PMID: 9194164Apr 1, 1997Paper

Asparagine-127 of xylanase A from Streptomyces lividans, a key residue in glycosyl hydrolases of superfamily 4/7: kinetic evidence for its involvement in stabilization of the catalytic intermediate

Protein Engineering
M RobergeD Kluepfel

Abstract

Site-directed mutagenesis of asparagine-127 (N127) of xylanase A (XlnA) from Streptomyces lividans, belonging to family 10 and superfamily 4/7 of glycosyl hydrolases, was chosen to study the role of this conserved residue. The isosteric mutation N127D introduced did not affect the fold of XlnA as revealed by circular dichroism. Comparison of the kinetic constants of N127D and wild-type XlnA revealed a 70-fold decrease in the specificity constant (kcat/K(M)) towards birchwood xylan, which is attributed solely to the difference in the kcat value and indicates a role of N127 in stabilization of the catalytic intermediate. N127 also plays a role in maintaining the ionization states of the two catalytic residues, as shown by the modified pH profile of XlnA-N127D. Characterization of XlnA-N127D and the analysis of the three-dimensional structure of XlnA converge towards a stabilization role for N127 in the catalytic site of XlnA.

Citations

Oct 29, 1998·Protein Science : a Publication of the Protein Society·A SchmidtC Kratky
Jul 6, 2010·Applied Biochemistry and Biotechnology·Zidong XuPingkai Ouyang
Jul 28, 1999·FEMS Microbiology Reviews·N KulkarniM Rao
Sep 28, 2000·Current Opinion in Chemical Biology·C S Rye, S G Withers
Jun 29, 2000·Annual Review of Biochemistry·H D Ly, S G Withers
Oct 20, 2005·Journal of Bioscience and Bioengineering·Mamoru NishimotoKiyoshi Hayashi
Jan 5, 2002·DNA Sequence : the Journal of DNA Sequencing and Mapping·A HernándezJ Soliveri
Jul 29, 2017·International Journal of Microbiology·Hind Al-DarkazaliSuthep Wiyakrutta
Nov 21, 2007·Applied Biochemistry and Biotechnology·Ahmed Jawaard AfzalKhawar Sohail Siddiqui
Feb 8, 2011·Journal of Agricultural and Food Chemistry·Xiangfei SongXixi Wu

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