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Regulation of human erythrocyte amp deaminase ec 3.5.4.6 by atp and 2 3 bis phospho glycerate


, : Regulation of human erythrocyte amp deaminase ec 3.5.4.6 by atp and 2 3 bis phospho glycerate. Agricultural and Biological Chemistry 40(9): 1797-1803

AMP deaminase (EC 3.5.4.6) is a key enzyme in the adenine nucleotide metabolism of human erythrocytes. ATP activates the enzyme, while 2,3-bisphosphoglycerate inhibits it. Complexes of Mg and these organic phosphate compounds are not effectors of AMP deaminase. The AMP deaminase activity in the physiological range of AMP was calculated from AMP-saturation curves which were drawn by measuring the activity under simulated intracellular conditions. Since human erythrocytes have a high level of AMP deaminase, the enzyme activity must be repressed to a low level, which accounts for the half-life of adenine nucleotides in the erythrocyte. Although it is evident from the experimental results that 2,3-bisphosphoglycerate plays an important role in the repression of the activity of this enzyme, the in vivo rate of turnover of adenine nucleotides cannot be explained by the inhibitory effect of 2,3-bisphosphoglycerate alone.

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Related references

Miller K.B.; Hass L.F., 1978: Coulombic and catalytic properties of the polymorphic forms of human erythrocyte phospho glycerate mutase and bis phospho glycerate synthase. Federation Proceedings 37(6): 1796

Momsen, G.; Vestergaard-Bogind, B., 1978: Human erythrocyte 2 3 di phospho glycerate metabolism influence of 1 3 di phospho glycerate and ortho phosphate in vitro studies at low ph with computer simulations. The kinetics of 2,3-diphosphoglycerate (2,3-DPG) net breakdown were examined in intact human erythrocytes incubated at pH 7.00 and 37.degree. C. The concentrations of 2,3-DPG, 1,3-diphosphoglycerate (1,3-DPG), 3-phosphoglycerate, ATP, Pi [orthopho...

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