@article{e4c7762254c348fc9676f619b08f0f5e,
title = "Catalytic thiol and carboxylate: Role of cysteine and glutamic acid in the xylosidic activity of endoxylanase from Chainia sp. (NCL 82-5-1)",
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.",
keywords = "Chainia sp., Chemical modification, Endoxylanase, Substrate protection",
author = "Subray, {S. Hegde} and Ameeta, {R. Kumar} and Krishna, {N. Ganesh} and Khan, {Islam M.}",
note = "Funding Information: Authors thank Dr. R. P. Roy, National Institute of Immunology, New Delhi, for his help in carrying out the CD analysis. We acknowledge National Facility for protein sequencing, IIT, Bombay, and Professor A. K Lala for peptide sequencing. We also thank Dr. V. Shankar for his useful suggestions and critical reading of the manuscript. Financial assistance to S.S.H. and A.R.K. in the form of a fellowship from the Council of Scientific and Industrial Research (CSIR), India, is gratefully acknowledged. This work was carried out as part of an ongoing protein engineering project to K.N.G. and M.I.K. sponsored by the Department of BioTechnology (DBT) and CSIR (India).",
year = "1998",
month = jul,
day = "15",
doi = "10.1006/abbi.1998.0729",
language = "English (US)",
volume = "355",
pages = "153--159",
journal = "Archives of Biochemistry and Biophysics",
issn = "0003-9861",
publisher = "Academic Press Inc.",
number = "2",
}