A single residue affects the dynamics and shape of a tetrameric GH43 β-1,4-d-xylosidase from Levilactobacillus brevis DSM1269.

The turnover number ( k cat ) of both Lb Xyn43B and Lb Xyn43B/Thr274Ala was higher for X2 than for X3, while the K m showed a decreasing trend (although not statistically significant) for X3 compared with X2, indicating that this enzyme may have some further substrate interactions in addition to the two subsites (−1 and +1), shown for other structurally studied GH43 subfamily 11 β‐xylosidases.

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