Summary: ATP:citrate lyase has been purified some 20-fold from the oleaginous yeast, CBS 1809. The enzyme, which is labile, was stabilized by the addition of ATP and citrate to extraction buffers. Michaelis-Menten kinetics were exhibited towards ATP and citrate. The molecular weight of the enzyme was determined to be approximately 510000. There was a specific requirement for ATP for activity. No activity was observed in the absence of Mg, although Co and Mn could partially substitute for Mg. ADP inhibited activity (50% inhibition at 1 mM), as did long-chain fatty acyl-CoA esters (50% inhibition with 4μm oleoyl-CoA). The possibility of control of ATP:citrate lyase activity by fluctuations in the prevailing energy charge or by changes in the intracellular concentrations of long-chain fatty acyl-CoA esters is discussed.


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