FUNCTIONAL-ROLE AND PROPERTIES OF AMP-DEAMINASE

Authors
Citation
Vi. Lushchak, FUNCTIONAL-ROLE AND PROPERTIES OF AMP-DEAMINASE, Biochemistry, 61(2), 1996, pp. 143-154
Citations number
59
Categorie Soggetti
Biology
Journal title
ISSN journal
00062979
Volume
61
Issue
2
Year of publication
1996
Pages
143 - 154
Database
ISI
SICI code
0006-2979(1996)61:2<143:FAPOA>2.0.ZU;2-S
Abstract
AMP-deaminase (AMPDA) catalyzes the deamination of AMP with the format ion of IMP and ammonia, Being an integral enzyme of the purine nucleot ide cycle (PNC), AMPDA participates in deamination of amino acids and provides their incorporation into carbohydrate metabolism, fumarate be ing one of the PNC products. Since AMPDA competes with 5'-nucleotidase for AMP, participating in the regulation of the level of the physiolo gically important product of purine nucleotide metabolism adenosine, i nvestigation of the properties of the enzyme may be important in deter mining the physiological state of an organism under normal conditions, under different environmental conditions, and in some pathologies. In this review information on molecular properties and isoforms, the par ticipation of AMPDA in the operation of the PNC in animal tissues, cod ing genes, and regulation of properties of the enzyme by different eff ecters including regulation by reversible phosphorylation and binding with myofibrils and myosin is summarized. Some attention is given to t he possible correlation between deficiency of AMPDA activity and some neuromuscular disease.