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Literature summary for 1.2.4.1 extracted from

  • Hengeveld, A.F.; Westphal, A.H.; de Kok, A.
    Expression and characterisation of the homodimeric E1 component of the Azotobacter vinelandii pyruvate dehydrogenase complex (1997), Eur. J. Biochem., 250, 260-268 .
    View publication on PubMed
Search for more literature for 1.2.4.1

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Azotobacter vinelandii

General Stability

General Stability Organism
enzyme is stable in high ionic strength buffers Azotobacter vinelandii
enzyme is unstable in low ionic strength buffers and in the presence of organic solvents Azotobacter vinelandii

Inhibitors

Inhibitors Comment Organism Structure
acetyl-CoA product inhibition, acetyl CoA interacts directly with the E1p component Azotobacter vinelandii
CoA allosteric inhibition Azotobacter vinelandii

Organic Solvent Stability

Organic Solvent Comment Organism
Ethanol 1-2%, rapid inactivation Azotobacter vinelandii

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii V9H1F5
-
-

Storage Stability

Storage Stability Organism
4°C, recombinant enzyme in saturated ammonium sulfate, pH 7.0, stabel for 6 months Azotobacter vinelandii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information non-complex-bound E1p shows the same cooperativity as found for complex-bound E1p in the pyruvate dehydrogenase complex, EC 1.2.1.104. A Hill coefficient of 1.2-1.6 is calculated for non-complex bound E1p Azotobacter vinelandii ?
-
-
pyruvate + CoA + ferricyanide
-
 Azotobacter vinelandii acetyl-CoA + CO2 + ferrocyanide
-
 ?

Synonyms

Synonyms Comment Organism
PdhE
-
 Azotobacter vinelandii

pH Stability

pH Stability pH Stability Maximum Comment Organism
9.5
-
 15 min, 60% residual activity Azotobacter vinelandii