Initial-velocity kinetics of succinoyl-coenzyme A-3-oxo acid coenzyme A-transferase from sheep kidney.
The initial-velocity kinetics of sheep kidney CoA-transferase are consistent with a Ping Pong mechanism. A KAcAc-CoA of 2.7 X 10(-5) M, KSucc-CoA of 1.6 X 10(-4) M, KSucc of 5.6 X 10(-3) M and KAcAc of 6.7 X 10(-5) M were determined by using a direct assay system that monitors the concentration of magnesium acetoacetyl-CoA enolate. However, product-inhibition kinetics of sheep kidney CoA-transferase are inconsistent with a Ping Pong mechanism. The possible involvement of separate binding sites for succinate and acetoacetate are discussed.
D000090:Acetoacetates / Q000378:metabolism; D000105:Acetyl Coenzyme A / Q000031:analogs & derivatives / Q000378:metabolism; D000214:Acyl Coenzyme A / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D015256:Coenzyme A-Transferases; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D008956:Models, Chemical; D012756:Sheep; D013466:Sulfurtransferases / Q000037:antagonists & inhibitors / Q000378:metabolism*
D000090:Acetoacetates; D000214:Acyl Coenzyme A; C010667:acetoacetyl CoA; C016635:acetoacetic acid; D000105:Acetyl Coenzyme A; C012046:succinyl-coenzyme A; D013466:Sulfurtransferases; D015256:Coenzyme A-Transferases; C021460:3-ketoacid CoA-transferase