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Literature summary extracted from

  • Danner, D.J.; Heffelfinger, S.C.
    Isolation of branched-chain alpha-keto acid dehydrogenase as active complex from bovine liver (1988), Methods Enzymol., 166, 298-302.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.2.4.4 thiamine diphosphate
-
Bos taurus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.2.4.4 mitochondrion
-
Bos taurus 5739
-

Organism

EC Number Organism UniProt Comment Textmining
1.2.4.4 Bos taurus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.4.4 multienzyme complex Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.2.4.4 liver
-
Bos taurus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.2.4.4 5.5
-
multienzyme complex Bos taurus

Storage Stability

EC Number Storage Stability Organism
1.2.4.4 -70°C, multienzyme complex is stable for at least 2 years Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.4.4 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
-
Bos taurus [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
-
?
1.2.4.4 3-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
-
Bos taurus [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2
-
?
1.2.4.4 4-methyl-2-oxopentanoate + NAD+ + CoA
-
Bos taurus 3-methylbutanoyl-CoA + CO2 + NADH
-
?

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.4.4 CoA
-
Bos taurus
1.2.4.4 NAD+
-
Bos taurus