3.5.4.6	malfunction	AMP deaminase 3 is mutated in one of the mutant clones resistant to anthrax lethal toxin-induced death, AMPD3 deficiency does not affect anthrax lethal toxin entering cells and the cleavage of mitogen-activated protein kinase kinase by lethal factor inside cells, but does impair a downstream event that is linked to cell death. Restoration of anthrax lethal toxin sensitivity with ectopic reconstitution of AMPD3 expression	720959	
3.5.4.6	metabolism	ATP depletion due to excessive degradation of adenine nucleotides by up-regulated AMP deaminase underlies ventricular stiffening during acute pressure overloading in Type 2 diabetes mellitus hearts	757444	
3.5.4.6	metabolism	high ammonia production in McArdle patients is not based on enzyme induction of AMP deaminase (AMPD) and adenylate kinase but possibly due to kinetic activation of the enzyme AMPD by increased concentration of the substrate AMP	757811	
3.5.4.6	metabolism	multicopy integrants of crt genes and co-expression of AMP deaminase improve lycopene production in Yarrowia lipolytica	757279	
3.5.4.6	metabolism	transgenic Solanum lycopersicum lines over expressing AMP deaminase under the control of a fruit-specific promoter show substantially enhanced levels of AMP deaminase expression in comparison to the wild-type control. Elevated AMP deaminase levels results in the reduced accumulation of glutamate and increased levels of the umami nucleotide GMP	757993	
3.5.4.6	physiological function	during pregnancy the isoform composition of human placental AMP-deaminase changes as an adaptation of enzyme to changing metabolic requirements of the growing fetus, overview	720641	
3.5.4.6	physiological function	requirement of AMPD3 in anthrax lethal toxin-induced cell death of RAW 264.7 cells	720959	
3.5.4.6	physiological function	the enzyme appears to play a role in regulation of relative concentrations of intracellular purine nucleotide pools, the stabilization of adenylate energy charge, and the deamination of amino acids via the purine nucleotide cycle	756164	
3.5.4.6	physiological function	the enzyme plays a role in supplying guanylates required for the intensive multiplication of thymocytes	734811