REGULATION OF CYTOSOL 5'-NUCLEOTIDASE BY ADENYLATE ENERGY-CHARGE
REGULATION OF CYTOSOL 5'-NUCLEOTIDASE BY ADENYLATE ENERGY-CHARGE
复制标题
DOI:
10.1016/0005-2744(81)90268-0
复制
发表时间:
1981-01-01
期刊:
影响因子:
--
通讯作者:
ITOH, R
中科院分区:
文献类型:
--
作者:
ITOH, R
In the physiological range of the adenylate energy charge in liver (0.7-0.9), the rate of AMP-hydrolysis catalyzed by rat liver cytosol 5''-nucleotidase (5''-ribonucleotide phosphohydrolase, EC 3.1.3.5) increased sharply with decreasing energy charge. A decrease in the concentration of Pi caused marked acceleration of the AMP-hydrolyzing activity over the physiological range of adenylate energy charge. These responses seem to serve to protect the cells against a metabolic stress which could result from sudden utilization of ATP by removal of AMP. The AMP-hydrolyzing activity of this enzyme decreased sharply as the size of the adenine nucleotide pool decreased in the physiological range. This effect may be a self-limiting response to prevent excess depletion of the pool. IMP-hydrolyzing activity of this enzyme increased with increasing adenylate energy charge. But no marked response to its variation within the physiological range was observed. On the basis of the data obtained in this study, the IMP-hydrolyzing activity of the cytosol 5''-nucleotidase in rat liver cells seems to be comparable to that of AMP deaminase reaction, but the AMP-hydrolyzing activity was estimated to be less than 10% of AMP deaminase reaction at energy charge value of about 0.7. This strongly suggests that the AMP .fwdarw. IMP .fwdarw. inosine pathway is more significant than the AMP .fwdarw. adenosine .fwdarw. inosine pathway in rat liver.