Literature summary extracted from

Sharp, J.A.; Edwards, M.R.
Initial-velocity kinetics of succinoyl-coenzyme A-3-oxo acid coenzyme A-transferase from sheep kidney (1983), Biochem. J., 213, 179-185.

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
2.8.3.5	acetoacetyl-CoA	product inhibition, kinetics	Ovis aries
2.8.3.5	succinate	kinetics; product inhibition	Ovis aries
2.8.3.5	succinyl-CoA	product inhibition	Ovis aries

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
2.8.3.5	additional information	-	additional information	-	Ovis aries

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.8.3.5	Ovis aries	-	-	-

Reaction

EC Number	Reaction	Comment	Organism	Reaction ID
2.8.3.5	succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA	mechanism	Ovis aries	a

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
2.8.3.5	kidney	-	Ovis aries	-

Specific Activity [micromol/min/mg]

EC Number	Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
2.8.3.5	180	-	-	Ovis aries

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2.8.3.5	succinyl-CoA + acetoacetate	-	Ovis aries	succinate + acetoacetyl-CoA	-	r

Temperature Optimum [°C]

EC Number	Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
2.8.3.5	30	-	assay at	Ovis aries

pH Optimum

EC Number	pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
2.8.3.5	8.1	-	assay at	Ovis aries

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Release 2023.1 (January 2023)