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The title enzyme is competitively inhibited by compounds, for example alpha-D-xylopyranosylpyridinium salts and 1,6-anhydro-D-glucopyranose, for which the normal 4C1 conformation of the xylopyranose ring is precluded. It is competitively inhibited by compounds, for example beta-D-xylopyranosylpyridinium salts and 1,6-anhydro-L-idopyranose, for which the 1C4 conformation is precluded, and which have no accessible conformations in common with the first set of inhibitors. It is also competitively inhibited by alpha-L-arabinofuranosides. Inhibition by 1,6-anhydroglucopyranose, 1,6-anhydro-L-idopyranose and L-arabinono-gamma-lactone is competitive with respect to each other. alpha-D-Xylopyranosyl fluoride is not a detectable substrate, by itself or in the presence of a representative of any of the three types of inhibitor. On the basis of these and literature data, it is proposed that the natural substrate is a hemicellulose fragment containing the D-Xylp beta (1 leads to 4)-[L-Araf alpha (1 leads to 3)]D-Xylp structure. Tentative inferences about the catalytic mechanism can also be drawn.

biochemical journal

Competitive inhibition of the inverting <i>β</i>-xylosidase of <i>Bacillus pumilus</i> 12 by monosaccharide derivatives of different structural and conformational types. A possible natural substrate

Competitive inhibition of the inverting β-xylosidase of Bacillus pumilus 12 by monosaccharide derivatives of different structural and conformational types. A possible natural substrate