The presence of essential arginine residues at the active sites of citrate lyase complex from Klebsiella aerogenes

The acyl-transferase and acyl-lyase activities of $\text{Klebsiella aerogenes}$ citrate lyase complex are inactivated by the arginine specific reagents phenylglyoxal and 2,3-butanedione, the former reagent being the more potent inhibitor. Citrate and (3$\text{S}$)-citryl-CoA protect the transferase activity, while acetyl-CoA markedly enhances the rate of the inactivation. (3$\text{S}$)-Citryl-CoA protects the lyase subunit in the complex from inactivation. The kinetics of inactivation suggest the involvement of a single arginine residue at each of the active sites of the transferase and of the lyase subunits.