Proteolysis of acinetobacter citrate synthase by subtilisin.
Citrate synthase from Acinetobacter calcoaceticus was subjected to proteolysis with subtilisin. Although the enzyme proved relatively resistant to inactivation by this treatment, SDS-polyacrylamide gel electrophoresis clearly revealed breakdown of the citrate synthase to smaller fragments. The regulatory responses of the native enzyme to inhibition by NADH and re-activation by AMP were retained on proteolysis, indicating that the fragments bind tightly to each other and preserve the overall cooperative molecular interactions.
D000150:Acinetobacter / Q000201:enzymology*; D000249:Adenosine Monophosphate / Q000494:pharmacology; D002950:Citrate (si)-Synthase / Q000378:metabolism*; D004789:Enzyme Activation; D007700:Kinetics; D008970:Molecular Weight; D009243:NAD / Q000494:pharmacology; D007652:Oxo-Acid-Lyases / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis; D013381:Subtilisins / Q000378:metabolism*
D010446:Peptide Fragments; D009243:NAD; D000249:Adenosine Monophosphate; D002950:Citrate (si)-Synthase; D013381:Subtilisins; D007652:Oxo-Acid-Lyases