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Literature summary for 1.2.1.25 extracted from

  • Namba, Y.; Yoshizawa, K.; Ejima, A.; Hayashi, T.; Kaneda, T.
    Coenzyme A- and nicotinamide adenine dinucleotide-dependent branched chain alpha-keto acid dehydrogenase. I. Purification and properties of the enzyme from Bacillus subtilis (1969), J. Biol. Chem., 244, 4437-4447.
    View publication on PubMed
Search for more literature for 1.2.1.25

Inhibitors

Inhibitors Comment Organism Structure
2-oxoisopentanoate competitive Bacillus subtilis
iodoacetate
-
 Bacillus subtilis
L-2-Oxo-3-methylpentanoate competitive Bacillus subtilis
NEM
-
 Bacillus subtilis
PCMB
-
 Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.11
-
 CoA
-
 Bacillus subtilis
1.66
-
 L-alpha-keto-beta-methylvalerate
-
 Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-methyl-2-oxobutanoate + CoA + NAD+ specific for the L-isomer Bacillus subtilis 2-methylpropanoyl-CoA + CO2 + NADH
-
 ?
4-methyl-2-oxopentanoate + CoA + NAD+
-
 Bacillus subtilis 3-methyl-butanoyl-CoA + CO2 + NADH
-
 ?
L-alpha-keto-beta-methylvalerate + CoA + NAD+
-
 Bacillus subtilis ?
-
 r

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Bacillus subtilis

pH Range

pH Minimum pH Maximum Comment Organism
6 7.5 pH 6.0: about 25% of maximal activity, pH 7.5: about 45% of maximal activity Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
CoA required Bacillus subtilis
additional information CoA and NAD+ can be replaced by potassium ferricyanide but the activity is much lower Bacillus subtilis
additional information enzyme probably identical with EC 1.2.4.4 Bacillus subtilis
NAD+ required Bacillus subtilis