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Literature summary for 3.1.2.2 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

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

Inhibitors

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

KM Value [mM]

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

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Sus scrofa 5829
-
mitochondrion
-
Sus scrofa 5739
-

Metals/Ions

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
300000
-
gel filtration Sus scrofa

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial, 44.3fold Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
cardiac muscle
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
28
-
assay at Sus scrofa

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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
47.5
-
5 min, in 0.02 M Tris-buffer, pH 8.0, 35-39% loss of activity Sus scrofa
50
-
5 min, in 0.02 M Tris-buffer, pH 8.0, 80% loss of activity Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
-
Sus scrofa
8
-
assay at Sus scrofa

Ki Value [mM]

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

pI Value

Organism Comment pI Value Maximum pI Value
Sus scrofa
-
-
4.5