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Literature summary for 5.1.3.8 extracted from

  • Maru, I.; Ohta, Y.; Murata, K.; Tsukada, Y.
    Molecular cloning and identification of N-acetyl-D-glucosamine 2-epimerase from porcine kidney as a renin-binding protein (1996), J. Biol. Chem., 271, 16294-16299.
    View publication on PubMed
Search for more literature for 5.1.3.8

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3
-
 N-acetyl-D-mannosamine
-
 Sus scrofa
7.4
-
 N-acetyl-D-glucosamine
-
 Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45000
-
 2 * 45000, SDS-PAGE Sus scrofa
93000
-
 sedimentation equilibrium Sus scrofa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Sus scrofa involved in biosynthesis of N-acetylneuraminic acid ?
-
 ?

Organism

Organism UniProt Comment Textmining
Sus scrofa P17560
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
 Sus scrofa
-

Storage Stability

Storage Stability Organism
-20°C, 20 mM potassium phosphate buffer, pH 7.6, 1.0 mM EDTA, 0.05% 2-mercaptoethanol, 5.0% sucrose, stable for at least 6 months Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information involved in biosynthesis of N-acetylneuraminic acid Sus scrofa ?
-
 ?
N-acetyl-D-glucosamine
-
 Sus scrofa N-acetyl-D-mannosamine
-
 r
N-acetyl-D-mannosamine
-
 Sus scrofa N-acetyl-D-glucosamine
-
 r
N-Acyl-D-glucosamine r Sus scrofa N-Acyl-D-mannosamine
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 45000, SDS-PAGE Sus scrofa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
47
-
-
 Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
-
 Sus scrofa

Cofactor

Cofactor Comment Organism Structure
ATP not essential for reaction, but 20fold enhancement of activity, Km: 0.018 mM Sus scrofa
dATP not essential for reaction, but 20fold enhancement of activity Sus scrofa