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A GH67 α-glucuronidase gene derived from Bacillus halodurans C-125 was expressed in E. coli to obtain a recombinant enzyme ( Bh GlcA67). Using the purified enzyme, the enzymatic properties and substrate specificities of the enzyme were investigated. Bh GlcA67 showed maximum activity at pH 5.4 and 45 °C. When Bh GlcA67 was incubated with birchwood, oat spelts, and cotton seed xylan, the enzyme did not release any glucuronic acid or 4- O -methyl-glucuronic acid from these substrates. Bh GlcA67 acted only on 4- O -methyl-α-D-glucuronopyranosyl-(1→2)-β-D-xylopyranosyl-(1→4)-β-D-xylopyranosyl-(1→4)-β-D-xylopyranose (MeGlcA 3 Xyl 3 ), which has a glucuronic acid side chain with a 4- O -methyl group located at its non-reducing end, but did not on β-D-xylopyranosyl-(1→4)-[4- O -methyl-α-D-glucuronopyranosyl-(l→2)]-β-D-xylopyranosyl-(1→4)-β-D-xylopyranosyl-(1→4)-β-D-xylop- yranose (MeGlcA 3 Xyl 4 ) and α-D-glucuronopyranosyl-(l→2)-β-D-xylopyranosyl-(1→4)-β-D-xylopyranosyl-(1→4)-β-D-xylopyranose (GlcA 3 Xyl 3 ). The environment for recognizing the 4- O -methyl group of glucuronic acid was observed in all the crystal structures of reported GH67 glucuronidases, and the amino acids for discriminating the 4- O -methyl group of glucuronic acid were widely conserved in the primary sequences of the GH67 family, suggesting that the 4- O -methyl group is critical for the activities of the GH67 family.

journal of applied glycoscience

4-&lt;i&gt;O&lt;/i&gt;-Methyl Modifications of Glucuronic Acids in Xylans Are Indispensable for Substrate Discrimination by GH67 α-Glucuronidase from &lt;i&gt;Bacillus halodurans&lt;/i&gt; C-125