In situ studies on AMP deaminase as a control system of the adenylate energy charge in yeasts.
The role of AMP deaminase reaction in the stabilization of the adenylate energy charge was investigated using permeabilized yeast cells. The addition of Pi or Zn2+, which inhibits AMP deaminase, remarkably retarded the depletion of total adenylate pool and the recovery of the adenylate energy charge. Polyamine, an activator of the enzyme, decreased total adenylates, resulting in the enhanced recovery of the energy charge in situ. AMP deaminase can act as a regulatory enzyme in the system that stabilizes the adenylate energy charge in yeast cells under the conditions of severe metabolic stress.
D000659:AMP Deaminase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000244:Adenosine Diphosphate / Q000378:metabolism; D000249:Adenosine Monophosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D004734:Energy Metabolism; D009709:Nucleotide Deaminases / Q000378:metabolism*; D010710:Phosphates / Q000494:pharmacology; D011073:Polyamines / Q000494:pharmacology; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D015032:Zinc / Q000494:pharmacology
D010710:Phosphates; D011073:Polyamines; D000249:Adenosine Monophosphate; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D009709:Nucleotide Deaminases; D000659:AMP Deaminase; D015032:Zinc