Mechanism of enzymic acetylation of des-acetyl citrate lyase.
A new enzyme, acetate:SH-[acyl-carrier-protein] enzyme ligase (AMP), has been purified about 30-fold from cell-free extracts of Klebsiella aerogenes. The enzyme, in the presence of acetate and ATP, catalyzes the acetylation of enzymically inactive des-acetyl citrate lyase to enzymically active citrate lyase (EC 4.1.3.6). Acetate and ATP could be replaced by acetyl adenylate. Acetyl-CoA can act as acetyl donor in this activation only if trace amounts of adenine nucleotides and auxiliary enzymes are present. These allow formation of acetyl adenylate in acetate- and ATP-generating reactions.
D000085:Acetates; D000105:Acetyl Coenzyme A; D000107:Acetylation; D000249:Adenosine Monophosphate; D001151:Arsenic; D002352:Carrier Proteins; D002951:Citrates; D007700:Kinetics; D007709:Klebsiella / Q000201:enzymology*; D008025:Ligases / Q000302:isolation & purification; D008722:Methods; D007652:Oxo-Acid-Lyases; D010770:Phosphotransferases; D013438:Sulfhydryl Compounds
D000085:Acetates; D002352:Carrier Proteins; D002951:Citrates; D013438:Sulfhydryl Compounds; D000249:Adenosine Monophosphate; D000105:Acetyl Coenzyme A; D010770:Phosphotransferases; D007652:Oxo-Acid-Lyases; D008025:Ligases; D001151:Arsenic