Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.1.3.8 extracted from

  • Ghosh, S.; Roseman, S.
    The sialic acids. V. N-Acyl-D-glucosamine 2-epimerase (1965), J. Biol. Chem., 240, 1531-1536.
    View publication on PubMed

General Stability

General Stability Organism
not stable to freezing and thawing Sus scrofa
stable to dialysis Sus scrofa

Inhibitors

Inhibitors Comment Organism Structure
EDTA inhibition can be overcome by Mg2+ Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
hog
-

Purification (Commentary)

Purification (Comment) Organism
-
Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
kidney cortex 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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-Acyl-D-glucosamine r Sus scrofa N-Acyl-D-mannosamine
-
?
N-Acyl-D-glucosamine also catalyzes epimerization of the corresponding N-glycolyl derivatives 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 absolute requirement for ATP, but no conversion to ADP or AMP Sus scrofa
dATP
-
Sus scrofa