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Literature summary extracted from

  • Kersters-Hilderson, H.; Van Doorslaer, E.; Lippens, M.; De Bruyne, C.K.
    The pH dependence and group modification of beta-D-xylosidase from Bacillus pumilus: Evidence for sulfhydryl and histidyl groups (1984), Arch. Biochem. Biophys., 234, 61-72.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.37 5,5'-dithiobis(2-nitrobenzoic acid) rapid inactivation by modification of an essential thiol group Bacillus pumilus
3.2.1.37 diethyldicarbonate inactivation indicates a carbethoxylation of histidine residues Bacillus pumilus
3.2.1.37 methylmethanethiolsulfonate rapid decrease in activity, treatment with dithiothreitol restores activity to about 75% Bacillus pumilus
3.2.1.37 n-butyl beta-D-xylopyranoside pH above 7.5 affects the binding of the competitive inhibitor Bacillus pumilus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.37 intracellular
-
 Bacillus pumilus 5622
-

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.37 Bacillus pumilus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.37 cell culture enzyme production induced in xylan or xylose media Bacillus pumilus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.37 p-nitrophenyl beta-D-xylopyranoside + H2O
-
 Bacillus pumilus p-nitrophenol + beta-D-xylopyranose
-
 ?

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.37 7.5
-
 activity decreases above, involvement of an essential acid-base group, which is protonated for catalysis Bacillus pumilus