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Literature summary for 5.1.3.8 extracted from

  • Ghosh, S.; Roseman, S.
    N-Acetylglucosamine 2-epimerase from hog kidney (1966), Methods Enzymol., 8, 191-195.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
EDTA
-
Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3
-
N-acetyl-D-mannosamine
-
Sus scrofa
3.4
-
N-acetyl-D-glucosamine
-
Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.3
-
-
Sus scrofa

Storage Stability

Storage Stability Organism
stored in ice, stable for ar least 1 week Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 8
-
Sus scrofa

pH Range

pH Minimum pH Maximum Comment Organism
6.3 8.3 6.3: about 50% of maximal activity, 8.3: about 80% of maximal activity Sus scrofa

Cofactor

Cofactor Comment Organism Structure
ATP stimulates Sus scrofa
ATP Km: 1 mM Sus scrofa
ATP absolute requirement for ATP, but no conversion to ADP or AMP Sus scrofa
dATP can partially replace ATP in stimulation Sus scrofa