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Literature summary for 1.8.1.4 extracted from

  • Hodgson, J.A.; Lowe, P.N.; Perham, R.N.
    Wild-type and mutant forms of the pyruvate dehydrogenase multienzyme complex from Bacillus subtilis (1983), Biochem. J., 211, 463-472.
    View publication on PubMedView publication on EuropePMC

General Stability

General Stability Organism
stable to trypsin treatment Bacillus subtilis

Localization

Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
55000
-
2 * 55000, SDS-PAGE Bacillus subtilis
110000
-
gel filtration Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
from pyruvate dehydrogenase complex Bacillus subtilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
125
-
-
Bacillus subtilis

Storage Stability

Storage Stability Organism
-20°C, stable for several months Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dihydrolipoamide + NAD+
-
Bacillus subtilis lipoamide + NADH
-
?

Subunits

Subunits Comment Organism
dimer 2 * 55000, SDS-PAGE Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Bacillus subtilis