Literature summary for 1.2.4.1 extracted from

Arjunan, P.; Nemeria, N.; Brunskill, A.; Chandrasekhar, K.; Sax, M.; Yan, Y.; Jordan, F.; Guest, J.R.; Furey, W.
Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution (2002), Biochemistry, 41, 5213-5221.

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant pyruvate dehydrogenase multienzyme complex component E1, sitting drop vapor diffusion method, mixing of equal amounts of protein and precipitant solution of 0.006-0.01 ml, the latter containing 15-20% PEG2000 monomethyl ether, 10% propanol, 0.2% NaN3, and 60 mM HEPES, pH 7.1, 22°C, 2-5 weeks, native and selenomethionine crystals, X-ray diffraction structure determination and analysis at 1.85 A resolution	Escherichia coli

Crystallization (Comment)

Organism

purified recombinant pyruvate dehydrogenase multienzyme complex component E1, sitting drop vapor diffusion method, mixing of equal amounts of protein and precipitant solution of 0.006-0.01 ml, the latter containing 15-20% PEG2000 monomethyl ether, 10% propanol, 0.2% NaN3, and 60 mM HEPES, pH 7.1, 22°C, 2-5 weeks, native and selenomethionine crystals, X-ray diffraction structure determination and analysis at 1.85 A resolution

Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
99470	-	pyruvate dehydrogenase multienzyme complex component E1	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
pyruvate + CoA + NAD+	Escherichia coli	reaction of the citric acid or Krebs cycle	acetyl-CoA + CO2 + NADH	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0AFG8	pyruvate dehydrogenase multienzyme complex component E1	-

Reaction

Reaction	Comment	Organism	Reaction ID
pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2	active site interactions, reaction mechanism	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
additional information	reactions performed by the whole enzyme complex, overview	Escherichia coli	?	-	?
pyruvate + CoA + NAD+	-	Escherichia coli	acetyl-CoA + CO2 + NADH	-	?
pyruvate + CoA + NAD+	reaction of the citric acid or Krebs cycle	Escherichia coli	acetyl-CoA + CO2 + NADH	-	?

Subunits

Subunits	Comment	Organism
dimer	pyruvate dehydrogenase multienzyme complex component E1, 3 domains with alpha/beta fold, active sites are located at the interface between subunits, crystal structure	Escherichia coli

Synonyms

Synonyms	Comment	Organism
PDHC	-	Escherichia coli
pyruvate dehydrogenase multienzyme complex	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Escherichia coli
thiamine diphosphate	dependent on, 2 bound in the V-conformation in clefts between the 2 subunits, completely buried in the structure, binding structure	Escherichia coli