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EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
aspartyl-n-acetyl-beta-d-glucosaminidase,
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aspartamidohydrolase
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aspartyl-N-acetyl-beta-D-glucosaminidase
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beta-aspartylacetylglucosaminidase
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snail-glycosylamidase
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1-beta-aspartyl-N-acetyl-D-glucosaminylamine + H2O = L-asparagine + N-acetyl-D-glucosamine
1-beta-aspartyl-N-acetyl-D-glucosaminylamine + H2O = L-asparagine + N-acetyl-D-glucosamine
splits glycopeptides, containing the group 1-[beta-aspartyl]-N-glucosamine, only when the NH2-and CO2-group of the aspartic acid are free
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1-beta-aspartyl-N-acetyl-D-glucosaminylamine + H2O = L-asparagine + N-acetyl-D-glucosamine
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hydrolysis of N-glycosyl bond
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1-beta-aspartyl-N-acetyl-D-glucosaminylamine L-asparaginohydrolase
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1,2-dideoxy-1-[L-beta-aspartamido]-2-acetamido-beta-D-glucopyranose + H2O
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1-beta-aspartyl-2-acetamido-1,2-dideoxy-D-glucosylamine + H2O
N-acetylglucosamine + asparagine
glycopeptide + H2O
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1-beta-aspartyl-2-acetamido-1,2-dideoxy-D-glucosylamine + H2O
N-acetylglucosamine + asparagine
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1-beta-aspartyl-2-acetamido-1,2-dideoxy-D-glucosylamine + H2O
N-acetylglucosamine + asparagine
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action of the enzyme is followed by alpha(1-6)mannosidase, EC 3.2.1.24
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glycopeptide + H2O
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additional information
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630 units/g protein, eluate of starch block after electrophoresis
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7.7
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6 - 8
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activity near the maximum, completely inactive at pH 4.4
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human
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snail, L.
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sheep
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rat
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brenda
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brenda
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brenda
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brenda
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brenda
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40000
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ultracentrifugation
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37
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3-5 min at 100°C, activity lost
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stable to lyophilization and freezing after butanol extraction
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-20°C stable for several months
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4°C, pH 2-10, several days
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zone electrophoresis on starch block
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Eylar, E.H.; Murakami, M.
beta-Aspartyl-N-acetylglucosaminadase from epididymis
Methods Enzymol.
8
597-600
1966
Ovis ammon
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Kaverzneva, E.D.; Tschuchrova, A.I.; Kisseleva, V.V.
_ber Glykosylamidasen aus Limnaea stagnalis L.
Liebigs Ann. Chem.
738
130-135
1970
Lymnaea stagnalis
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brenda
Haeuw, J.F.; Grard, T.; Alonso, C.; Strecker, G.; Michalski, J.C.
The core-specific lysosomal alpha(1-6)-mannosidase activity depends on aspartamidohydrolase activity
Biochem. J.
297
463-466
1994
Homo sapiens, Rattus rattus
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brenda
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