title: Contribution of salt bridges to alkaliphily of Bacillus alkaline xylanase.
abstract: Xylanase J (XynJ) from alkaliphilic Bacillussp. strain 41M-1 is an alkaline xylanase. Structure comparison indicated that there were several specific salt bridges in the catalytic cleft of XynJ compared with neutral xylanases. Mutant enzymes were prepared by substituting several amino acids comprising the salt bridges. Some mutants exhibited acidophilic shift in optimum pH, whereas another showed alkaliphilic shift. These results suggested that the characteristic salt bridges could contribute to the alkaliphily of XynJ.
authors.affiliation: Department of Bioengineering, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 226-8501, Japan.
authors.forename: Hirohito
authors.initials: H
authors.lastname: Umemoto
authors.lastname: Ihsanawati
authors.forename: Mayuko
authors.initials: M
authors.lastname: Inami
authors.forename: Rie
authors.initials: R
authors.lastname: Yatsunami
authors.forename: Toshiaki
authors.initials: T
authors.lastname: Fukui
authors.forename: Takashi
authors.initials: T
authors.lastname: Kumasaka
authors.forename: Nobuo
authors.initials: N
authors.lastname: Tanaka
authors.forename: Satoshi
authors.initials: S
authors.lastname: Nakamura
mesh_terms: D001407:Bacillus / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D043364:Endo-1,4-beta Xylanases / Q000737:chemistry* / Q000235:genetics; D006863:Hydrogen-Ion Concentration; D016297:Mutagenesis, Site-Directed; D012492:Salts / Q000737:chemistry
chemical_list: D001426:Bacterial Proteins; D012492:Salts; D043364:Endo-1,4-beta Xylanases