Lushak V I
Natural Sciences Dept., Vasyl Stefanyk Precarpathian University, Ivano-Frankivsk, Ukraine.
Ukr Biokhim Zh (1999). 2000 Jan-Feb;72(1):9-20.
AMP-deaminase (AMPD) catalyzes the irreversible hydrolysis of AMP to IMP and ammonia. Being the integral enzyme of purine nucleotide cycle, AMPD participates in deamination of amino acids and their involvement into carbohydrate metabolism. This enzyme competes with 5'-nuclease for AMP it is indirectly involved in regulation of adenosine level. The role of AMPD may be supported also by the correlation between its activity and several neuromuscular and immunologic pathologies. The information on the izoforms, gene expression both in the normal and pathological states is given. Activity of AMPD is regulated by the substrate availability, adenylate pool, GTP, product of catalysed reaction IMP, ++inorganical phosphate, etc. Currently the growing scope of data is displaying the possible role of reversible phosphorylation and binding to cellular elements in regulation of the properties of AMPD under change of physiological state of organism.
AMP脱氨酶(AMPD)催化AMP不可逆地水解为IMP和氨。作为嘌呤核苷酸循环的组成酶,AMPD参与氨基酸的脱氨基作用及其在碳水化合物代谢中的参与。这种酶与5'-核酸酶竞争AMP,它间接参与腺苷水平的调节。AMPD的活性与几种神经肌肉和免疫病理学之间的相关性也可能支持其作用。文中给出了正常和病理状态下同工型、基因表达的信息。AMPD的活性受底物可用性、腺苷酸池、GTP、催化反应产物IMP、无机磷酸盐等调节。目前,越来越多的数据显示,在机体生理状态变化时,可逆磷酸化和与细胞成分结合在调节AMPD特性方面可能发挥的作用。