ENZYME entry: EC 4.2.2.11
| Accepted Name |
|---|
| Guluronate-specific alginate lyase.
|
| Alternative Name(s) |
|---|
| Alginase II. |
| Poly(alpha-L-guluronate) lyase. |
| Reaction catalysed |
|---|
| Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and alpha-L-guluronate at their reducing end |
| Comment(s) |
|---|
- The enzyme catalyzes the degradation of alginate by a beta-
elimination reaction.
- It cleaves the (1->4) bond between alpha-L-guluronate and either
alpha-L-guluronate or beta-D-mannuronate, generating oligosaccharides
with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-
reducing ends and alpha-L-guluronate at the reducing end.
- Depending on the composition of the substrate, the enzyme produces
oligosaccharides ranging from two to six residues, with preference
for shorter products.
- Cf. EC 4.2.2.3.
|
| Cross-references |
|---|
| BRENDA | 4.2.2.11 |
| EC2PDB | 4.2.2.11 |
| ExplorEnz | 4.2.2.11 |
| PRIAM enzyme-specific profiles | 4.2.2.11 |
| KEGG Ligand Database for Enzyme Nomenclature | 4.2.2.11 |
| IUBMB Enzyme Nomenclature | 4.2.2.11 |
| IntEnz | 4.2.2.11 |
| MEDLINE | Find literature relating to 4.2.2.11 |
| MetaCyc | 4.2.2.11 |
| Rhea expert-curated reactions | 4.2.2.11 |
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ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 4.2.2.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.2.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.-.-.-