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Literature summary 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

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.11.4 ADP kinetics Oryctolagus cuniculus
2.7.11.4 Ca2+
-
Oryctolagus cuniculus
2.7.11.4 Dichloroacetate ATP slightly protects Oryctolagus cuniculus
2.7.11.4 additional information no inhibition by GTP Oryctolagus cuniculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.4.4 0.014
-
3-methyl-2-oxopentanoate
-
Oryctolagus cuniculus
1.2.4.4 0.015
-
4-methyl-2-oxopentanoate
-
Oryctolagus cuniculus
1.2.4.4 0.028
-
3-methyl-2-oxobutanoate
-
Oryctolagus cuniculus
1.2.4.4 0.715
-
pyruvate
-
Oryctolagus cuniculus
2.7.11.4 0.025
-
ATP pH 7.5, 30°C Oryctolagus cuniculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.11.4 EGTA 0.1 mM Oryctolagus cuniculus
2.7.11.4 Mg2+ requirement, actual substrate: MgATP2- Oryctolagus cuniculus
2.7.11.4 Mg2+ Km-value: 0.025 mM Oryctolagus cuniculus
2.7.11.4 additional information no activation by Ca2+ Oryctolagus cuniculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.4.4 additional information
-
MW of the multienzyme complex is 2000000 Da, determined by gel filtration Oryctolagus cuniculus
2.7.11.4 2000000
-
above 2000000, gel filtration Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.4.4 additional information Oryctolagus cuniculus regulation by phosphorylation-dephosphorylation ?
-
?
2.7.11.4 ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] Oryctolagus cuniculus phosphorylation inactivates EC 1.2.4.4 ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.4.4 multienzyme complex Oryctolagus cuniculus
2.7.11.4 alpha-ketoacid dehydrogenase complex Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.2.4.4 liver
-
Oryctolagus cuniculus
-
2.7.11.4 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 3.2
-
-
Oryctolagus cuniculus

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
-
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
-
?
1.2.4.4 additional information regulation by phosphorylation-dephosphorylation Oryctolagus cuniculus ?
-
?
1.2.4.4 pyruvate + NAD+ + CoA
-
Oryctolagus cuniculus acetyl-CoA + CO2 + NADH
-
?
2.7.11.4 ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] GTP cannot replace ATP Oryctolagus cuniculus ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
?
2.7.11.4 ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphorylates exclusively MW 47000 subunit of substrate Oryctolagus cuniculus ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
?
2.7.11.4 ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphorylation inactivates EC 1.2.4.4 Oryctolagus cuniculus ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.11.4 37
-
assay at Oryctolagus cuniculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.11.4 additional information
-
HEPES-potassium buffer promotes higher activity than imidazole-chloride, 4-morpholinopropanesulfonic acid-potassium or potassium phosphate buffer Oryctolagus cuniculus
2.7.11.4 7.1
-
-
Oryctolagus cuniculus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.7.11.4 6.5 8.3 about half-maximal activity at pH 6.5 and 8.3 Oryctolagus cuniculus

Cofactor

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

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.11.4 0.13
-
ADP pH 7.5, 30°C Oryctolagus cuniculus