Catalytic thiol and carboxylate: Role of cysteine and glutamic acid in the xylosidic activity of endoxylanase from Chainia sp. (NCL 82-5-1)

S. Hegde Subray, R. Kumar Ameeta, N. Ganesh Krishna, Islam M. Khan

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)153-159
Number of pages7
JournalArchives of Biochemistry and Biophysics
Volume355
Issue number2
DOIs
StatePublished - Jul 15 1998
Externally publishedYes

Keywords

  • Chainia sp.
  • Chemical modification
  • Endoxylanase
  • Substrate protection

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

Fingerprint Dive into the research topics of 'Catalytic thiol and carboxylate: Role of cysteine and glutamic acid in the xylosidic activity of endoxylanase from Chainia sp. (NCL 82-5-1)'. Together they form a unique fingerprint.

Cite this