie, J. Wei, W. Yang and A. Xu, 2003. cDNA cloning, idenfication and charaacterization of a novel cystatin from the tentacle of Cyanea capillata. Biochemie, 85: 1033-1039.
  13. Yamada T. and N. Akutsu, 1990. Purification, catalytic properties and thermal stability of threo-Ds-3-isopropylmalate dehydrogenase coded by leuB gene from an external thermophile, Thermus thermophylius strain HBS. J. Biochem., 108: 449-456.
  14. Bienvenue D.L., D.M. Gilner, R.S. Davis, B. Bennett and R.C. Holz, 2003. Substrate specificity, metal binding properties and spectroscopic characterization of the DupE-Encoded N-Succinyl-L,L-Diaminopimlin Acid Desuccinilase from Hacmiphilas influenzae. Biochemistry, 42: 10756-10763.
  15. Erable, B., I. Goubet, S. Lamare, D. Ligou and T. Maugard, 2004. Haloalkane hydrolysis by Rhodococcus erytropolis cells. Biotech. Bioeng., 86: 47-54.
  16. Miles, C.A. and A.J. Bailey, 2004. Studies of the collagene-like peptide (Pro-Pro-Gly)10 confirm that the shape and position of the type I collagene denaturation endotherm is governed by the rate of helix unfolding. J. Mol. Biol., 337: 917-931.
  17. Krupyanko, V.I., 1990. A Vector Method of Representation of Enzymatic Reactions. Nauka, Moscow, pp: 3-142.
  18. Krupyanko, V.I., 1996. Applicability of vector presentation of enzymatic reactions to the analysis of enzyme activation and inhibition. Applied Biochem. Microbiol., 32: 144-152.
  19. 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
  20. Krupyanko, V.I., Z.S. Kagan, G.S. Ivanova and S.I. Bezborodova, 1978. Activation parameters for the cleavage reaction of cytidine-2N;3N-monophosphate catalyzed by Penicillium brevicompactum and Aspergillus clavatus Rnases. Biochemistry, 43: 184-186.
  21. Vladimir, S.S., 1968. Nucleases. NLM., Moscow, pp: 9-211.
  22. Irvin, H.S., 1975. Enzyme Kinetics. John Wiley and Sons, New York, pp: 47-100.
  23. McComb, R.B., G.N. Bowers and S. Posen, 1979. Alkaline Phosphatase. Plenum Press, New York.

Search

Leave a Comment

Your email address will not be published. Required fields are marked *