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Literature summary for 5.4.2.3 extracted from

  • Cheng, P.W.; Carlson, D.M.
    Mechanism of phosphoacetylglucosamine mutase (1979), J. Biol. Chem., 254, 8353-8357.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
glucose 1,6-diphosphate required for reaction with glucose 1-phosphate, Km: 0.025 mM Sus scrofa
N-Acetylglucosamine 1,6-diphosphate required for reaction with N-acetylglucosamine 1-phosphate Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0237
-
N-acetylglucosamine 1-phosphate
-
Sus scrofa
0.658
-
glucose 1-phosphate
-
Sus scrofa

Metals/Ions

Metals/Ions Comment Organism Structure
phosphate covalently linked to the enzyme. The phosphate-protein linkage is stable in mild acid, at 50 C for up to 2 h. However phosphate is completely released under mild alkaline conditions at 50 C within 1 h Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
59000
-
gel filtration Sus scrofa
64000
-
1 * 64000, SDS-PAGE Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Reaction

Reaction Comment Organism Reaction ID
N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate ping-pong mechanism Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
submandibular gland
-
Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Glucose 1-phosphate in presence of glucose 1,6-diphosphate Sus scrofa Glucose 6-phosphate
-
?
N-Acetyl-D-glucosamine 1-phosphate in presence of N-acetylglucosamine 1,6-diphosphate Sus scrofa N-Acetyl-D-glucosamine 6-phosphate
-
?

Subunits

Subunits Comment Organism
monomer 1 * 64000, SDS-PAGE Sus scrofa

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
enzyme is present in two forms of different heat stability Sus scrofa