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Literature summary for 4.1.2.4 extracted from

  • Valentin-Hansen, P.; Boetius, F.; Hammer-Jespersen, K.; Svendsen, I.
    The primary structure of Escherichia coli K12 2-deoxyribose 5-phosphate aldolase (1982), Eur. J. Biochem., 125, 561-566.
    View publication on PubMed
Search for more literature for 4.1.2.4

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
27200
-
 1 * 27200, the enzyme exists as monomer and as dimer, SDS-PAGE Escherichia coli
27200
-
 2 * 27200, the enzyme exists as monomer and as dimer, SDS-PAGE Escherichia coli
27737
-
 1 * 27737, enzyme exists as monomer and as dimer, calculation from DNA sequence Escherichia coli
27737
-
 2 * 27737, enzyme exists as monomer and as dimer, calculation from DNA sequence Escherichia coli
33000
-
 monomeric form, gel filtration in 10 mM Tris/HCl containing 50 mM KCl and 2 mM EDTA Escherichia coli
50000
-
 dimeric form, gel filtration in 50 mM potassium phosphate buffer, pH 7.5 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 K 12
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde Schiff base intermediate Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-deoxy-D-ribose 5-phosphate
-
 Escherichia coli D-glyceraldehyde 3-phosphate + acetaldehyde
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 27200, the enzyme exists as monomer and as dimer, SDS-PAGE Escherichia coli
dimer 2 * 27737, enzyme exists as monomer and as dimer, calculation from DNA sequence Escherichia coli
monomer 1 * 27200, the enzyme exists as monomer and as dimer, SDS-PAGE Escherichia coli
monomer 1 * 27737, enzyme exists as monomer and as dimer, calculation from DNA sequence Escherichia coli