Partial purification of rat liver cytoplasmic acetyl-CoA synthetase; characterization of some properties.
Rat liver cytoplasmic acetyl-CoA synthetase was partially purified (purification factor = 23, yield = 30%). The apparent Kms for acetate, coenzyme A, ATP and MgCl2 were determined and found to be 52.5 microM, 50.5 microM, 570 microM and 1.5 mM, respectively. The partially-purified enzyme showed a low affinity for short-chain carbon substrates other than acetate. The properties of the partially-purified enzyme were compared with those of enzymes from other sources.
D000106:Acetate-CoA Ligase / Q000302:isolation & purification* / Q000378:metabolism; D000818:Animals; D003066:Coenzyme A Ligases / Q000302:isolation & purification*; D003600:Cytosol / Q000201:enzymology; D005260:Female; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D051381:Rats; D011919:Rats, Inbred Strains; D013379:Substrate Specificity
D003066:Coenzyme A Ligases; D000106:Acetate-CoA Ligase