2011
DOI: 10.1074/jbc.m110.215962
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Abstract: 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… Show more

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Cited by 87 publications
(87 citation statements)
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“…By contrast, the mechanism by which AXHd3 arabinofuranosidases not only accommodate a double substitution but also display absolute specificity for such structures is unknown. A distinctive feature of GH43 is that the active site of the β-xylosidases and arabinofuranosidases are highly conserved (10) (Fig. S1), consistent with the observation that β-xylosidases and some arabinofuranosidases are capable of also cleaving α-arabinofuranosyl and β-xylopyranosyl linkages, respectively (12,15) .…”
Section: For Review)supporting
confidence: 54%
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“…By contrast, the mechanism by which AXHd3 arabinofuranosidases not only accommodate a double substitution but also display absolute specificity for such structures is unknown. A distinctive feature of GH43 is that the active site of the β-xylosidases and arabinofuranosidases are highly conserved (10) (Fig. S1), consistent with the observation that β-xylosidases and some arabinofuranosidases are capable of also cleaving α-arabinofuranosyl and β-xylopyranosyl linkages, respectively (12,15) .…”
Section: For Review)supporting
confidence: 54%
“…The active site of GH43 β-Dxylosidases and α-L-arabinofuranosidases are highly conserved (10), and thus it is not clear how these enzymes select β-D-xylosyl and α-L-arabinofuranosyl linkages, respectively, in natural substrates. It is possible that this flexibility in substrate recognition could be harnessed to introduce novel functionalities into the active site of selected GH43 enzymes.…”
Section: Hiaxhd3mentioning
confidence: 99%
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“…ABFs that release Araf from doubly substituted Xylp are specifically releasing either 1,2-or 1,3-linked given the surfix d2 or d3, respectively (Cartmell et al, 2011;McKee et al, 2012;Pouvreau et al, 2011;Van Laere et al, 1997.…”
Section: Classification Of -L-arabinofuranosidasesmentioning
confidence: 99%
“…The active site topology of ABFs and other debranching enzymes was defined by Cartmell et al (Cartmell et al, 2011) as follows: the scissile bond is between the arabinose decoration at subsite 1 (the active site) and the backbone Xylp at subsite +1. Subsites extended toward the reducing end of the xylan backbone (from the +1 subsite) are defined as +2R, +3R etc., whereas subsites extending toward the non-reducing end of the polymer are designated 2NR, 3NR, and so forth ( Fig.…”
Section: The Active Site Pocketmentioning
confidence: 99%