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Literature summary 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

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

Organism

EC Number Organism UniProt Comment Textmining
3.2.2.11 Ovis ammon
-
sheep
-

Purification (Commentary)

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.2.11 epididymis
-
Ovis ammon
-

Specific Activity [micromol/min/mg]

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

Storage Stability

EC Number Storage Stability Organism
3.2.2.11 -20°C stable for several months Ovis ammon

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.2.11 1-beta-aspartyl-2-acetamido-1,2-dideoxy-D-glucosylamine + H2O
-
Ovis ammon N-acetylglucosamine + asparagine
-
?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.2.11 7.7
-
-
Ovis ammon

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.2.11 6 8 activity near the maximum, completely inactive at pH 4.4 Ovis ammon