Any feedback?
Literature summary for 3.2.1.96 extracted from
- New evidence of the substrate specificity of endo-beta-N-acetylglucosaminidase D (1984), J. Biochem., 95, 1209-1213.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptococcus pneumoniae | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| glycopeptide + H2O | specificity | Streptococcus pneumoniae | ? | - |
? |  |
| additional information | specificity | Streptococcus pneumoniae | ? | - |
? | |
| additional information | endo-beta-N-acetylglucosaminidase D does not require the presence of a free hydroxyl group at the C-4 position of the alpha-mannosyl residue of the trisaccharide glycan Manalpha, 3Manbeta1, 4GlcNAcbeta1,- | Streptococcus pneumoniae | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| endo-beta-N-acetylglucosaminidase D | - |
Streptococcus pneumoniae |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
