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Literature summary for 2.3.1.12 extracted from

  • Ali, S.T.; Guest, J.R.
    Isolation and characterization of lipoylated and unlipoylated domains of the E2p subunit of the pyruvate dehydrogenase complex of Escherichia coli (1990), Biochem. J., 271, 139-145.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Protein Variants

Protein Variants Comment Organism
K244Q unlipoylatable domain Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 molecular weight of lipolyl domains Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dihydrolipoamide + acetyl-CoA Escherichia coli
-
 S-acetyldihydrolipoamide + CoA
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
lipoprotein 3 lipoyl domains Escherichia coli

Purification (Commentary)

Purification (Comment) Organism
isolation of lipoyl domains Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dihydrolipoamide + acetyl-CoA
-
 Escherichia coli S-acetyldihydrolipoamide + CoA
-
 ?

Subunits

Subunits Comment Organism
polymer domain structure Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70
-
 1 h stable, isolated lipoyl domains Escherichia coli

pH Stability

pH Stability pH Stability Maximum Comment Organism
3 11 isolated E. coli lipoyl domains stay soluble in this range Escherichia coli