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Literature summary for 1.2.4.1 extracted from

  • Jung, H.I.; Perham, R.N.
    Prediction of the binding site on E1 in the assembly of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus (2003), FEBS Lett., 555, 405-410.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
modeling of the beta-subunit of the pyruvate decarboxylase component of the pyruvate dehydrogenase complex based on the crystal structures of the homologous 2-oxoisovalerate decarboxylase of Pseudomonas putida and Homo sapiens. The negatively charged side chain of Glu285 and the hydrophobic side chain of Phe324 are of particular importance in the interaction with the peripheral subunit-binding domain of the dihydrolipoyl acetyltransferase component of the complex Geobacillus stearothermophilus

Protein Variants

Protein Variants Comment Organism
D203A enzymatic activity similar to wild-type, mutant retains the normal capacity to bind the peripheral subunit-binding domain Geobacillus stearothermophilus
E251A enzymatic activity similar to wild-type, mutant retains the normal capacity to bind the peripheral subunit-binding domain Geobacillus stearothermophilus
E285A enzymatic activity similar to wild-type, mutant retains the normal capacity to bind the peripheral subunit-binding domain. Mutant subunit dissociates from the wild-type peripheral subunit-binding domain about 9fold faster than wild-type Geobacillus stearothermophilus
F324A enzymatic activity similar to wild-type, mutant retains the normal capacity to bind the peripheral subunit-binding domain. Mutant subunit dissociates from the wild-type peripheral subunit-binding domain about 13fold faster than wild-type Geobacillus stearothermophilus
K252A enzymatic activity similar to wild-type, mutant retains the normal capacity to bind the peripheral subunit-binding domain Geobacillus stearothermophilus
M322A enzymatic activity similar to wild-type, mutant retains the normal capacity to bind the peripheral subunit-binding domain Geobacillus stearothermophilus
N323A enzymatic activity similar to wild-type, mutant retains the normal capacity to bind the peripheral subunit-binding domain Geobacillus stearothermophilus
R255A enzymatic activity similar to wild-type, mutant retains the normal capacity to bind the peripheral subunit-binding domain Geobacillus stearothermophilus

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus P21874 beta subunit
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.17
-
wild-type, 30°C, pH not specified in the publication Geobacillus stearothermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + CoA + 2,6-dichlorophenolindophenol
-
Geobacillus stearothermophilus acetyl-CoA + CO2 + reduced 2,6-dichlorophenolindophenol
-
?

Synonyms

Synonyms Comment Organism
PdhB
-
Geobacillus stearothermophilus
pyruvate dehydrogenase E1 component subunit beta
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Geobacillus stearothermophilus