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Literature summary extracted from

  • Isohashi, F.; Nakanishi, Y.; Matsunaga, T.; Sakamoto, Y.
    A cold-labile acetyl-coenzyme-A hydrolase from the supernatant fraction of rat liver. Reactivation and reconstitution of the active species from the inactive monomer (1984), Eur. J. Biochem., 142, 177-181.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.2.1 acetyl-CoA at time of rewarming 0.5 mM acetyl-CoA restores the activity about 50% Rattus norvegicus
3.1.2.1 albumin albumin enhances the reactivation of the monomeric form Rattus norvegicus
3.1.2.1 ATP at time of rewarming ATP greatly enhances the restoration of the activity, 2 mM ATP restores the enzyme activity about 70% Rattus norvegicus
3.1.2.1 diphosphate 450 mM pyrophosphate restores the activity about 80% at time of rewarming Rattus norvegicus
3.1.2.1 phosphate 920 mM phosphate restores the activity about 80% at time of rewarming Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.2.1 additional information extramitochondrial Rattus norvegicus
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.2.1 135000
-
-
Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
3.1.2.1 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.2.1
-
Rattus norvegicus

Renatured (Commentary)

EC Number Renatured (Comment) Organism
3.1.2.1 from cold inactivation Rattus norvegicus

Source Tissue

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

Subunits

EC Number Subunits Comment Organism
3.1.2.1 monomer sucrose density gradient centrifugation Rattus norvegicus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.2.1 37
-
warming at 37°C after cold exposure is optimal for reactivation Rattus norvegicus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.1.2.1 7 8 purified dimeric enzyme fairly stable in potassium phosphate buffer of pH 7.0-8.0 Rattus norvegicus