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Literature summary for 3.2.2.11 extracted from

  • Eylar, E.H.; Murakami, M.
    beta-Aspartyl-N-acetylglucosaminadase from epididymis (1966), Methods Enzymol., 8, 597-600.
No PubMed abstract available

General Stability

General Stability Organism
stable to lyophilization and freezing after butanol extraction Ovis ammon

Organism

Organism UniProt Comment Textmining
Ovis ammon
-
sheep
-

Purification (Commentary)

Purification (Comment) Organism
zone electrophoresis on starch block Ovis ammon

Source Tissue

Source Tissue Comment Organism Textmining
epididymis
-
Ovis ammon
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
630 units/g protein, eluate of starch block after electrophoresis Ovis ammon

Storage Stability

Storage Stability Organism
-20°C stable for several months Ovis ammon

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-beta-aspartyl-2-acetamido-1,2-dideoxy-D-glucosylamine + H2O
-
Ovis ammon N-acetylglucosamine + asparagine
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.7
-
-
Ovis ammon

pH Range

pH Minimum pH Maximum Comment Organism
6 8 activity near the maximum, completely inactive at pH 4.4 Ovis ammon