Purification and properties of rat liver AMP deaminase

Characteristics of aspartate deamination by the puring nucleotide cycle in the cytosol fraction of rat liver

“…These results are consistent with those of other authors, who have shown that AMP deaminases isolated from rat liver (Smith & Kizer, 1969) and from calf brain (Setlow & Lowenstein, 1968) Fig. 3 shows that the production of NH3 from AMP was stimulated by both adenylyl-imidodiphosphate and adenylyl-(fiy-methylene)diphosphonate.…”

“…The supernatant was then centrifuged at 38000g for 30min to remove the remaining mitochondria and microsomal fraction. The use of the preparation medium described above ensured minimum microsomal contamination and provided conditions for maximum activity of AMP deaminase, which is activated by alkali-metal cations (Smith & Kizer, 1969).…”

Catabolism of Adenosine 5'-Monophosphate by Extracts of the Marine Bacterium Beneckea natriegens

“…Mammalian AMP deaminases are activated by ATP, yet inactivated by increases in energy charge in the 0.6 to 0.9 region (Burger & Lowenstein, 1967;Smith & Kizer, 1969;Drummond & Yamamoto, 197r ;Chapman & Atkinson, 1973). On the other hand, several AMP nucleotidases are inhibited by ATP (Burger & Lowenstein, 1967;Woods et al, 1970;Drummond & Yamamoto, 1971).…”

Purification and characterization of developmentally regulated AMP deaminase from Dictyostelium discoideum

“…In addition, ATP acts to lower the apparent K, of the enzyme without changing the maximal velocity as described for enzyme preparations from both liver and Ehrlich ascites tumor cells, in which AMP deaminase has been demonstrated to have a central role in the maintainance of the adenylate energy charge [7, 111. Inhibition by GTP has been demonstrated in other systems [32,37,411 possibly serving to control the potential conversion of adenylated to guanylated nucleotides through the intermediate IMP [44]. In addition, ATP acts to lower the apparent K, of the enzyme without changing the maximal velocity as described for enzyme preparations from both liver and Ehrlich ascites tumor cells, in which AMP deaminase has been demonstrated to have a central role in the maintainance of the adenylate energy charge [7, 111. Inhibition by GTP has been demonstrated in other systems [32,37,411 possibly serving to control the potential conversion of adenylated to guanylated nucleotides through the intermediate IMP [44].…”

“…The substrate-specific enzyme has several properties like those of other AMP deaminases including an apparent K, in the millimolar range, activation by ATP, and inhibition by both GTP and inorganic phosphate. In addition, ATP acts to lower the apparent K, of the enzyme without changing the maximal velocity as described for enzyme preparations from both liver and Ehrlich ascites tumor cells, in which AMP deaminase has been demonstrated to have a central role in the maintainance of the adenylate energy charge [7, 111. Inhibition by GTP has been demonstrated in other systems [32,37,411 possibly serving to control the potential conversion of adenylated to guanylated nucleotides through the intermediate IMP [44]. Inhibition by 1 m M EDTA suggests the possible presence of a metal in the enzyme.…”