Chaetomium globosum endo-1,4-β-xylanase (XylCg) is distinguished from other xylanases by its high turnover rate (1,860 s(-1)), the highest ever reported for fungal xylanases. One conserved amino acid, W48, in the substrate binding pocket of wild-type XylCg was identified as an important residue affecting XylCg's catalytic efficiency.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3502898 | PMC |
| http://dx.doi.org/10.1128/AEM.02261-12 | DOI Listing |
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