Palmitoyl coenzyme A synthetase activation by uncomplexed ATP.
Uncomplexed ATP, ADP, alpha, beta-methylene ATP and adenosinetetraphosphate were shown to activate long chain fatty acyl-coenzyme A synthetase. The presence of uncomplexed nucleotides was shown: (1) to induce the palmitoyl-AMP-dependent palmitoyl-coenzyme A formation, (2) to activate the MgATP-dependent overall reaction and (3) to stabilize the synthetase against ageing denaturation. In all three cases the observed nucleotide activation was shown to be eliminated upon metal chelation.
D000227:Adenine Nucleotides / Q000494:pharmacology; D000244:Adenosine Diphosphate / Q000494:pharmacology; D000255:Adenosine Triphosphate / Q000031:analogs & derivatives / Q000494:pharmacology*; D002614:Chelating Agents / Q000494:pharmacology; D003066:Coenzyme A Ligases / Q000378:metabolism*; D004789:Enzyme Activation / Q000187:drug effects; D010169:Palmitic Acids
D000227:Adenine Nucleotides; D002614:Chelating Agents; D010169:Palmitic Acids; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D003066:Coenzyme A Ligases