ENZYME entry: EC 3.2.1.155
| Accepted Name |
| Xyloglucan-specific exo-beta-1,4-glucanase.
|
| Reaction catalysed |
| Hydrolysis of (1->4)-D-glucosidic linkages in xyloglucans so as to successively remove oligosaccharides from the chain end |
| Comment(s) |
- The enzyme removes XXXG heptasaccharides, XXLG/XLXG octasaccharides
and XLLG nonasaccharides from the end of tamarind seed xyloglucan
polymers in a processive manner.
- Hydrolysis occurs at the unsubstituted D-glucopyranose residue in the
main backbone.
- It is not known whether the cleavage takes place at the reducing or
non-reducing end of the polymer.
- Very low activity with beta-D-glucans.
- The enzyme from Chrysosporium lucknowense shifts to an endoglucanase
mode when acting on linear substrates without bulky substituents on
the polymeric backbone such as barley beta-glucan.
|
| Cross-references |
| BRENDA | 3.2.1.155 |
| EC2PDB | 3.2.1.155 |
| ExplorEnz | 3.2.1.155 |
| PRIAM enzyme-specific profiles | 3.2.1.155 |
| KEGG Ligand Database for Enzyme Nomenclature | 3.2.1.155 |
| IUBMB Enzyme Nomenclature | 3.2.1.155 |
| IntEnz | 3.2.1.155 |
| MEDLINE | Find literature relating to 3.2.1.155 |
| MetaCyc | 3.2.1.155 |
| UniProtKB/Swiss-Prot |
|
View entry in original ENZYME format
View entry in raw text format (no links)
All UniProtKB/Swiss-Prot
entries referenced
in this entry, with possibility to download in different formats, align etc.
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.-.-.-