Direct deamination of AMP, ADP, ATP and NADH by non-specific adenylate deaminase in the foot muscle of the snail Helix pomatia.
Homogeneous adenylate deaminase from snail foot muscle deaminated 5'-AMP, 5'-ADP, 5'-ATP and NADH with similar velocity and affinity to all substrates. At millimolar concentration NAD+ was also deaminated to a comparable extent, but NADP+, NADPH and FAD were not substrates for the snail enzyme. The amount of deaminase activity per g of fresh tissue is 5-10 times greater than in the muscle of any other species studied. The activity of the snail deaminase is regulated by pH, KCl and buffer concentrations, and Pi; however, regulation seems to be very poor in comparison with that of muscle deaminases from other species, specific to 5'-AMP. Snail enzyme appears as the first animal deaminase so far described that has such characteristics. It offers also some opportunities as an analytical tool as a consequence of its very high affinity toward adenylates.
D000659:AMP Deaminase / Q000302:isolation & purification / Q000378:metabolism*; D000227:Adenine Nucleotides / Q000378:metabolism*; D000244:Adenosine Diphosphate / Q000378:metabolism; D000249:Adenosine Monophosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002854:Chromatography, Paper; D006372:Helix, Snails / Q000201:enzymology*; D007700:Kinetics; D009132:Muscles / Q000201:enzymology*; D009243:NAD / Q000378:metabolism*; D009709:Nucleotide Deaminases / Q000378:metabolism*; D013379:Substrate Specificity
D000227:Adenine Nucleotides; D009243:NAD; D000249:Adenosine Monophosphate; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D009709:Nucleotide Deaminases; D000659:AMP Deaminase