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Literature summary extracted from

  • Hrmova, M.; MacGregor, E.A.; Biely, P.; Stewart, R.J.; Fincher, G.B.
    Substrate binding and catalytic mechanism of a barley beta-D-glucosidase/(1,4)-beta-D-glucan exohydrolase (1998), J. Biol. Chem., 273, 11134-11143.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.74 1,2-anhydro-myo-inositol
-
 Hordeum vulgare

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.74 additional information
-
 additional information laminarioligosaccharide degree of polymerization 2, 5.37, laminarioligosaccharide degree of polymerization 3, 2.77, laminarioligosaccharide degree of polymerization 4, 0.52 Hordeum vulgare
3.2.1.74 0.29
-
 cellohexaose
-
 Hordeum vulgare
3.2.1.74 0.41
-
 cellopentaose
-
 Hordeum vulgare
3.2.1.74 0.89
-
 cellotetraose
-
 Hordeum vulgare
3.2.1.74 0.97
-
 cellotriose
-
 Hordeum vulgare
3.2.1.74 2.67
-
 cellobiose
-
 Hordeum vulgare

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.74 Hordeum vulgare
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.74 seedling
-
 Hordeum vulgare
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.74 cellobiose + H2O
-
 Hordeum vulgare D-glucose + cellotetraose + cellotriose
-
 ?
3.2.1.74 cellohexaose + H2O
-
 Hordeum vulgare D-glucose + ?
-
 ?
3.2.1.74 cellopentaose + H2O
-
 Hordeum vulgare D-glucose + ?
-
 ?
3.2.1.74 cellotetraose + H2O
-
 Hordeum vulgare D-glucose + cellotriose + cellobiose
-
 ?
3.2.1.74 cellotriose + H2O
-
 Hordeum vulgare D-glucose + cellobiose
-
 ?
3.2.1.74 p-nitrophenyl-beta-D-glucopyranoside + H2O
-
 Hordeum vulgare 4-nitrophenol + D-glucose when incubated with 100 mM substrate, products are also 4-nitrophenyl-beta-laminaribioside, 4-nitrophenyl-beta-cellobioside and 4-nitrophenyl-beta-gentiobioside ?