Journal archive > 2010 > N 6 November-December

KINETIC REGULARITIES AND MECHANISMS OF ACTION OF?CALIX[4]ARENE C-99
ON? ATPase ACTIVITY OF MYOSIN SUBFRAGMENT-1 OF MYOMETRIUM

A. A. Bevza1, R. D. Labyntseva1, О.? V.? Bevza1, S. O. Cherenok2, V. ?I.? Kalchenko2, S. O. Kosterin1

1Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;
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2Institute of Organic Chemistry, National Academy of Sciences of Ukraine, Kyiv;
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It has been shown that calix[4]arene C-99 inhibited myosin subfragment-1 ATPase of myo­metrium. This inhibition is noncompetitive as to ATP and Mg2+. At the same time, this compound reduces the seeming enzymatic hydrolysis maximum rate of nucleoside triphosphate with respect to ATP and Mg2+.
With the help of computer design the interaction of mentioned calix[4]arene with myosin subfragment-1 of myometrium has been investigated. Several mechanisms involved in the calix[4]arene C-99 inhibition of myosin head ATPase were supposed and participation of hydrogen, hydrophobic and electrostatic interactions in these mechanisms was discussed.

Key words: calix[4]arenеs C-99, subfragment-1 of myosin, myometrium, smooth muscles, enzymic hydrolysis of АТР, kinetic properties of АТРаse, computer design, docking.

?The original article in Ukrainian is available for download in PDF format.