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Literature summary for 1.2.4.4 extracted from

  • Paxton, R.; Harris, R.A.
    Isolation of rabbit liver branched chain alpha-ketoacid dehydrogenase and regulation by phosphorylation (1982), J. Biol. Chem., 257, 14433-14439.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
thiamine diphosphate
-
Oryctolagus cuniculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.014
-
3-methyl-2-oxopentanoate
-
Oryctolagus cuniculus
0.015
-
4-methyl-2-oxopentanoate
-
Oryctolagus cuniculus
0.028
-
3-methyl-2-oxobutanoate
-
Oryctolagus cuniculus
0.715
-
pyruvate
-
Oryctolagus cuniculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
MW of the multienzyme complex is 2000000 Da, determined by gel filtration Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Oryctolagus cuniculus regulation by phosphorylation-dephosphorylation ?
-
?

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
multienzyme complex Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2
-
-
Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
-
Oryctolagus cuniculus [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
-
?
3-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
-
Oryctolagus cuniculus [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2
-
?
4-methyl-2-oxopentanoate + NAD+ + CoA
-
Oryctolagus cuniculus 3-methylbutanoyl-CoA + CO2 + NADH
-
?
additional information regulation by phosphorylation-dephosphorylation Oryctolagus cuniculus ?
-
?
pyruvate + NAD+ + CoA
-
Oryctolagus cuniculus acetyl-CoA + CO2 + NADH
-
?

Cofactor

Cofactor Comment Organism Structure
CoA
-
Oryctolagus cuniculus
NAD+
-
Oryctolagus cuniculus