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Literature summary for 2.3.1.9 extracted from

  • Huth, W.; Jonas, R.; Wunderlich, I.; Seubert, W.
    On the mechanism of ketogenesis and its control. Purification, kinetic mechanism and regulation of different forms of mitochondrial acetoacetyl-CoA thiolases from ox liver (1975), Eur. J. Biochem., 59, 475-489.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
acetoacetyl-CoA
-
Bos taurus
CoA both directions Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.01
-
acetoacetyl-CoA isoenzyme A, thiolysis Bos taurus
0.025
-
CoA isoenzyme A, thiolysis Bos taurus
0.032
-
acetoacetyl-CoA isoenzyme B, thiolysis Bos taurus
0.08
-
acetyl-CoA enzyme B Bos taurus
0.091
-
acetyl-CoA isoenzyme A, synthesis Bos taurus
0.091
-
acetyl-CoA isoenzyme B, synthesis Bos taurus
0.154
-
CoA isoenzyme B, thiolysis Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
CoA + acetoacetyl-CoA Bos taurus
-
acetyl-CoA + acetyl-CoA
-
?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
2 forms: A and B
-

Purification (Commentary)

Purification (Comment) Organism
isoenzymes A and B, ammonium sulfate, cellulose phosphate column, crystallization Bos taurus

Reaction

Reaction Comment Organism Reaction ID
2 acetyl-CoA = CoA + acetoacetyl-CoA mechanism Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Bos taurus
-

Storage Stability

Storage Stability Organism
-10°C, less than 0.2 mg/ml protein, 50 mM Tris, pH 7.2, 0.5 mM dithiothreitol, 8 d, 60-70% loss of activity Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CoA + acetoacetyl-CoA
-
Bos taurus acetyl-CoA + acetyl-CoA
-
?
CoA + acetoacetyl-CoA rate of synthesis is 0.31 and 0.08 the rate of thiolysis for isoenzyme A and B, respectively Bos taurus acetyl-CoA + acetyl-CoA
-
r

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.1 8.4 isoenzyme A and B, acetoacetyl-CoA synthesis Bos taurus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0016
-
acetoacetyl-CoA isoenzyme A Bos taurus
0.05
-
CoA
-
Bos taurus