Inverting character of family GH115 α-glucuronidases

Kolenová, Katarína; Ryabova, Olena; Vršanská, Mária; Biely, Peter

doi:10.1016/j.febslet.2010.08.031

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Volume 584, Issue 18 , Pages 4063-4068, 24 September 2010

Inverting character of family GH115 α-glucuronidases

Edited by Judit Ovádi

Institute of Chemistry, Center for Glycomics, Slovak Academy of Sciences, Dúbravská cesta 9, 845 38 Bratislava, Slovakia

Received 1 June 2010; received in revised form 21 July 2010; accepted 19 August 2010. published online 30 August 2010.

Abstract

α-Glucuronidases of glycoside hydrolase family 115 of the xylose-fermenting yeast Pichia stipitis and wood-destroying fungus Schizophyllum commune liberate 4-O-methyl-d-glucuronic acid residues from aldouronic acids and glucuronoxylan. The specific activities of both enzymes depended on polymerization degree of the acidic xylooligosaccharides and were inhibited by linear β-1,4-xylooligosaccharides. These results suggest interaction of the enzyme with several xylopyranosyl residues of the xylan main chain. Using ¹H NMR spectroscopy and reduced aldopentaouronic acid (MeGlcA³Xyl₄-ol) as a substrate, it was found that both enzymes are inverting glycoside hydrolases releasing 4-O-methyl-d-glucuronic acid (MeGlcA) as its β-anomer.

Abbreviations: MeGlcA, 4-O-Methyl-d-glucuronic acid, GH, Glycoside hydrolase

Keywords: α-Glucuronidase, Inverting glycoside hydrolase, ¹H NMR spectroscopy, Pichia stipitis, Schizophyllum commune