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.