| Accepted Name |
|---|
| cyclic beta-1,2-glucan glucanotransferase
|
| Reaction catalysed |
|---|
| Cyclizes part of a (1->2)-beta-D-glucan chain by formation of a (1->2)-beta-D-glucosidic bond |
| Comment(s) |
|---|
- This enzyme is the cyclization domain of cyclic beta-1,2-glucan
synthase.
- Enzymes from Brucella abortus and Thermoanaerobacter italicus were
characterized.
- The cyclization domain of cyclic beta-1,2-glucan synthase is flanked
by an N-terminal beta-1,2-glucosyltransferase domain (cf.
EC 2.4.1.391) and a C-terminal beta-1,2-glucoside phosphorylase
domain (cf. EC 2.4.1.333), with the former responsible for elongation
and the latter for chain length control.
- The cyclization domain of T. italicus cyclizes linear
oligosaccharides with a degree of polymerization (DP) of 21 or higher
to produce cyclic glucans with DP 17 or higher.
- The cyclization domain also disproportionates linear beta-1,2-
glucooligosaccharides without cycling.
- The entire cyclic beta-1,2-glucan synthase from B. abortus
synthesizes cyclic beta-1,2-glucans with DP 17-22.
|
| Cross-references |
|---|
| BRENDA | 2.4.1.397 |
| EC2PDB | 2.4.1.397 |
| ExplorEnz | 2.4.1.397 |
| KEGG Ligand Database for Enzyme Nomenclature | 2.4.1.397 |
| IUBMB Enzyme Nomenclature | 2.4.1.397 |
| MEDLINE | Find literature relating to 2.4.1.397 |
| MetaCyc | 2.4.1.397 |
| Rhea expert-curated reactions | 2.4.1.397 |
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ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 2.4.1.-
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