Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.2.1.21 extracted from

  • Fukuda, T.; Kato-Murai, M.; Kadonosono, T.; Sahara, H.; Hata, Y.; Suye, S.; Ueda, M.
    Enhancement of substrate recognition ability by combinatorial mutation of beta-glucosidase displayed on the yeast cell surface (2007), Appl. Microbiol. Biotechnol., 76, 1027-1033.
    View publication on PubMed
Search for more literature for 3.2.1.21

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli strain DH5alpha, display of the enzyme on the cell surface of Saccharomyces cerevisiae Aspergillus oryzae

Protein Variants

Protein Variants Comment Organism
G294A site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Aspergillus oryzae
G294C site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Aspergillus oryzae
G294D site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme Aspergillus oryzae
G294E site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Aspergillus oryzae
G294F site-directed mutagenesis, the mutant shows 1.5fold higher activities for substrate recognition than the wild-type enzyme Aspergillus oryzae
G294H site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Aspergillus oryzae
G294I site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Aspergillus oryzae
G294K site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Aspergillus oryzae
G294L site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Aspergillus oryzae
G294M site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Aspergillus oryzae
G294N site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Aspergillus oryzae
G294P site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Aspergillus oryzae
G294Q site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Aspergillus oryzae
G294R site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Aspergillus oryzae
G294S site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Aspergillus oryzae
G294T site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Aspergillus oryzae
G294V site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Aspergillus oryzae
G294W site-directed mutagenesis, the mutant shows 1.5fold higher activities for substrate recognition than the wild-type enzyme Aspergillus oryzae
G294Y site-directed mutagenesis, the mutant shows 1.6fold higher activities for substrate recognition than the wild-type enzyme Aspergillus oryzae
additional information rapid construction of a library of mutant BGL1 from Aspergillus oryzae by yeast cell surface engineering Aspergillus oryzae

Localization

Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cellobiose + H2O Aspergillus oryzae
-
 2 beta-D-glucose
-
 ?

Organism

Organism UniProt Comment Textmining
Aspergillus oryzae
-
-
-

Reaction

Reaction Comment Organism Reaction ID
celloheptaose + 6 H2O = 7 beta-D-glucose W293 of the SDW segment, which is the residue next to the nucleophile D292 in family 3 BGL, is very important for hydrolytic reaction as a binder to a substrate. G294 of the SDWG sequence might play an important role in catalysis, interaction between the sugar rings and aromatic ring of W293 at the entrance of the catalytic pocket enhances the substrate recognition of beta-glucosidase Aspergillus oryzae
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl beta-D-cellobioside + 2 H2O
-
 Aspergillus oryzae 4-nitrophenol + 2 beta-D-glucose
-
 ?
4-nitrophenyl beta-D-glucopyranoside + H2O
-
 Aspergillus oryzae 4-nitrophenol + beta-D-glucose
-
 ?
cellobiose + H2O
-
 Aspergillus oryzae 2 beta-D-glucose
-
 ?
cellobiose + H2O interaction between the sugar rings and aromatic ring of W293 at the entrance of the catalytic pocket enhances the substrate recognition of beta-glucosidase Aspergillus oryzae 2 beta-D-glucose
-
 ?

Synonyms

Synonyms Comment Organism
beta-glucosidase 1
-
 Aspergillus oryzae
BGL1
-
 Aspergillus oryzae
More the enzyme belongs to the glycosyl hydrolase family 3 Aspergillus oryzae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Aspergillus oryzae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
 assay at Aspergillus oryzae