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COA3 — CS

Text-mined interactions from Literome

Wlassics et al., Biochemistry 1989 : The data indicate that citrate synthase stabilizes the ionized form of Ac(= S)CoA by 5 kcal/mol relative to the un-ionized form, that the ionized dithioester is on the reaction pathway, and that below pH 8.3 the slow carbon-carbon bond forming reaction is responsible for the 10 ( 6 ) decrease in Vmax caused by substituting sulfur for oxygen in the thioester carbonyl
Fahien et al., J Biol Chem 1988 : The potential ability of the aminotransferase to transfer directly alpha-ketoglutarate to the alpha-ketoglutarate dehydrogenase complex in this multienzyme system plus the ability of succinyl-CoA , a product of this transfer, to inhibit citrate synthase could play a role in preventing alpha-ketoglutarate and citrate from accumulating in high levels
Löhlein-Werhahn et al., Biol Chem Hoppe Seyler 1988 : Studies on the citryl-CoA dependent inhibition of citrate-synthase with source variants from baker 's yeast, Escherichia coli and Sulfolobus solfataricus
Mita et al., J Exp Zool 1983 : Crude citrate synthase from sea urchin unfertilized and fertilized eggs was inhibited by palmitoyl-CoA , though malate dehydrogenase was not inhibited
Fahien et al., Arch Biochem Biophys 1983 : Furthermore, glutamate dehydrogenase can compete with citrate synthase for palmitoyl-CoA and thus can prevent palmitoyl-CoA from enhancing interactions between citrate synthase and either malate dehydrogenase or the aminotransferase
Simpson et al., J Neurochem 1981 : Oxaloacetate, [ 14C ] malate and endogenous citrate synthase were found not to interfere significantly with lyase estimations, but NADH was required in the reaction mixture to inhibit acetyl-CoA hydrolase activity