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.

SUBMITTER: Singh RK 

PROVIDER: S-EPMC3502898 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature