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Literature summary extracted from

  • Lee, K.Y.; Schulz, H.
    Isolation, properties, and regulation of a mitochondrial acyl coenzyme A thioesterase from pig heart (1979), J. Biol. Chem., 254, 4516-4523.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.2.2 bovine serum albumin activation Sus scrofa
3.1.2.2 bovine serum albumin only with long-chain acyl-CoA as substrate Sus scrofa
3.1.2.20 bovine serum albumin activation Sus scrofa
3.1.2.20 bovine serum albumin only with long-chain acyl-CoA as substrate Sus scrofa

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.2.2 ADP
-
 Sus scrofa
3.1.2.2 AMP acetyl-CoA as substrate Sus scrofa
3.1.2.2 ATP competitive to acetyl-CoA Sus scrofa
3.1.2.2 citrate
-
 Sus scrofa
3.1.2.2 CoA-S-S-CoA competitive to acetyl-CoA; i.e. oxidized CoA, additive with NADH, kinetics Sus scrofa
3.1.2.2 CoASH product inhibition, acetyl-CoA as substrate, kinetics Sus scrofa
3.1.2.2 Cu2+
-
 Sus scrofa
3.1.2.2 diethyldicarbonate
-
 Sus scrofa
3.1.2.2 diisopropylfluorophosphate
-
 Sus scrofa
3.1.2.2 GTP acetyl-CoA as substrate Sus scrofa
3.1.2.2 hexadecanoyl-CoA substrate inhibition Sus scrofa
3.1.2.2 malate weak Sus scrofa
3.1.2.2 Mn2+
-
 Sus scrofa
3.1.2.2 additional information no inhibition by EDTA, Mg2+, Fe2+, NAD+, NADP+, NADPH, glutamate, 2-oxoglutarate, pyruvate, alanine, asparagine, succinate; no inhibition by NEM Sus scrofa
3.1.2.2 NADH additive with oxidized CoA, noncompetitive Sus scrofa
3.1.2.2 Ni2+
-
 Sus scrofa
3.1.2.2 PMSF no inhibition Sus scrofa
3.1.2.2 Zn2+
-
 Sus scrofa
3.1.2.20 ADP
-
 Sus scrofa
3.1.2.20 AMP acetyl-CoA as substrate Sus scrofa
3.1.2.20 ATP competitive to acetyl-CoA Sus scrofa
3.1.2.20 citrate
-
 Sus scrofa
3.1.2.20 CoA-S-S-CoA competitive to acetyl-CoA; i.e. oxidized CoA, additive with NADH, kinetics Sus scrofa
3.1.2.20 CoASH product inhibition, acetyl-CoA as substrate, kinetics Sus scrofa
3.1.2.20 Cu2+
-
 Sus scrofa
3.1.2.20 diethyldicarbonate
-
 Sus scrofa
3.1.2.20 diisopropylfluorophosphate
-
 Sus scrofa
3.1.2.20 GTP acetyl-CoA as substrate Sus scrofa
3.1.2.20 hexadecanoyl-CoA substrate inhibition Sus scrofa
3.1.2.20 malate weak Sus scrofa
3.1.2.20 Mn2+
-
 Sus scrofa
3.1.2.20 additional information no inhibition by EDTA, Mg2+, Fe2+, NAD+, NADP+, NADPH, glutamate, 2-oxoglutarate, pyruvate, alanine, asparagine, succinate; no inhibition by NEM Sus scrofa
3.1.2.20 NADH additive with oxidized CoA, noncompetitive Sus scrofa
3.1.2.20 Ni2+
-
 Sus scrofa
3.1.2.20 PMSF no inhibition Sus scrofa
3.1.2.20 Zn2+
-
 Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.2.2 0.048
-
 acetyl-CoA
-
 Sus scrofa
3.1.2.2 0.048
-
 acetoacetyl-CoA
-
 Sus scrofa
3.1.2.2 0.048
-
 succinyl-CoA
-
 Sus scrofa
3.1.2.2 0.048
-
 n-butyryl-CoA
-
 Sus scrofa
3.1.2.2 0.048
-
 n-decanoyl-CoA
-
 Sus scrofa
3.1.2.20 0.048
-
 acetyl-CoA
-
 Sus scrofa
3.1.2.20 0.048
-
 acetoacetyl-CoA
-
 Sus scrofa
3.1.2.20 0.048
-
 succinyl-CoA
-
 Sus scrofa
3.1.2.20 0.048
-
 n-butyryl-CoA
-
 Sus scrofa
3.1.2.20 0.048
-
 n-decanoyl-CoA
-
 Sus scrofa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.2.2 cytosol
-
 Sus scrofa 5829
-
3.1.2.2 mitochondrion
-
 Sus scrofa 5739
-
3.1.2.20 cytosol
-
 Sus scrofa 5829
-
3.1.2.20 mitochondrion
-
 Sus scrofa 5739
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.2.2 Ca2+ activation, 0.1-2 mM Sus scrofa
3.1.2.20 Ca2+ activation, 0.1-2 mM Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.2.2 300000
-
 gel filtration Sus scrofa
3.1.2.20 300000
-
 gel filtration Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.2.2 hexadecanoyl-CoA + H2O Sus scrofa reaction at 60% the rate of acetoacetyl-CoA hydrolysis CoA + hexadecanoate
-
 ?
3.1.2.20 hexadecanoyl-CoA + H2O Sus scrofa reaction at 60% the rate of acetoacetyl-CoA hydrolysis CoA + hexadecanoate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.2.2 Sus scrofa
-
-
-
3.1.2.20 Sus scrofa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.2.2 partial, 44.3fold Sus scrofa
3.1.2.20 partial, 44.3fold Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.2.2 cardiac muscle
-
 Sus scrofa
-
3.1.2.20 cardiac muscle
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.2.2 2.7
-
 partially purified enzyme Sus scrofa
3.1.2.20 2.7
-
 partially purified enzyme Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.2.2 3-hydroxybutyryl-CoA + H2O reaction at 4.3% the rate of acetoacetyl-CoA hydrolysis Sus scrofa CoA + 3-hydroxybutanoate
-
 ?
3.1.2.2 3-hydroxydecanoyl-CoA + H2O reaction at 1.4% the rate of acetoacetyl-CoA hydrolysis Sus scrofa CoA + 3-hydroxydecanoate
-
 ?
3.1.2.2 3-oxodecanoyl-CoA + H2O
-
 Sus scrofa CoA + 3-oxodecanoate
-
 ?
3.1.2.2 acetoacetyl-CoA + H2O best substrate Sus scrofa CoA + acetoacetate
-
 ?
3.1.2.2 acetyl-CoA + H2O reaction at 33% the rate of acetoacetyl-CoA hydrolysis Sus scrofa CoA + acetate
-
 ?
3.1.2.2 acyl-CoA + H2O
-
 Sus scrofa CoA + a carboxylate
-
 ?
3.1.2.2 crotonyl-CoA + H2O i.e. [trans]-2-butenoyl-CoA, reaction at 9.4% the rate of acetoacetyl-CoA hydrolysis Sus scrofa CoA + crotonate
-
 ?
3.1.2.2 decanoyl-CoA + H2O reaction at 89% the rate of acetoacetyl-CoA hydrolysis Sus scrofa CoA + decanoate
-
 ?
3.1.2.2 hexadecanoyl-CoA + H2O reaction at 60% the rate of acetoacetyl-CoA hydrolysis Sus scrofa CoA + hexadecanoate
-
 ?
3.1.2.2 additional information no substrates are malonyl-CoA, acetoacetyl glutathione, acetoacetyl N-acetylcysteamine or acetoacetyl pantetheine Sus scrofa ?
-
 ?
3.1.2.2 n-butyryl-CoA + H2O reaction at 81% the rate of acetoacetyl-CoA hydrolysis Sus scrofa CoA + n-butanoate
-
 ?
3.1.2.2 oleoyl-CoA + H2O i.e. [cis]-9-octadecenoyl-CoA, reaction at 40% the rate of acetoacetyl-CoA hydrolysis Sus scrofa CoA + oleate
-
 ?
3.1.2.2 succinyl-CoA + H2O reaction at 33% the rate of acetoacetyl-CoA hydrolysis Sus scrofa CoA + succinate
-
 ?
3.1.2.20 3-hydroxybutyryl-CoA + H2O reaction at 4.3% the rate of acetoacetyl-CoA hydrolysis Sus scrofa CoA + 3-hydroxybutanoate
-
 ?
3.1.2.20 3-hydroxydecanoyl-CoA + H2O reaction at 1.4% the rate of acetoacetyl-CoA hydrolysis Sus scrofa CoA + 3-hydroxydecanoate
-
 ?
3.1.2.20 3-oxodecanoyl-CoA + H2O
-
 Sus scrofa CoA + 3-oxodecanoate
-
 ?
3.1.2.20 acetoacetyl-CoA + H2O best substrate Sus scrofa CoA + acetoacetate
-
 ?
3.1.2.20 acetyl-CoA + H2O reaction at 33% the rate of acetoacetyl-CoA hydrolysis Sus scrofa CoA + acetate
-
 ?
3.1.2.20 acyl-CoA + H2O
-
 Sus scrofa CoA + a carboxylate
-
 ?
3.1.2.20 crotonyl-CoA + H2O i.e. [trans]-2-butenoyl-CoA, reaction at 9.4% the rate of acetoacetyl-CoA hydrolysis Sus scrofa CoA + crotonate
-
 ?
3.1.2.20 decanoyl-CoA + H2O reaction at 89% the rate of acetoacetyl-CoA hydrolysis Sus scrofa CoA + decanoate
-
 ?
3.1.2.20 hexadecanoyl-CoA + H2O reaction at 60% the rate of acetoacetyl-CoA hydrolysis Sus scrofa CoA + hexadecanoate
-
 ?
3.1.2.20 additional information no substrates are malonyl-CoA, acetoacetyl glutathione, acetoacetyl N-acetylcysteamine or acetoacetyl pantetheine Sus scrofa ?
-
 ?
3.1.2.20 n-butyryl-CoA + H2O reaction at 81% the rate of acetoacetyl-CoA hydrolysis Sus scrofa CoA + n-butanoate
-
 ?
3.1.2.20 oleoyl-CoA + H2O i.e. [cis]-9-octadecenoyl-CoA, reaction at 40% the rate of acetoacetyl-CoA hydrolysis Sus scrofa CoA + oleate
-
 ?
3.1.2.20 succinyl-CoA + H2O reaction at 33% the rate of acetoacetyl-CoA hydrolysis Sus scrofa CoA + succinate
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.2.2 28
-
 assay at Sus scrofa
3.1.2.20 28
-
 assay at Sus scrofa

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.2.2 45
-
 5 min, in 0.02 M Tris-buffer, pH 8.0, 15-19% loss of activity, 10 min, 35-38% loss of activity Sus scrofa
3.1.2.2 47.5
-
 5 min, in 0.02 M Tris-buffer, pH 8.0, 35-39% loss of activity Sus scrofa
3.1.2.2 50
-
 5 min, in 0.02 M Tris-buffer, pH 8.0, 80% loss of activity Sus scrofa
3.1.2.20 45
-
 5 min, in 0.02 M Tris-buffer, pH 8.0, 15-19% loss of activity, 10 min, 35-38% loss of activity Sus scrofa
3.1.2.20 47.5
-
 5 min, in 0.02 M Tris-buffer, pH 8.0, 35-39% loss of activity Sus scrofa
3.1.2.20 50
-
 5 min, in 0.02 M Tris-buffer, pH 8.0, 80% loss of activity Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.2.2 additional information
-
-
 Sus scrofa
3.1.2.2 8
-
 assay at Sus scrofa
3.1.2.20 additional information
-
-
 Sus scrofa
3.1.2.20 8
-
 assay at Sus scrofa

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.1.2.2 0.008
-
 CoA pH 8.0, 28°C, versus acetyl-CoA Sus scrofa
3.1.2.2 0.052
-
 ATP pH 8.0, 28°C, versus acetyl-CoA Sus scrofa
3.1.2.2 0.053
-
 CoA-S-S-CoA pH 8.0, 28°C, versus acetyl-CoA Sus scrofa
3.1.2.2 0.085
-
 CoA-S-S-CoA pH 8.0, 28°C, with palmitoyl-CoA as substrate Sus scrofa
3.1.2.2 0.5
-
 NADH pH 8.0, 28°C, with palmitoyl-CoA as substrate Sus scrofa
3.1.2.20 0.008
-
 CoA pH 8.0, 28°C, versus acetyl-CoA Sus scrofa
3.1.2.20 0.052
-
 ATP pH 8.0, 28°C, versus acetyl-CoA Sus scrofa
3.1.2.20 0.053
-
 CoA-S-S-CoA pH 8.0, 28°C, versus acetyl-CoA Sus scrofa
3.1.2.20 0.085
-
 CoA-S-S-CoA pH 8.0, 28°C, with palmitoyl-CoA as substrate Sus scrofa
3.1.2.20 0.5
-
 NADH pH 8.0, 28°C, with palmitoyl-CoA as substrate Sus scrofa

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.1.2.2 Sus scrofa
-
-
 4.5
3.1.2.20 Sus scrofa
-
-
 4.5