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Literature summary for 1.2.1.104 extracted from

  • Hiromasa, Y.; Aso, Y.; Yamashita, S.
    Purification of pyruvate dehydrogenase complex from an extreme thermophile, Bacillus caldolyticus, and its thermal stability (1993), Biosci. Biotechnol. Biochem., 57, 1062-1066 .
    View publication on PubMed
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Organism

Organism UniProt Comment Textmining
[Bacillus] caldolyticus
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-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.4
-
 pH 7.0, 30°C [Bacillus] caldolyticus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + CoA + NAD+
-
 [Bacillus] caldolyticus acetyl-CoA + CO2 + NADH
-
 ?

Subunits

Subunits Comment Organism
multimer x * 39800, x * 41700, 53700, and 57500, i.e. pyruvate decarboxylase subunits (E1), lipoate acetyltransferase (E2), and lipoamide dehydrogenase (E3), respectively, SDS-PAGE [Bacillus] caldolyticus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
65
-
 30 min, 50% loss of component E1 activity [Bacillus] caldolyticus
85
-
 30 min, 50% loss of component E3 activity [Bacillus] caldolyticus

pH Stability

pH Stability pH Stability Maximum Comment Organism
4.5 11.3 E3 component [Bacillus] caldolyticus
5.7 10.2 E1 component [Bacillus] caldolyticus