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The structure and f...
The structure and function of an arabinan-specific alpha-1,2-arabinofuranosidase identified from screening the activities of bacterial GH43 glycoside hydrolases
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Cartmell, Alan (författare)
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- McKee, Lauren, 1985- (författare)
- KTH,Skolan för bioteknologi (BIO),University of Georgia, United States
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Pena, Maria J. (författare)
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- Larsbrink, Johan (författare)
- KTH,Glykovetenskap
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- Brumer, Harry (författare)
- KTH,Glykovetenskap
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Kaneko, Satoshi (författare)
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Ichinose, Hitomi (författare)
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Lewis, Richard J. (författare)
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Vikso-Nielsen, Anders (författare)
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Gilbert, Harry J. (författare)
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Marles-Wright, Jon (författare)
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(creator_code:org_t)
- American Society for Biochemistry and Molecular Biology, 2011
- 2011
- Engelska.
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Ingår i: Journal of Biological Chemistry. - : American Society for Biochemistry and Molecular Biology. - 0021-9258 .- 1083-351X. ; 286:17
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Reflecting the diverse chemistry of plant cell walls, microorganisms that degrade these composite structures synthesize an array of glycoside hydrolases. These enzymes are organized into sequence-, mechanism-, and structure-based families. Genomic data have shown that several organisms that degrade the plant cell wall contain a large number of genes encoding family 43 (GH43) glycoside hydrolases. Here we report the biochemical properties of the GH43 enzymes of a saprophytic soil bacterium, Cellvibrio japonicus, and a human colonic symbiont, Bacteroides thetaiotaomicron. The data show that C. japonicus uses predominantly exo-acting enzymes to degrade arabinan into arabinose, whereas B. thetaiotaomicron deploys a combination of endo-and side chain-cleaving glycoside hydrolases. Both organisms, however, utilize an arabinan-specific alpha-1,2-arabinofuranosidase in the degradative process, an activity that has not previously been reported. The enzyme can cleave alpha-1,2-arabinofuranose decorations in single or double substitutions, the latter being recalcitrant to the action of other arabinofuranosidases. The crystal structure of the C. japonicus arabinan-specific alpha-1,2-arabinofuranosidase, CjAbf43A, displays a five-bladed beta-propeller fold. The specificity of the enzyme for arabinan is conferred by a surface cleft that is complementary to the helical backbone of the polysaccharide. The specificity of CjAbf43A for alpha-1,2-L-arabinofuranose side chains is conferred by a polar residue that orientates the arabinan backbone such that O2 arabinose decorations are directed into the active site pocket. A shelflike structure adjacent to the active site pocket accommodates O3 arabinose side chains, explaining how the enzyme can target O2 linkages that are components of single or double substitutions.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
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Cartmell, Alan
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McKee, Lauren, 1 ...
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Pena, Maria J.
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Larsbrink, Johan
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Brumer, Harry
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Kaneko, Satoshi
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visa fler...
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Ichinose, Hitomi
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Lewis, Richard J ...
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Vikso-Nielsen, A ...
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Gilbert, Harry J ...
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Marles-Wright, J ...
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visa färre...
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