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Literature summary extracted from

  • Antonenkov, V.D.; Van Veldhoven, P.P.; Waelkens, E.; Mannaerts, G.P.
    Comparison of the stability and substrate specificity of purified peroxisomal 3-oxoacyl-CoA thiolases A and B from rat liver (1999), Biochim. Biophys. Acta, 1437, 136-141.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.16 CoA at concentrations above 0.025 mM Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.16 additional information
-
 additional information
-
 Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.16 peroxisome thiolase A from normal rat liver peroxisomes and thiolase B from livers of clofibrate-treated rats Rattus norvegicus 5777
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.16 41000
-
 2 * 41000, SDS-PAGE, thiolase B dimer dissociates into monomer with low activity during cold inactivation, thiolase A maintains its dimeric structure Rattus norvegicus
2.3.1.16 85000
-
 thiolase A and B, gel filtration Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.16 Rattus norvegicus
-
 male Wistar rats
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.16 thiolase A and B Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.16 liver
-
 Rattus norvegicus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.1.16 119
-
 thiolase A, substrate: 3-oxooctanoyl-CoA Rattus norvegicus
2.3.1.16 123
-
 thiolase B, substrate: 3-oxooctanoyl-CoA Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.16 CoA + 3-oxoacyl-CoA
-
 Rattus norvegicus acyl-CoA + acetyl-CoA
-
 ?
2.3.1.16 CoA + 3-oxooctanoyl-CoA
-
 Rattus norvegicus acetyl-CoA + hexanoyl-CoA
-
 ?
2.3.1.16 CoA + 3-oxopalmitoyl-CoA
-
 Rattus norvegicus acetyl-CoA + tetradecanoyl-CoA
-
 ?
2.3.1.16 CoA + acetoacetyl-CoA
-
 Rattus norvegicus acetyl-CoA + acetyl-CoA
-
 ?
2.3.1.16 additional information thiolase A and B possess virtually the same substrate specificity Rattus norvegicus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.16 dimer 2 * 41000, SDS-PAGE, thiolase B dimer dissociates into monomer with low activity during cold inactivation, thiolase A maintains its dimeric structure Rattus norvegicus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.3.1.16 additional information
-
 thiolase B exhibits cold-lability: loss of acitvity is more pronounced at 4°C than at 30°C, in the presence of KCl, thiolase A is stable under the same conditions, thiolase A exhibits higher stabiliy than thiolase B at 46°C, lability of the thiolase B might be compensated for by the formation of a more stable multienzyme complex Rattus norvegicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.16 additional information
-
 thiolase A pI: 8.45, thiolase B pI: 8.7 Rattus norvegicus