Role of arginine in substrate binding and tryptophan microenvironment of endoxylanase from Chainia sp. (NCL 82-5-1)

Subray Hegde, A. R. Kumar, K. N. Ganesh, M. I. Khan

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Chemical modification of the endoxylanase from Chainia sp. with group specific chemical modifiers in the absence and presence of substrate and the kinetics of modification revealed the involvement of a guanidinium group in the catalytic function of the enzyme. The failure of the substrate to quench the fluorescence of the Arg modified enzyme indicates the involvement of Arg in substrate binding. Modification of Trp by N-bromosuccinimide leads to inactivation of the enzyme through peptide cleavage although substrate binding quenches the enzyme fluorescence. Analysis of quenching of enzyme fluorescence by collisional quenchers viz. acrylamide, potassium iodide and cesium chloride suggests that all the Trp residues are located in a similar moderately hydrophobic environment.

Original languageEnglish (US)
Pages (from-to)249-258
Number of pages10
JournalJournal of Biochemistry, Molecular Biology and Biophysics
Volume2
Issue number4
StatePublished - 1999
Externally publishedYes

Fingerprint

Endo-1,4-beta Xylanases
Tryptophan
Arginine
Substrates
Enzymes
Fluorescence
Bromosuccinimide
Potassium Iodide
Potassium Chloride
Acrylamide
Guanidine
Chemical modification
Quenching
Peptides
Kinetics

Keywords

  • Chainia sp.
  • Chemical modification
  • Fluorescence quenching
  • Substrate protection
  • Xylanase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Genetics
  • Molecular Biology

Cite this

Role of arginine in substrate binding and tryptophan microenvironment of endoxylanase from Chainia sp. (NCL 82-5-1). / Hegde, Subray; Kumar, A. R.; Ganesh, K. N.; Khan, M. I.

In: Journal of Biochemistry, Molecular Biology and Biophysics, Vol. 2, No. 4, 1999, p. 249-258.

Research output: Contribution to journalArticle

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AU - Khan, M. I.

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