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Literature summary for 2.3.1.12 extracted from

  • Wang, J.; Nemeria, N.S.; Chandrasekhar, K.; Kumaran, S.; Arjunan, P.; Reynolds, S.; Calero, G.; Brukh, R.; Kakalis, L.; Furey, W.; Jordan, F.
    Structure and function of the catalytic domain of the dihydrolipoyl acetyltransferase component in Escherichia coli pyruvate dehydrogenase complex (2014), J. Biol. Chem., 289, 15215-15230.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
His9-tagged catalytic domain, hanging drop vapor diffusion method, using 0.2 M potassium thiocyanate and 20% (w/v) polyethylene glycol 3350 Escherichia coli

Protein Variants

Protein Variants Comment Organism
H602C inactive Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
30028
-
x * 30028, catalytic domain, calculated from amino acid sequence Escherichia coli
30030
-
x * 30030, catalytic domain, FT mass spectrometry 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
-
r

Organism

Organism UniProt Comment Textmining
Escherichia coli P06959
-
-

Purification (Commentary)

Purification (Comment) Organism
nickel affinity resin column chromatography, Superdex G75 gel filtration, and G3000SW TSK gel filtration 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
-
r
CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine
-
Escherichia coli acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine
-
r

Subunits

Subunits Comment Organism
? x * 30028, catalytic domain, calculated from amino acid sequence Escherichia coli
? x * 30030, catalytic domain, FT mass spectrometry Escherichia coli
trimer x-ray crystallography Escherichia coli

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate
-
Escherichia coli