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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.21 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

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

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.21 Aspergillus oryzae
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.21 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.21 4-nitrophenyl beta-D-cellobioside + 2 H2O
-
 Aspergillus oryzae 4-nitrophenol + 2 beta-D-glucose
-
 ?
3.2.1.21 4-nitrophenyl beta-D-glucopyranoside + H2O
-
 Aspergillus oryzae 4-nitrophenol + beta-D-glucose
-
 ?
3.2.1.21 cellobiose + H2O
-
 Aspergillus oryzae 2 beta-D-glucose
-
 ?
3.2.1.21 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

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.21 30
-
 assay at Aspergillus oryzae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.21 5
-
 assay at Aspergillus oryzae