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Literature summary for 1.2.4.2 extracted from

  • Frank, R.A.; Price, A.J.; Northrop, F.D.; Perham, R.N.; Luisi, B.F.
    Crystal structure of the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex (2007), J. Mol. Biol., 368, 639-651.
    View publication on PubMed

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapour diffusion method with 12% (w/v) polyethylene glycol 4000, 50 mM sodium citrate (pH 5.6) Escherichia coli

Protein Variants

Protein Variants Comment Organism
H260A mutant has a dramatically reduced catalytic rate Escherichia coli
H298A mutant has a dramatically reduced catalytic rate Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
210000
-
2 * 105000, SDS-PAGE Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AFG3
-
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation, HiLoad Q-Sepharose column chromatography, and Superdex S200 gel filtration Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
-
Escherichia coli [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
?

Subunits

Subunits Comment Organism
homodimer x-ray crystallography Escherichia coli

Synonyms

Synonyms Comment Organism
2-oxoglutarate decarboxylase
-
Escherichia coli
E1 component of the 2-oxoglutarate dehydrogenase multienzyme complex
-
Escherichia coli
E1o component
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate dependent Escherichia coli