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Literature summary for 2.3.1.12 extracted from

  • Arjunan, P.; Wang, J.; Nemeria, N.S.; Reynolds, S.; Brown, I.; Chandrasekhar, K.; Calero, G.; Jordan, F.; Furey, W.
    Novel binding motif and new flexibility revealed by structural analyses of a pyruvate dehydrogenase-dihydrolipoyl acetyltransferase subcomplex from the Escherichia coli pyruvate dehydrogenase multienzyme complex (2014), J. Biol. Chem., 289, 30161-30176.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli AG1 cells Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
E1p-E2p didomain subcomplex, sitting drop vapor diffusion method, using 20% (w/v) PEG 3350, 0.2% (w/v) NaN3, and 0.2 M ammonium tartrate dibasic buffer (pH 6.35) Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
65959
-
 x * 65959, calculated from amino acid sequence Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine Escherichia coli
-
 CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P06959
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine
-
 Escherichia coli CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine
-
 ?

Subunits

Subunits Comment Organism
? x * 65959, calculated from amino acid sequence Escherichia coli

Synonyms

Synonyms Comment Organism
dihydrolipoyl acetyltransferase
-
 Escherichia coli
pyruvate dehydrogenase complex component E2p
-
 Escherichia coli