Chicken heart citrate synthase: some mechanism studies.
Some mechanism studies on chicken and pig citrate synthase are described. Gibacron Blue F3GA apparently binds into both the oxaloacetate and the acetyl-CoA subsites of the enzyme. Protection by ligands against urea-induced denaturation indicates that several di(tri)-carboxylic acids bind into the oxaloacetate subsite, whereas ATP, but not Mg2+ ATP, binds into the acetyl-CoA subsite. Oxaloacetate, citrate and D-malate induce a transconformation in the enzyme, whereas alpha-ketoglutarate, L-malate and succinate do not.
D000818:Animals; D001665:Binding Sites; D002645:Chickens; D002950:Citrate (si)-Synthase / Q000378:metabolism*; D007700:Kinetics; D009206:Myocardium / Q000201:enzymology*; D007652:Oxo-Acid-Lyases / Q000378:metabolism*; D011487:Protein Conformation / Q000187:drug effects; D011489:Protein Denaturation / Q000187:drug effects; D013045:Species Specificity; D013552:Swine; D014227:Triazines / Q000494:pharmacology
D014227:Triazines; C012842:Cibacron Blue F 3GA; D002950:Citrate (si)-Synthase; D007652:Oxo-Acid-Lyases