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Literature summary for 3.2.1.96 extracted from

  • Chien, S.F.; Weinburg, R.; Li, S.C.; Li, Y.T.
    endo-beta-N-Acetylglucosaminidase from fig latex (1977), Biochem. Biophys. Res. Commun., 76, 317-323.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Ficus carica
-
-
-

Purification (Commentary)

Purification (Comment) Organism
endo-beta-N-acetylglucosaminidase F-I and F-II Ficus carica
partial Ficus carica

Source Tissue

Source Tissue Comment Organism Textmining
latex
-
Ficus carica
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(Man)3(GlcNAc)2-N-dansyl-Asn + H2O
-
Ficus carica GlcNAc-N-dansyl-Asn + (Man)3-GlcNAc
-
?
(Man)3(GlcNAc)2Asn + H2O di-N-acetylchitobiosyl linkage is hydrolyzed faster than the linkage in the glycopeptides (Man)5(GlcNAc)3Asn and (Man)6(GlcNAc)2Asn by enzyme form F-I. No activity with the enzyme form F-II Ficus carica (Man)3GlcNAc + GlcNAc-Asn
-
?
(Man)5(GlcNAc)2-N-dansyl-Asn + H2O
-
Ficus carica GlcNAc-N-dansyl-Asn + (Man)5-GlcNAc
-
?
(Man)5(GlcNAc)2Asn + H2O di-N-acetylchitobiosyl linkage is hydrolyzed faster than the linkage in the glycopeptides (Man)5(GlcNAc)3Asn and (Man)6(GlcNAc)2Asn by enzyme form F-I Ficus carica (Man)5GlcNAc + GlcNAc-Asn
-
?
(Man)6(GlcNAc)2Asn + H2O di-N-acetylchitobiosyl linkage is hydrolyzed faster than the linkage in the glycopeptides (Man)5(GlcNAc)3Asn and (Man)6(GlcNAc)2Asn by enzyme form F-I Ficus carica (Man)6GlcNAc + GlcNAc-Asn
-
?