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 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 (3S)-citryl-CoA protect the transferase activity, while acetyl-CoA markedly enhances the rate of the inactivation. (3S)-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.
D000214:Acyl Coenzyme A / Q000378:metabolism; D000217:Acyltransferases / Q000037:antagonists & inhibitors; D001120:Arginine / Q000032:analysis*; D001665:Binding Sites; D002951:Citrates / Q000378:metabolism; D019343:Citric Acid; D006531:HEPES; D007709:Klebsiella / Q000201:enzymology*; D009097:Multienzyme Complexes / Q000032:analysis*; D007652:Oxo-Acid-Lyases / Q000032:analysis*; D014325:Tromethamine
D000214:Acyl Coenzyme A; D002951:Citrates; D009097:Multienzyme Complexes; D014325:Tromethamine; D019343:Citric Acid; C029890:citryl-coenzyme A; D001120:Arginine; D000217:Acyltransferases; D007652:Oxo-Acid-Lyases; C019909:citrate (pro-3S)-lyase; D006531:HEPES