Glucan endo-1,3-β-D-glucosidase
(Redirected from Callase)
| Glucan endo-1,3-β-D-glucosidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.2.1.39 | ||||||||
| CAS no. | 9025-37-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Glucan endo-1,3-β-D-glucosidase (EC 3.2.1.39, endo-1,3-β-glucanase, laminarinase, laminaranase, oligo-1,3-glucosidase, callase, beta-1,3-glucanase, Kitalase (trademark), 1,3-β-D-glucan 3-glucanohydrolase, endo-(1,3)-β-D-glucanase, (1→3)-β-glucan 3-glucanohydrolase, endo-1,3-β-D-glucanase, endo-1,3-β-glucosidase, 1,3-β-D-glucan glucanohydrolase) is an enzyme with systematic name 3-β-D-glucan glucanohydrolase.[1][2] This enzyme catalyses the following chemical reaction
- Hydrolysis of (1→3)-β-D-glucosidic linkages in (1→3)-β-D-glucans
This enzyme is marginally active on mixed-link (1→3,1→4)-β-D-glucans.
References
[edit]- ^ Chesters CG, Bull AT (January 1963). "The enzymic degradation of laminarin. 2. The multicomponent nature of fungal laminarinases". The Biochemical Journal. 86 (1): 31–8. PMC 1201707. PMID 14020682.
- ^ Reese ET, Mandels M (April 1959). "β-D-Glucanases in fungi". Canadian Journal of Microbiology. 5 (2): 173–185. doi:10.1139/m59-022. PMID 13638895.
External links
[edit]- Glucan+endo-1,3-beta-D-glucosidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
