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Literature summary for 1.2.4.1 extracted from

  • Fries, M.; Stott, K.M.; Reynolds, S.; Perham, R.N.
    Distinct modes of recognition of the lipoyl domain as substrate by the E1 and E3 components of the pyruvate dehydrogenase multienzyme complex (2006), J. Mol. Biol., 366, 132-139.
    View publication on PubMed
Search for more literature for 1.2.4.1

Cloned(Commentary)

Cloned (Comment) Organism
-
 Geobacillus stearothermophilus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
152000
-
-
 Geobacillus stearothermophilus

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Geobacillus stearothermophilus

Reaction

Reaction Comment Organism Reaction ID
pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2 substrate channelling in the multienzyme complex rests on the recognition of the lipoyl domain by enzyme. Cofactor thiamine diphosphate and substrate pyruvate have distinct effects on enzyme/lipoyl domain interaction. conformational freedom is allowed by the linker in the movement of the lipoyl domain between active sites Geobacillus stearothermophilus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information binds to the di-domain (lipoyl domain + linker + peripheral subunit binding domain) of the dihydrolipoyl acetyltransferase (E2) component for acetylation Geobacillus stearothermophilus ?
-
 ?
pyruvate + CoA + NAD+
-
 Geobacillus stearothermophilus acetyl-CoA + CO2 + NADH
-
 ?

Subunits

Subunits Comment Organism
heterotetramer x-ray crystallography Geobacillus stearothermophilus
More substrate channelling in the multienzyme complex rests on the recognition of the lipoyl domain by enzyme. Cofactor thiamine diphosphate and substrate pyruvate have distinct effects on enzyme/lipoyl domain interaction. conformational freedom is allowed by the linker in the movement of the lipoyl domain between active sites Geobacillus stearothermophilus

Synonyms

Synonyms Comment Organism
E1 component of the pyruvate dehydrogenase multienzyme complex
-
 Geobacillus stearothermophilus
thiamine diphosphate-dependent 2-oxo acid decarboxylase
-
 Geobacillus stearothermophilus

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate dependent Geobacillus stearothermophilus