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.
History
EC 3.2.1.39 created 1965
Pathway
ec00500  Starch and sucrose metabolism
Orthology
K01199  glucan endo-1,3-beta-D-glucosidase
K19891  glucan endo-1,3-beta-glucosidase 1/2/3
K19892  glucan endo-1,3-beta-glucosidase 4
K19893  glucan endo-1,3-beta-glucosidase 5/6
Genes
RSS: 109441457
ATH: AT1G11820 AT1G66250 AT2G01630 AT3G13560 AT4G31140 AT5G58090
ALY: ARALYDRAFT_478745 ARALYDRAFT_484077 ARALYDRAFT_495914 ARALYDRAFT_678872 ARALYDRAFT_894267 ARALYDRAFT_913356
CRB: 17876086 17877453 17886892 17893804
CSAT: 104701221 104710092 104717078 104721722 104726376 104730182 104735163 104739829 104745607 104750408 104755438 104761909 104765140 104770590 104778052 104779479 104787652 104789925
EUS: EUTSA_v10004013mg EUTSA_v10006713mg EUTSA_v10013422mg EUTSA_v10018427mg EUTSA_v10020572mg EUTSA_v10025047mg
BRP: 103836214 103845244 103851660 103852070 103852319 103854051 103862032 103870118
BNA: 106354712 106362164 106369659 106375440 106381341 106383562 106388390 106392556 106401262 106405722 106407154 106413864 106424133 106426072 106432938 106440602 106452288 106452793 106454288
BOE: 106295886 106301285 106309604 106315508 106318292 106326888 106327214 106327794 106331142
THJ: 104803580 104803890 104805078 104805621 104811842 104815665 104818743 104822678 104823532 104823840
LJA: Lj0g3v0019959.1(Lj0g3v0019959.1) Lj0g3v0019969.1(Lj0g3v0019969.1) Lj0g3v0019969.2(Lj0g3v0019969.2) Lj0g3v0036859.1(Lj0g3v0036859.1) Lj0g3v0099909.1(Lj0g3v0099909.1) Lj0g3v0198239.1(Lj0g3v0198239.1) Lj0g3v0239939.1(Lj0g3v0239939.1) Lj0g3v0306599.1(Lj0g3v0306599.1) Lj2g3v3034050.1(Lj2g3v3034050.1) Lj4g3v0149330.1(Lj4g3v0149330.1) Lj4g3v0149330.2(Lj4g3v0149330.2) Lj4g3v2604040.1(Lj4g3v2604040.1) Lj4g3v3112890.1(Lj4g3v3112890.1) Lj4g3v3112890.2(Lj4g3v3112890.2) Lj5g3v0553280.1(Lj5g3v0553280.1) Lj6g3v0423710.1(Lj6g3v0423710.1) Lj6g3v1859490.1(Lj6g3v1859490.1) Lj6g3v1859510.1(Lj6g3v1859510.1)
DOSA: Os02t0139300-01(Os02g0139300) Os03t0221500-01(Os03g0221500) Os07t0510200-01(Os07g0510200) Os07t0577300-01(Os07g0577300) Os08t0224500-01(Os08g0224500)
ATS: 109735056(LOC109735056) 109748827(LOC109748827) 109756982(LOC109756982) 109770871(LOC109770871) 109772961(LOC109772961) 109778398(LOC109778398) 109778706(LOC109778706)
SLB: AWJ20_487(BGL2)
NTE: NEUTE1DRAFT116758(NEUTE1DRAFT_116758) NEUTE1DRAFT136240(NEUTE1DRAFT_136240)
ANI: AN7950.2
ANG: ANI_1_668034(An03g05290)
 » show all
Taxonomy
Reference
1  [PMID:14020682]
  Authors
CHESTERS CG, BULL AT.
  Title
The enzymic degradation of laminarin. 2. The multicomponent nature of fungal laminarinases.
  Journal
Biochem. J. 86 (1963) 31-8.
Reference
2  [PMID:13638895]
  Authors
REESE ET, MANDELS M.
  Title
Beta-D-1, 3 Glucanases in fungi.
  Journal
Can. J. Microbiol. 5 (1959) 173-85.
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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