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.
authors.affiliation: Department of Chemical Engineering, Konkuk University, Seoul, South Korea.
authors.forename: Raushan Kumar
authors.initials: RK
authors.lastname: Singh
authors.forename: Manish Kumar
authors.initials: MK
authors.lastname: Tiwari
authors.forename: In-Won
authors.initials: IW
authors.lastname: Kim
authors.forename: Zhilei
authors.initials: Z
authors.lastname: Chen
authors.forename: Jung-Kul
authors.initials: JK
authors.lastname: Lee
mesh_terms: D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000596:Amino Acids / Q000235:genetics / Q000378:metabolism; D020134:Catalytic Domain; D002597:Chaetomium / Q000201:enzymology*; D043364:Endo-1,4-beta Xylanases / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D008958:Models, Molecular; D008969:Molecular Sequence Data
chemical_list: D000596:Amino Acids; D043364:Endo-1,4-beta Xylanases