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Literature summary for 3.2.1.21 extracted from

  • Chuenchor, W.; Pengthaisong, S.; Robinson, R.C.; Yuvaniyama, J.; Svasti, J.; Cairns, J.R.
    The structural basis of oligosaccharide binding by rice BGlu1 beta-glucosidase (2011), J. Struct. Biol., 173, 169-179.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Oryza sativa

Crystallization (Commentary)

Crystallization (Comment) Organism
structures of the BGlu1 E176Q mutant, its complexes with cellotetraose, cellopentaose and laminaribiose, and its covalent intermediate with 2-deoxy-2-fluoroglucoside are determined at 1.65, 1.95, 1.80, 2.80, and 1.90 A resolution, respectively Oryza sativa

Protein Variants

Protein Variants Comment Organism
E176A inactive under standard assay conditions, mutant can be rescued by (small nucleophiles) acetate and azide but not as mutant E176Q Oryza sativa
E176D inactive under standard assay conditions, mutant can not be rescued by any small nucleophile Oryza sativa
E176Q E176Q active site mutant can be effectively rescued by small nucleophiles, such as acetate, azide and ascorbate, for hydrolysis of aryl glycosides in a pH-independent manner above pH 5. Cellotriose, cellotetraose, cellopentaose, cellohexaose and laminaribiose are not hydrolyzed by the mutant and instead exhibit competitive inhibition Oryza sativa
E386D 3000fold less active than wild-type Oryza sativa
E386Q 60000fold less active than wild-type Oryza sativa

Organism

Organism UniProt Comment Textmining
Oryza sativa
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl beta-D-glucopyranoside + H2O
-
Oryza sativa 4-nitrophenol + D-glucopyranose
-
?

Synonyms

Synonyms Comment Organism
beta-glucosidase
-
Oryza sativa

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information in the presence of 50 mM azide, the apparent kcat values of the E176Q and E176A mutants are nearly independent of the pH from pH 5-10, while those of the wild-type and E176D enzymes decrease 30 and 8fold, respectively, as the pH increases from 5 to 10 Oryza sativa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
assay at Oryza sativa