Probing the Role of Sigma p Interaction and Energetics in the Catalytic Efficiency of Endo-1,4-[Beta]-Xylanase

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 affect...

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Bibliographic Details
Published in:Applied and environmental microbiology 2012-12, Vol.78 (24), p.8817
Main Authors: Singh, Raushan Kumar, Tiwari, Manish Kumar, Kim, In-Won, Chen, Zhilei, Lee, Jung-Kul
Format: Article
Language:English
Subjects:
Amino acids
Catalysis
Enzymes
Fungi
Microbiology
Online Access:Get full text
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Summary: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. [PUBLICATION ABSTRACT]
ISSN:0099-2240
1098-5336