KEGG   ENZYME: 3.2.1.39Help
Entry
EC 3.2.1.39                 Enzyme                                 

Name glucan endo-1,3-beta-D-glucosidase;
endo-1,3-beta-glucanase;
laminarinase;
laminaranase;
oligo-1,3-glucosidase;
endo-1,3-beta-glucanase;
callase;
beta-1,3-glucanase;
kitalase;
1,3-beta-D-glucan 3-glucanohydrolase;
endo-(1,3)-beta-D-glucanase;
(1->3)-beta-glucan 3-glucanohydrolase;
endo-1,3-beta-D-glucanase;
endo-1,3-beta-glucosidase;
1,3-beta-D-glucan glucanohydrolase
Class Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl
compounds
BRITE hierarchy
Sysname 3-beta-D-glucan glucanohydrolase
Reaction(IUBMB) Hydrolysis of (1->3)-beta-D-glucosidic linkages in
(1->3)-beta-D-glucans
Reaction(KEGG) (other) R00308 R06204(G)
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Comment Different from EC 3.2.1.6 endo-1,3(4)-beta-glucanase. Very limited
action on mixed-link (1->3,1->4)-beta-D-glucans. Hydrolyses
laminarin, paramylon and pachyman.
Pathway PATH: ec00500  Starch and sucrose metabolism
Orthology KO: K01199  glucan endo-1,3-beta-D-glucosidase
Genes ATH: AT3G57260(BGL2)
MGR: MGG_09733
TET: TTHERM_00243770 TTHERM_00637420 TTHERM_00956460 TTHERM_00956480
SFR: Sfri_1319
SAZ: Sama_1396
SDE: Sde_3121
PIN: Ping_0554
MMR: Mmar10_0247
NAR: Saro_1608
SAL: Sala_0919
RHA: RHA1_ro05769 RHA1_ro05771
FJO: Fjoh_2435
Taxonomy
Structures PDB: 1GHS  2CYG  2HYK  2VY0  3DGT  3EM5  3F55  3GD0  3GD9  
Reference
  Authors
  Title

  Journal
  Organism

1  [PMID:14020682]
CHESTERS CG, BULL AT.
The enzymic degradation of laminarin. 2. The multicomponent nature
of fungal laminarinases.
Biochem. J. 86 (1963) 31-8.
Myrothecium verrucaria, Penicillium stipitatum, Streptomyces sp.,
Trichoderma viride
Reference
  Authors
  Title
  Journal
  Organism
2  [PMID:13638895]
REESE ET, MANDELS M.
Beta-D-1, 3 Glucanases in fungi.
Can. J. Microbiol. 5 (1959) 173-85.
Aspergillus niger [GN:ang]
Other DBs ExplorEnz - The Enzyme Database: 3.2.1.39
IUBMB Enzyme Nomenclature: 3.2.1.39
ExPASy - ENZYME nomenclature database: 3.2.1.39
BRENDA, the Enzyme Database: 3.2.1.39
CAS: 9025-37-0

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