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Literature summary extracted from

  • Whitty, A.; Fierke, C.A.; Jencks, W.P.
    Role of binding energy with coenzyme A in catalysis by 3-oxoacid coenzyme A transferase (1995), Biochemistry, 34, 11678-11689.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.8.3.5 Sodium sulfate increases the activity at 1 mM Sus scrofa

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.8.3.5 ADP
-
 Sus scrofa
2.8.3.5 coenzyme A
-
 Sus scrofa
2.8.3.5 desulfo-CoA competitive inhibition with respect to acetoacetyl-CoA Sus scrofa
2.8.3.5 desulfopantetheine competitive inhibition with respect to acetoacetyl-CoA Sus scrofa
2.8.3.5 N-acetylaletheine reacts with the enzyme thiol ester E-CoA to form a catalytically inactive enzyme Sus scrofa
2.8.3.5 N-acetylcysteamine reacts with the enzyme thiol ester E-CoA to form a catalytically inactive enzyme Sus scrofa
2.8.3.5 pantothenol
-
 Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.8.3.5 0.0002
-
 acetoacetate pH 8.1, 25°C, presence of sodium sulfate Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
2.8.3.5 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.8.3.5 heart
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.3.5 succinyl-CoA + acetoacetate
-
 Sus scrofa succinate + acetoacetyl-CoA
-
 ?

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.8.3.5 1.7
-
 CoA pH 8.1, 25° Sus scrofa
2.8.3.5 2.7
-
 desulfo-CoA pH 8.1, 25° Sus scrofa
2.8.3.5 45
-
 ADP pH 8.1, 25° Sus scrofa
2.8.3.5 110
-
 desulfopoantetheine pH 8.1, 25° Sus scrofa
2.8.3.5 120
-
 pantothenol pH 8.1, 25° Sus scrofa