Inverting character of family GH115 α-glucuronidases.
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.
Kolenová
Katarína
K
Institute of Chemistry, Center for Glycomics, Slovak Academy of Sciences, Bratislava, Slovakia.
Ryabova
Olena
O
Vrsanská
Mária
M
Biely
Peter
P
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*
D006026:Glycoside Hydrolases; C096734:alpha-glucuronidase