Contribution of salt bridges to alkaliphily of Bacillusalkaline xylanase | Zendy

Hitoshi Umemoto | Zendy; Ihsanawati Ihsanawati | Zendy; Masaki Inami | Zendy; Rie Yatsunami | Zendy; Toshiaki Fukui | Zendy; Takashi Kumasaka | Zendy; Nobuyuki Tanaka | Zendy; Seiji Nakamura | Zendy

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Contribution of salt bridges to alkaliphily of Bacillusalkaline xylanase

Author(s) -

Hitoshi Umemoto,

Ihsanawati Ihsanawati,

Masaki Inami,

Rie Yatsunami,

Toshiaki Fukui,

Takashi Kumasaka,

Nobuyuki Tanaka,

Seiji Nakamura

Publication year - 2007

Publication title -

nucleic acids symposium series

Language(s) - English

Resource type - Journals

eISSN - 1746-8272

pISSN - 0261-3166

DOI - 10.1093/nass/nrm231

Subject(s) - xylanase , salt (chemistry) , mutant , chemistry , enzyme , strain (injury) , biochemistry , food science , biology , organic chemistry , anatomy , gene

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.

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