Characteristics of aspartate deamination by the puring nucleotide cycle in the cytosol fraction of rat liver.
1. The component reactions of the puring nucleotide cycle were studied in cytosol extracts of rat liver. 2. AMP deaminase was strongly activated by ATP and analogues of ATP. 3. IMP was converted into ATP by a system requiring the presence of aspartate, GTP and a nucleoside triphosphate-regenerating system. 4. Under appropriate conditions, NH3 was produced from aspartate. 5. From the rates at which these reactions occur it is concluded that the purine nucleotide cycle may have sufficient activity to be a major pathway of amino acid deamination in liver.
D000659:AMP Deaminase / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism / Q000494:pharmacology; D000818:Animals; D001224:Aspartic Acid / Q000378:metabolism* / Q000494:pharmacology; D003600:Cytosol / Q000187:drug effects / Q000378:metabolism; D003641:Deamination; D004789:Enzyme Activation / Q000187:drug effects; D005260:Female; D006160:Guanosine Triphosphate / Q000494:pharmacology; D008099:Liver / Q000187:drug effects / Q000378:metabolism*; D008274:Magnesium / Q000494:pharmacology; D008930:Mitochondria, Liver / Q000187:drug effects / Q000378:metabolism; D011685:Purine Nucleotides / Q000378:metabolism*; D051381:Rats
D011685:Purine Nucleotides; D001224:Aspartic Acid; D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate; D000659:AMP Deaminase; D008274:Magnesium