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Literature summary for 2.8.3.5 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
Search for more literature for 2.8.3.5

Activating Compound

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

Inhibitors

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
 Sus scrofa
-

Substrates and Products (Substrate)

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

Ki Value [mM]

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