EC 3.2.1.39 - Glucan endo-1,3-β-D-glucosidase

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IntEnz Enzyme Nomenclature
EC 3.2.1.39

Names

Accepted name:
glucan endo-1,3-β-D-glucosidase
Other names:
(1→3)-β-glucan 3-glucanohydrolase
(1→3)-β-glucan endohydrolase
1,3-β-D-glucan 3-glucanohydrolase
β-1,3-glucanase
callase
endo-(1,3)-β-D-glucanase
endo-(1→3)-β-D-glucanase
endo-1,3-β-D-glucanase
endo-1,3-β-glucanase
endo-1,3-β-glucosidase
kitalase
laminaranase
laminarinase
oligo-1,3-glucosidase
1,3-β-D-glucan glucanohydrolase
Systematic name:
3-β-D-glucan glucanohydrolase

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00507 , PROSITE:PDOC00794
Structural data: CSA , EC2PDB
Gene Ontology: GO:0042973
CAS Registry Number: 9025-37-0
UniProtKB/Swiss-Prot: (83) [show] [UniProt]

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: 31-38 (1963). [PMID: 14020682]
  2. Reese, E.T. and Mandels, M.
    β-D-1,3-Glucanases in fungi.
    Can. J. Microbiol. 5: 173-185 (1959). [PMID: 13638895]

[EC 3.2.1.39 created 1965]