| EC |
3.2.1.39 |
| Accepted name: |
glucan endo-1,3-β-D-glucosidase |
| Reaction: |
Hydrolysis of (1→3)-β-D-glucosidic linkages in (1→3)-β-D-glucans |
| Other name(s): |
endo-1,3-β-glucanase; laminarinase; laminaranase; oligo-1,3-glucosidase; endo-1,3-β-glucanase; callase; β-1,3-glucanase; kitalase; 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 |
| Systematic name: |
3-β-D-glucan glucanohydrolase |
| Comments: |
Different from EC 3.2.1.6 endo-1,3(4)-β-glucanase. Very limited action on mixed-link (1→3,1→4)-β-D-glucans. Hydrolyses laminarin, paramylon and pachyman. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9025-37-0 |
| References: |
| 1. |
Chesters, C.G.C. and Bull, A.T. The enzymic degradation of laminarin. 2. The multicomponent nature of fungal laminarinases. Biochem. J. 86 (1963) 31–38. [PMID: 14020682] |
| 2. |
Reese, E.T. and Mandels, M. β-D-1,3-Glucanases in fungi. Can. J. Microbiol. 5 (1959) 173–185. [PMID: 13638895] |
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| [EC 3.2.1.39 created 1965] |
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