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Literature summary for 3.1.2.19 extracted from

  • Alexson, S.E.H.; Svensson, L.T.; Nedergaard, J.
    NADH-sensitive propionyl-CoA hydrolase in brown adipose tissue mitochondria of the rat (1989), Biochim. Biophys. Acta, 1005, 13-19.
    View publication on PubMed
Search for more literature for 3.1.2.19

Activating Compound

Activating Compound Comment Organism Structure
additional information cold acclimation induces enzyme activity Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
beta-NADH weak inhibition, 46% at 0.4 mM Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial matrix
-
 Rattus norvegicus 5759
-
mitochondrion
-
 Rattus norvegicus 5739
-
additional information submitochondrial and subcellular distribution Rattus norvegicus
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
100000
-
 about, gel filtration Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
 adult female Sprague-Dawley rats
-

Purification (Commentary)

Purification (Comment) Organism
partial Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
brown adipose tissue
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information broad substrate spectrum, substrate specificity Rattus norvegicus ?
-
 ?
additional information from the substrate specificity curves it is not possible to conclude whether the long-chain acyl-CoA hydrolase activity is due to the broad-spectrum enzyme or to a different long-chain acyl-CoA hydrolase Rattus norvegicus ?
-
 ?
nonanoyl-CoA + H2O best substrate Rattus norvegicus CoA + nonanoate
-
 ?