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Literature summary for 1.2.4.4 extracted from

  • Cook, K.G.; Yeaman, S.J.
    Purification, resolution, and reconstitution of branched-chain 2-keto acid dehydrogenase complex from bovine kidney (1988), Methods Enzymol., 166, 303-308.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
thiamine diphosphate
-
Bos taurus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35000
-
alpha2,beta2, 2 * 46000 + 2 * 35000, enzyme from kidney, SDS-PAGE Bos taurus
46000
-
alpha2,beta2, 2 * 46000 + 2 * 35000, enzyme from kidney, SDS-PAGE Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Bos taurus the activity of the multienzyme complex is regulated by reversible phosphorylation of the alpha-subunit of the E1 component, EC 1.2.4.4. ?
-
?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
Bos taurus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Bos taurus

Storage Stability

Storage Stability Organism
-20°C, after concentration and dialysis into 50 mM Tris-HCl buffer, 0.1 mM EDTA, 0.1 mM EGTA, 1 mM benzamidine, 1 mM PMSF, 1 mM DTT, pH 7.3, multienzyme complex is stable for at least 2 months Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the activity of the multienzyme complex is regulated by reversible phosphorylation of the alpha-subunit of the E1 component, EC 1.2.4.4. Bos taurus ?
-
?

Subunits

Subunits Comment Organism
tetramer alpha2,beta2, 2 * 46000 + 2 * 35000, enzyme from kidney, SDS-PAGE Bos taurus

Cofactor

Cofactor Comment Organism Structure
CoA
-
Bos taurus
NAD+
-
Bos taurus