| Literature DB >> 23023743 |
Raushan Kumar Singh1, Manish Kumar Tiwari, In-Won Kim, Zhilei Chen, Jung-Kul Lee.
Abstract
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.Entities:
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Year: 2012 PMID: 23023743 PMCID: PMC3502898 DOI: 10.1128/AEM.02261-12
Source DB: PubMed Journal: Appl Environ Microbiol ISSN: 0099-2240 Impact factor: 4.792