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Literature summary extracted from

  • Kuntothom, T.; Raab, M.; Tvaroska, I.; Fort, S.; Pengthaisong, S.; Canada, J.; Calle, L.; Jimenez-Barbero, J.; Ketudat Cairns, J.R.; Hrmova, M.
    Binding of beta-D-glucosides and beta-D-mannosides by rice and barley beta-D-glycosidases with distinct substrate specificities (2010), Biochemistry, 49, 8779-8793.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.25 expression in Escherichia coli Hordeum vulgare

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.25 4-nitrophenyl beta-D-thioglucoside competitive, adopts 4NP-S-Glc 3S5 or 1S3 conformations upon binding according to STD NMR and trNOESY experiments. QM modeling and docking, based on GLIDE scores, predicts that 4-nitrophenyl beta-D-thioglucoside preferentially binds in 1S3 geometries Hordeum vulgare
3.2.1.25 4-nitrophenyl beta-D-thiomannoside competitive, adopts 4C1 geometry upon binding according to STD NMR and trNOESY experiments. QM modeling and docking, based on GLIDE scores, predicts that 4-nitrophenyl beta-D-thiomannoside preferentially binds in 1S3 geometries Hordeum vulgare

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.25 0.25
-
 4-nitrophenyl-beta-D-mannopyranose pH 4.0, 30°C Hordeum vulgare
3.2.1.25 0.5
-
 4-nitrophenyl-beta-D-glucopyranose pH 4.0, 30°C Hordeum vulgare

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.25 Hordeum vulgare B5A496 var. distichum
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.25 4-nitrophenyl beta-D-glucopyranose + H2O
-
 Hordeum vulgare 4-nitrophenol + beta-D-glucose
-
 ?
3.2.1.25 4-nitrophenyl beta-D-mannopyranoside + H2O
-
 Hordeum vulgare 4-nitrophenol + beta-D-mannose
-
 ?
3.2.1.25 additional information in glycoside recognition and substrate specificity of HvBII, a combination of the following determinants is likely to play key roles: the inherent conformational and spatial flexibilities of gluco- and manno-configured substrates in the enzymes' active sites, the subtle differences in the spatial disposition of active site residues and their capacities to form interactions with specific groups of substrates, and the small variations in the charge distributions and shapes of the catalytic sites Hordeum vulgare ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.25 HvBII
-
 Hordeum vulgare

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.25 0.5
-
 4-nitrophenyl-beta-D-glucopyranose pH 4.0, 30°C Hordeum vulgare
3.2.1.25 3.1
-
 4-nitrophenyl-beta-D-mannopyranose pH 4.0, 30°C Hordeum vulgare

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.2.1.25 0.095
-
 4-nitrophenyl beta-D-thioglucoside pH 4.0, 30°C Hordeum vulgare
3.2.1.25 0.266
-
 4-nitrophenyl beta-D-thiomannoside pH 4.0, 30°C Hordeum vulgare

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.2.1.25 1
-
 4-nitrophenyl-beta-D-glucopyranose pH 4.0, 30°C Hordeum vulgare
3.2.1.25 12.7
-
 4-nitrophenyl-beta-D-mannopyranose pH 4.0, 30°C Hordeum vulgare