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Literature summary extracted from

  • Morrison, E.Y.S.A.; Mullings, K.
    Isolation of a branched chain alpha-keto acid dehydrogenase from rabbit liver (1983), Biochim. Biophys. Acta, 755, 225-228.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.2.4.4 thiamine diphosphate
-
Oryctolagus cuniculus

General Stability

EC Number General Stability Organism
1.2.4.4 maximum solubilization with minimum inactivation at 44 mM perchlorate carefully timed for 13 min Oryctolagus cuniculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.4.4 0.091
-
3-methyl-2-oxobutanoate
-
Oryctolagus cuniculus
1.2.4.4 0.2
-
4-methyl-2-oxopentanoate
-
Oryctolagus cuniculus
1.2.4.4 0.25
-
3-methyl-2-oxopentanoate
-
Oryctolagus cuniculus
1.2.4.4 0.29
-
2-oxoglutarate
-
Oryctolagus cuniculus

Organism

EC Number Organism UniProt Comment Textmining
1.2.4.4 Oryctolagus cuniculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.4.4 multienzyme complex Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.2.4.4 liver
-
Oryctolagus cuniculus
-

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 additional information
-
-
Oryctolagus cuniculus

Storage Stability

EC Number Storage Stability Organism
1.2.4.4 0°C, glycerol buffer, 20% loss of activity after 24 h Oryctolagus cuniculus

Substrates and Products (Substrate)

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

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.4.4 CoA
-
Oryctolagus cuniculus
1.2.4.4 NAD+
-
Oryctolagus cuniculus