Probing the Role of Sigma π Interaction and Energetics in the Catalytic Efficiency of Endo-1,4-β-Xylanase

Raushan Kumar Singh; Manish Kumar Tiwari; In-Won Kim; Zhilei Chen; Jung-Kul Lee

Probing the Role of Sigma π Interaction and Energetics in the Catalytic Efficiency of Endo-1,4-β-Xylanase

Raushan Kumar Singh, Manish Kumar Tiwari, In-Won Kim, Zhilei Chen^*, Jung-Kul Lee^*

^*Corresponding author for this work

Department of Chemistry

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.

Original language	English
Journal	Applied and Environmental Microbiology
ISSN	0099-2240
Publication status	Published - 2012

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title = "Probing the Role of Sigma π Interaction and Energetics in the Catalytic Efficiency of Endo-1,4-β-Xylanase",

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.",

author = "Singh, {Raushan Kumar} and Tiwari, {Manish Kumar} and In-Won Kim and Zhilei Chen and Jung-Kul Lee",

year = "2012",

language = "English",

journal = "Applied and Environmental Microbiology",

issn = "0099-2240",

publisher = "American Society for Microbiology",

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T1 - Probing the Role of Sigma π Interaction and Energetics in the Catalytic Efficiency of Endo-1,4-β-Xylanase

AU - Singh, Raushan Kumar

AU - Tiwari, Manish Kumar

AU - Kim, In-Won

AU - Chen, Zhilei

AU - Lee, Jung-Kul

PY - 2012

Y1 - 2012

N2 - 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.

AB - 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.

M3 - Journal article

SN - 0099-2240

JO - Applied and Environmental Microbiology

JF - Applied and Environmental Microbiology

ER -

Probing the Role of Sigma π Interaction and Energetics in the Catalytic Efficiency of Endo-1,4-β-Xylanase

Abstract

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