Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Hawes, J.W.; Schnepf, R.J.; Jenkins, A.E.; Shimomura, Y.; Popov, K.M.; Harris, R.A.
    Roles of amino acid residues surrounding phosphorylation site 1 and branched-chain alpha-ketoacid dehydrogenase (BCKDH) in catalysis and phosphorylation site recognition by BCKDH kinase (1995), J. Biol. Chem., 270, 31071-31076.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.2.4.4 thiamine diphosphate
-
 Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
1.2.4.4 D296A inactive enzyme, no ability of component E1 apoenzyme to reconstitute with thiamine diphosphate Rattus norvegicus
1.2.4.4 H292A inactive enzyme, no binding of thiamine diphosphate Rattus norvegicus
1.2.4.4 R288A inactive enzyme, no detectable phosphorylation Rattus norvegicus
1.2.4.4 S293A 10fold increased Km-value for 3-methyl-2-oxobutanoate, 2.8fold increased Km-value for 4-methyl-2-oxopentanoate, no change in Km-value for thiamine diphosphate Rattus norvegicus
1.2.4.4 S293E no ability of the E1 apoenzyme to reconstitute with thiamine diphosphate Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.11.4 thiamine diphosphate inhibits phosphorylation of wild-type E1, mutant E1-S303A and mutant E1-D296A/S303A, but not phosphorylation of mutant E1-H292A Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.4.4 0.056
-
 3-methyl-2-oxobutanoate wild-type enzyme and mutant enzyme D297A Rattus norvegicus
1.2.4.4 0.058
-
 3-methyl-2-oxobutanoate mutant enzyme T294A Rattus norvegicus
1.2.4.4 0.059
-
 3-methyl-2-oxobutanoate mutant enzyme G290A and S298A Rattus norvegicus
1.2.4.4 0.062
-
 3-methyl-2-oxobutanoate mutant enzyme I289A and H291A Rattus norvegicus
1.2.4.4 0.064
-
 3-methyl-2-oxobutanoate mutant enzyme S295A Rattus norvegicus
1.2.4.4 0.568
-
 3-methyl-2-oxobutanoate mutant enzyme S293A Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
1.2.4.4 Rattus norvegicus
-
-
-
2.7.11.4 Rattus norvegicus
-
-
-

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
-
 Rattus norvegicus [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
-
 ?
1.2.4.4 4-methyl-2-oxopentanoate + NAD+ + CoA
-
 Rattus norvegicus 3-methylbutanoyl-CoA + CO2 + NADH
-
 ?
2.7.11.4 ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
-
 Rattus norvegicus ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
 ?
2.7.11.4 additional information R288A mutant of E1 is not phosphorylated by the enzyme Rattus norvegicus ?
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.4.4 CoA
-
 Rattus norvegicus
1.2.4.4 NAD+
-
 Rattus norvegicus