ENZYME entry: EC 3.2.1.152
| Accepted Name |
|---|
| Mannosylglycoprotein endo-beta-mannosidase.
|
| Alternative Name(s) |
|---|
| Endo-beta-mannosidase. |
| Reaction catalysed |
|---|
| Hydrolysis of the alpha-D-mannosyl-(1->6)-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl sequence of glycoprotein to alpha-D-mannosyl-(1->6)-D-mannose and N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl sequences |
| Comment(s) |
|---|
- The substrate group is a substituent on N-4 of an asparagine residue
in the glycoprotein.
- The mannose residue at the non-reducing end of the sequence may carry
further alpha-D-mannosyl groups on O-3 or O-6, but such a substituent
on O-3 of the beta-D-mannosyl group prevents the action of the
enzyme.
- The enzyme was obtained from the lily, Lilium longiflorum.
|
| Cross-references |
|---|
| BRENDA | 3.2.1.152 |
| EC2PDB | 3.2.1.152 |
| ExplorEnz | 3.2.1.152 |
| PRIAM enzyme-specific profiles | 3.2.1.152 |
| KEGG Ligand Database for Enzyme Nomenclature | 3.2.1.152 |
| IUBMB Enzyme Nomenclature | 3.2.1.152 |
| IntEnz | 3.2.1.152 |
| MEDLINE | Find literature relating to 3.2.1.152 |
| MetaCyc | 3.2.1.152 |
| UniProtKB/Swiss-Prot |
|
View entry in original ENZYME format
View entry in raw text format (no links)
All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 3.2.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.2.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.-.-.-