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Literature summary for 1.2.4.4 extracted from

  • Zhao, Y.; Hawes, J.; Popov, K.M.; Jaskiewicz, J.; Shimomura, Y.; Crabb, D.W.; Harris, R.A.
    Site-directed mutagenesis of phosphorylation sites of the branched chain alpha-ketoacid dehydrogenase complex (1994), J. Biol. Chem., 269, 18583-18587.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
thiamine diphosphate
-
Rattus norvegicus

Cloned(Commentary)

Cloned (Comment) Organism
-
Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
S293A mutation in the alpha-subunit, nearly 12fold increase in Km-value, no inactivation after incubation with ATP Rattus norvegicus
S293E mutation in the alpha-subunit, completely inactive enzyme Rattus norvegicus
S293E/S303E mutation in the alpha-subunit, no activity Rattus norvegicus
S303A mutation in the alpha-subunit, no effect upon enzyme activity Rattus norvegicus
S303E mutation in the alpha-subunit, no effect upon enzyme activity Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
ATP time-dependent inactivation of wild-type enzyme and mutant proteins S303A, S303E, with mutation in the alpha-subunit Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
160000
-
wild-type enzyme and mutant enzymes S293E, S293A, S303A and S293E/S303E, gel filtration Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
-
Rattus norvegicus [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
-
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Cofactor

Cofactor Comment Organism Structure
CoA
-
Rattus norvegicus
NAD+
-
Rattus norvegicus