| Inverting character of family GH115 α-glucuronidases. | |
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MedLine Citation:
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PMID: 20804758 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Katarína Kolenová; Olena Ryabova; Mária Vrsanská; Peter Biely |
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Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't Date: 2010-09-07 |
Journal Detail:
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Title: FEBS letters Volume: 584 ISSN: 1873-3468 ISO Abbreviation: FEBS Lett. Publication Date: 2010 Sep |
Date Detail:
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Created Date: 2010-09-27 Completed Date: 2010-10-21 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0155157 Medline TA: FEBS Lett Country: Netherlands |
Other Details:
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Languages: eng Pagination: 4063-8 Citation Subset: IM |
Copyright Information:
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Copyright © 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. |
Affiliation:
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Institute of Chemistry, Center for Glycomics, Slovak Academy of Sciences, Bratislava, Slovakia. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Glycoside Hydrolases
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chemistry,
metabolism* Hydrolysis Nuclear Magnetic Resonance, Biomolecular Phylogeny Pichia / enzymology* Schizophyllum / enzymology* Substrate Specificity Wood / microbiology* |
| Chemical | |
Reg. No./Substance:
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EC 3.2.1.-/Glycoside Hydrolases; EC 3.2.1.139/alpha-glucuronidase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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