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Literature summary for 1.2.4.1 extracted from

  • Hengeveld, A.F.; Schoustra, S.E.; Westphal, A.H.; De Kok, A.
    Pyruvate dehydrogenase from Azotobacter vinelandii: properties of the N-terminally truncated enzyme (1999), Eur. J. Biochem., 265, 1098-1107.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type pyruvate dehydrogenase and N-terminal deletion mutant E1pDelta48 in Escherichia coli Azotobacter vinelandii

Inhibitors

Inhibitors Comment Organism Structure
pyruvate
-
Azotobacter vinelandii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.024
-
lipoyl domain acyl group transfer reaction, recombinant pyruvate dehydrogenase with N-terminal deletion Azotobacter vinelandii
0.027
-
lipoyl domain acyl group transfer reaction, recombinant wild-type pyruvate dehydrogenase Azotobacter vinelandii

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + lipoyl domain
-
Azotobacter vinelandii acetylated lipoyl domain + CO2
-
r

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.9
-
lipoyl domain acyl group transfer reaction, recombinant wild-type pyruvate dehydrogenase Azotobacter vinelandii
1.1
-
lipoyl domain acyl group transfer reaction, recombinant pyruvate dehydrogenase with N-terminal deletion Azotobacter vinelandii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
wild-type pyruvate dehydrogenase and N-terminal deletion mutant Azotobacter vinelandii

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
31
-
pyruvate recombinant wild-type pyruvate dehydrogenase Azotobacter vinelandii
37
-
pyruvate recombinant pyruvate dehydrogenase with N-terminal deletion Azotobacter vinelandii