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Literature summary extracted from

  • Hoj, P.B.; Rodriguez, E.B.; Stick, R.V.; Stone, B.A.
    Differences in active site structure in a family of beta-glucan endohydrolases deduced from the kinetics of inactivation by epoxyalkyl beta-oligoglucosides (1989), J. Biol. Chem., 264, 4939-4947.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.39 (2,3)-epoxypropyl beta-D-laminaribiose number of glucosyl residues in the inhibitor affects aglycon chain length specificity and correct positioning of the substrate at the active site Nicotiana glutinosa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.73 27500
-
 x * 27500, enzyme inactivated by epoxyalkyl beta-D-oligoglucosides Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.39 Nicotiana glutinosa
-
-
-
3.2.1.73 Bacillus subtilis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.39 laminarin + H2O
-
 Nicotiana glutinosa D-glucose + ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.73 ? x * 27500, enzyme inactivated by epoxyalkyl beta-D-oligoglucosides Bacillus subtilis