title: Inverting character of family GH115 α-glucuronidases.
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 (1)H NMR spectroscopy and reduced aldopentaouronic acid (MeGlcA(3)Xyl(4)-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.
authors.affiliation: Institute of Chemistry, Center for Glycomics, Slovak Academy of Sciences, Bratislava, Slovakia.
authors.forename: Katarína
authors.initials: K
authors.lastname: Kolenová
authors.forename: Olena
authors.initials: O
authors.lastname: Ryabova
authors.forename: Mária
authors.initials: M
authors.lastname: Vrsanská
authors.forename: Peter
authors.initials: P
authors.lastname: Biely
mesh_terms: D006026:Glycoside Hydrolases / Q000737:chemistry / Q000378:metabolism*; D006868:Hydrolysis; D019906:Nuclear Magnetic Resonance, Biomolecular; D010802:Phylogeny; D010843:Pichia / Q000201:enzymology*; D012567:Schizophyllum / Q000201:enzymology*; D013379:Substrate Specificity; D014934:Wood / Q000382:microbiology*
chemical_list: D006026:Glycoside Hydrolases; C096734:alpha-glucuronidase