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Literature summary extracted from

  • Parker, P.J.; Randle, P.J.
    Partial purification and properties of branched-chain 2-oxo acid dehydrogenase of ox liver (1978), Biochem. J., 171, 751-757.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.2.4.4 thiamine diphosphate Km: 0.00035 mM in the reaction with 4-methyl-2-oxopentanoate Bos taurus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.4.4 3-methyl-2-oxobutanoate substrate inhibition Bos taurus
1.2.4.4 3-methylbutanoyl-CoA competitive with CoA Bos taurus
1.2.4.4 4-methyl-2-oxopentanoate substrate inhibition Bos taurus
1.2.4.4 D-3-methyl-2-oxopentanoate substrate inhibition Bos taurus
1.2.4.4 L-3-Methyl-2-oxopentanoate substrate inhibition Bos taurus
1.2.4.4 NADH competitive with NAD+ Bos taurus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.4.4 0.0087
-
4-methyl-2-oxopentanoate
-
Bos taurus
1.2.4.4 0.0156
-
3-methyl-2-oxobutanoate
-
Bos taurus
1.2.4.4 0.0172
-
DL-3-methyl-2-oxopentanoate
-
Bos taurus

Localization

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.4.4 Mg2+ required Bos taurus
1.2.4.4 Mg2+ Km: 0.0042 mM in the reaction with 4-methyl-2-oxopentanoate Bos taurus

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.4.4 partial Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.2.4.4 liver
-
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 D-3-methyl-2-oxopentanoate and L-3-methyl-2-oxopentanoate 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 Km: 0.0071 mM in the reaction with 4-methyl-2-oxopentanoate, Km: 0.009 mM in the reaction with 3-methyl-2-oxobutanoate, Km: 0.007 in the reaction with DL-3-methyl-2-oxopentanoate Bos taurus
1.2.4.4 NAD+ Km: 0.109 mM in the reaction with 4-methyl-2-oxopentanoate, Km: 0.126 mM in the reaction with 3-methyl-2-oxobutanoate, Km: 0.101 mM in the reaction with DL-3-methyl-2-oxobutanoate Bos taurus