3.2.1.58: glucan 1,3-beta-glucosidase
This is an abbreviated version!
For detailed information about glucan 1,3-beta-glucosidase, go to the full flat file.
Word Map on EC 3.2.1.58
Reaction
Synonyms
1,3-beta-D-glucanohydrolase, AkLam33, ALAM, beta-(1,3)(1,3)-glucanase, beta-(1,3)-glucanase, beta-1,3-exoglucanase, beta-1,3-glucan exo-hydrolase, beta-1,3-glucanase, BGL1, Bglu3B, BGN3.2, BGN3.4, CC1G_06564, CC1G_07313, Celf_3321, ChinLam, Exg, Exg1, EXG2, ExgA, ExgP, exo (13)-beta-glucanase, exo-1,3-beta-D-glucanase, exo-1,3-beta-glucanase, Exo-1,3-beta-glucanase I/II, exo-1,3-beta-glucosidase, Exo-beta 1,3 glucanase, exo-beta-(1,3)-glucanase, exo-beta-(13)-D-glucanase, exo-beta-(13)-glucanohydrolase, exo-beta-1,3-D-glucanase, exo-beta-1,3-glucanase, exo-beta-glucanase, Exo1, Glu1, Glu17A, glucan (1-->3)-beta-glucosidase, GP29, Lam55, Lam55A, lamC, laminarinase, More, panomycocin, PiEXO, tag83, Xog1
ECTree
3.2.1.58 glucan 1,3-beta-glucosidaseAdvanced search results
results (
results (Engineering
Engineering on EC 3.2.1.58 - glucan 1,3-beta-glucosidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E292S
site-directed mutagenesis, the mutant shows altered transglycosidase activity as the wild-type enzyme and displays modest glycosynthase activity with alpha-D-glucopyranosyl fluoride as the donor and 4-nitrophenyl-beta-D-glucopyranoside as the acceptor, but surprisingly shows a marked preference for synthesizing beta-1,6-linked over beta-1,3- and beta-1,4-linked disaccharide products. Mechanism and expected regiospecificity for the glycosynthase reaction, overview
F258A
activity of the F258 mutants falls off steadily in the order Phe>Trp>Tyr>Ile>Ala
F258I
activity of the F258 mutants falls off steadily in the order Phe>Trp>Tyr>Ile>Ala
F258W
activity of the F258 mutants falls off steadily in the order Phe>Trp>Tyr>Ile>Ala
F258Y
activity of the F258 mutants falls off steadily in the order Phe>Trp>Tyr>Ile>Ala
D595A
Thermochaetoides thermophila
the mutant has fully lost enzymatic activity on laminarin
E631A
Thermochaetoides thermophila
the mutant has fully lost enzymatic activity on laminarin
E654A
Thermochaetoides thermophila
the mutant has fully lost enzymatic activity on laminarin
H596L
Thermochaetoides thermophila
the mutant shows 60-80% enzymatic activity on laminarin compared with the wild type enzyme
Q159L
Thermochaetoides thermophila
the mutant shows 60-80% enzymatic activity on laminarin compared with the wild type enzyme
Q190L
Thermochaetoides thermophila
the mutant has fully lost enzymatic activity on laminarin
Q241L
Thermochaetoides thermophila
the mutant almost loses enzymatic activity on laminarin
S220A
Thermochaetoides thermophila
the mutant shows 60-80% enzymatic activity on laminarin compared with the wild type enzyme
W590G
Thermochaetoides thermophila
the mutant shows 60-80% enzymatic activity on laminarin compared with the wild type enzyme
W592G
Thermochaetoides thermophila
the mutant shows 60-80% enzymatic activity on laminarin compared with the wild type enzyme
D595A
Thermochaetoides thermophila DSM 1495
-
the mutant has fully lost enzymatic activity on laminarin
-
E631A
Thermochaetoides thermophila DSM 1495
-
the mutant has fully lost enzymatic activity on laminarin
-
E654A
Thermochaetoides thermophila DSM 1495
-
the mutant has fully lost enzymatic activity on laminarin
-
Q190L
Thermochaetoides thermophila DSM 1495
-
the mutant has fully lost enzymatic activity on laminarin
-
S220A
Thermochaetoides thermophila DSM 1495
-
the mutant shows 60-80% enzymatic activity on laminarin compared with the wild type enzyme
-
additional information
additional information
-
downregulation of the expression of an exo-beta-1,3-glucanase, exg2, using RNA interference, phenotype, overview
additional information
-
downregulation of the expression of an exo-beta-1,3-glucanase, exg2, using RNA interference, phenotype, overview
-
additional information
gene GLU1 is silenced via a sense and antisense mediated silencing mechanism, one transformant named C1 shows significantly reduced growth and sporulation relative to the wild-type
