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Structural and func...
Structural and functional investigation of a fungal member of carbohydrate esterase family 15 with potential specificity for rare xylans
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- Mazurkewich, Scott, 1982 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Scholzen, Karoline (author)
- Köpenhamns universitet,University of Copenhagen
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- Brusch, Rikke (author)
- Köpenhamns universitet,University of Copenhagen
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- Poulsen, Jens-Christian N (author)
- Köpenhamns universitet,University of Copenhagen
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- Theibich, Yusuf (author)
- Köpenhamns universitet,University of Copenhagen
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- Hüttner, Silvia, 1984 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Olsson, Lisbeth, 1963 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Larsbrink, Johan, 1982 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Leggio, Leila Lo (author)
- Köpenhamns universitet,University of Copenhagen
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(creator_code:org_t)
- 2023
- 2023
- English.
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In: Acta Crystallographica Section D: Structural Biology. - 2059-7983. ; 79, s. 545-555
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Abstract
Subject headings
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- In plant cell walls, covalent bonds between polysaccharides and lignin increase recalcitrance to degradation. Ester bonds are known to exist between glucuronic acid moieties on glucuronoxylan and lignin, and these can be cleaved by glucuronoyl esterases (GEs) from carbohydrate esterase family 15 (CE15). GEs are found in both bacteria and fungi, and some microorganisms also encode multiple GEs, although the reason for this is still not fully clear. The fungus Lentithecium fluviatile encodes three CE15 enzymes, of which two have previously been heterologously produced, although neither was active on the tested model substrate. Here, one of these, Lf CE15C, has been investigated in detail using a range of model and natural substrates and its structure has been solved using X-ray crystallography. No activity could be verified on any tested substrate, but biophysical assays indicate an ability to bind to complex carbohydrate ligands. The structure further suggests that this enzyme, which possesses an intact catalytic triad, might be able to bind and act on more extensively decorated xylan chains than has been reported for other CE15 members. It is speculated that rare glucuronoxylans decorated at the glucuronic acid moiety may be the true targets of Lf CE15C and other CE15 family members with similar sequence characteristics.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
- NATURVETENSKAP -- Biologi -- Strukturbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Structural Biology (hsv//eng)
- TEKNIK OCH TEKNOLOGIER -- Industriell bioteknik -- Biokatalys och enzymteknik (hsv//swe)
- ENGINEERING AND TECHNOLOGY -- Industrial Biotechnology -- Biocatalysis and Enzyme Technology (hsv//eng)
Keyword
- lignocellulose degradation
- hemicellulose
- Lentithecium fluviatile.
- α/β hydrolases
- biomass conversion
- rare xylans
- glucuronyl esterases
Publication and Content Type
- art (subject category)
- ref (subject category)
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- By the author/editor
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Mazurkewich, Sco ...
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Scholzen, Karoli ...
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Brusch, Rikke
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Poulsen, Jens-Ch ...
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Theibich, Yusuf
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Hüttner, Silvia, ...
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show more...
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Olsson, Lisbeth, ...
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Larsbrink, Johan ...
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Leggio, Leila Lo
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show less...
- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Biochemistry and ...
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Structural Biolo ...
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- ENGINEERING AND TECHNOLOGY
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ENGINEERING AND ...
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and Industrial Biote ...
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and Biocatalysis and ...
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Acta Crystallogr ...
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Chalmers University of Technology