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Literature summary extracted from

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.3.8 EDTA
-
 Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.3.8 3
-
 N-acetyl-D-mannosamine
-
 Sus scrofa
5.1.3.8 3.4
-
 N-acetyl-D-glucosamine
-
 Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
5.1.3.8 Sus scrofa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.3.8
-
 Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
5.1.3.8 kidney
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.1.3.8 5.3
-
-
 Sus scrofa

Storage Stability

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.3.8 N-acetyl-D-glucosamine
-
 Sus scrofa N-acetyl-D-mannosamine
-
 r
5.1.3.8 N-acetyl-D-mannosamine
-
 Sus scrofa N-acetyl-D-glucosamine
-
 r
5.1.3.8 N-Acyl-D-glucosamine r Sus scrofa N-Acyl-D-mannosamine
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.1.3.8 7 8
-
 Sus scrofa

pH Range

EC Number pH Minimum pH Maximum Comment Organism
5.1.3.8 6.3 8.3 6.3: about 50% of maximal activity, 8.3: about 80% of maximal activity Sus scrofa

Cofactor

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