V. I. Krupyanko
G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, 142290 Pushchino, Prospect Nauki 5, Moscow Region, Russia
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.
DOI: 10.3923/jbs.2005.633.636
URL: https://scialert.net/abstract/?doi=jbs.2005.633.636
DOI: 10.3923/jbs.2005.633.636
URL: https://scialert.net/abstract/?doi=jbs.2005.633.636
REFERENCES
- 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.
CrossRefDirect Link - 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.
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