1.
Arch Biochem Biophys
; 355(2): 153-9, 1998 Jul 15.
Artigo
em Inglês
| MEDLINE
| ID: mdl-9675021
RESUMO
Chemical modification of the endoxylanase from Chainia sp. with group-specific chemical modifiers in the absence and presence of substrate and kinetics of modification revealed the involvement of a thiol and a carboxylate in the catalytic function of the enzyme. The active-site peptides were chemically labeled and sequenced. The sequence alignment of the chemically labeled peptide with other family G/11 xylanases showed that the catalytic glutamate of Chainia xylanase is located in a highly homologous region and may function as an acid/base catalyst while thiol of the Cys may function as a nucleophile.