Poly(alpha-L-guluronate) lyase
| guluronate-specific alginate lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.2.2.11 | ||||||||
| CAS no. | 64177-88-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The enzyme guluronate-specific alginate lyase (EC 4.2.2.11, formerly called poly(α-L-guluronate) lyase) catalyzes the following process:
- Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-α-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and α-L-uluronate at their reducing end.
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is alginate α-L-guluronate—uronate lyase. Other names in common use include alginase II, guluronate lyase, L-guluronan lyase, L-guluronate lyase, poly-α-L-guluronate lyase, and polyguluronate-specific alginate lyase.
Structural studies
[edit]As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1UAI.
References
[edit]- Boyd J, Turvey JR (1977). "Isolation of poly-alpha-L-guluronate lyase from Klebsiella aerogenes". Carbohydr. Res. 57: 163–71. doi:10.1016/S0008-6215(00)81928-X. PMID 332364.
- Davidson IW, Sutherland IW, Lawson CJ (1976). "Purification and properties of an alginate lyase from a marine bacterium". Biochem. J. 159 (3): 707–13. doi:10.1042/bj1590707. PMC 1164172. PMID 1008828.
