Probing the role of sigma interaction and energetics in the catalytic efficiency of endo-1,4--xylanase. Academic Article

abstract

• Chaetomium globosum endo-1,4--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

• Chen, Zhilei

published proceedings

• Appl Environ Microbiol

author list (cited authors)

• Singh, R. K., Tiwari, M. K., Kim, I., Chen, Z., & Lee, J.

citation count

• 8

complete list of authors

• Singh, Raushan Kumar||Tiwari, Manish Kumar||Kim, In-Won||Chen, Zhilei||Lee, Jung-Kul

publication date

• December 2012

publisher

• American Society for Microbiology  Publisher

published in

• Applied and Environmental Microbiology  Journal

keywords

• Amino Acid Sequence
• Amino Acid Substitution
• Amino Acids
• Catalytic Domain
• Chaetomium
• Endo-1,4-beta Xylanases
• Kinetics
• Models, Molecular
• Molecular Sequence Data

Digital Object Identifier (DOI)

• 10.1128/AEM.02261-12

URI

• https://hdl.handle.net/1969.1/184529

start page

• 8817

end page

• 8821

volume

• 78

issue

• 24

URL

• http://dx.doi.org/10.1128/aem.02261-12