Rat-liver fatty-acid-synthesizing complex.
Under conditions favoring lipogenesis, a high-molecular-weight species of acetyl-CoA carboxylase was isolated that did not co-sediment with the in vitro polymerized enzyme. Assays for ATP-citrate lyase, acetyl-CoA carboxylase, and fatty acid synthetase indicated that all three enzymes were associated together as a high-molecular-weight complex and that under low-lipogenic conditions the level of these enzymes decreased. Phosphorylation of the isolated complex shifted it toward a lower molecular weight.
D001275:ATP Citrate (pro-S)-Lyase / Q000302:isolation & purification / Q000378:metabolism; D000103:Acetyl-CoA Carboxylase / Q000302:isolation & purification* / Q000378:metabolism; D000818:Animals; D064429:Fatty Acid Synthases / Q000302:isolation & purification* / Q000378:metabolism; D008025:Ligases / Q000302:isolation & purification*; D008099:Liver / Q000201:enzymology*; D008297:Male; D008970:Molecular Weight; D010766:Phosphorylation; D051381:Rats
D064429:Fatty Acid Synthases; D001275:ATP Citrate (pro-S)-Lyase; D008025:Ligases; D000103:Acetyl-CoA Carboxylase