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Literature summary for 1.2.1.104 extracted from

  • Visser, J.; Kester, H.; Huigen, A.
    Purification and some properties of the pyruvate dehydrogenase complex of Bacillus subtilis (1980), FEMS Microbiol. Lett., 9, 227-232 .
No PubMed abstract available
Search for more literature for 1.2.1.104

Inhibitors

Inhibitors Comment Organism Structure
NADH
-
 Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.01
-
 NAD+ pH 7.0, 25°C Bacillus subtilis
0.017
-
 CoA S0.5 value, pH 7.0, 25°C Bacillus subtilis
0.02
-
 NAD+ pH 7.5, 25°C Bacillus subtilis
0.1
-
 pyruvate pH 7.5, 25°C Bacillus subtilis
0.2
-
 pyruvate pH 7.0, 25°C Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Bacillus subtilis 168
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.9
-
 pH 7.2, 25°C Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + CoA + NAD+
-
 Bacillus subtilis acetyl-CoA + CO2 + NADH
-
 ?
pyruvate + CoA + NAD+
-
 Bacillus subtilis 168 acetyl-CoA + CO2 + NADH
-
 ?

Subunits

Subunits Comment Organism
oligomer x * 58000-59000, i.e. transacetylase, x * 53 000, i.e. lipoamide dehydrogenase, x * 40000-41000, x * 37000, SDS-PAGE Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
-
 Bacillus subtilis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.12
-
 NADH pH 7.0, 25°C Bacillus subtilis