REGULATORY PROPERTIES OF RAT-HEART AMP DEAMINASE

被引:31
作者
KALETHA, K
SKLADANOWSKI, A
机构
[1] Department of Biochemistry, Medical School, 80-211 Gdańsk
关键词
(Rat heart); Allosteric regulation; AMP deaminase; Nucleotide effect;
D O I
10.1016/0005-2744(79)90275-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The kinetic and regulatory properties of purified rat heart AMP deaminase were investigated. In the presence of 100 mM KCl, the enzyme exhibited a slightly sigmoid-shaped plot of reaction rate, vs. substrate concentration, which shifted to a more hyperbolic form when ATP, ADP or GTP were added. ATP was the most potent activator of the enzyme, whereas GTP at low (less than 0.25 mM) concentrations increased the enzyme activity. The activation effect was negligible at higher concentrations of GTP. The calculated value of K0.5 of approx. 3 mM for unactivated enzyme decreased to approx. 0.6 mM and 1.1 mM when 0.5 mM ATP or 1.5 mM ADP were present in the incubation mixture, respectively. The theoretical model (Monod J., Wyman, J. and Changeux, J.P. (1965) J. Mol. Biol. 12, 88-118) gave a partial explanation of these results. © 1979.
引用
收藏
页码:80 / 90
页数:11
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