Literature DB >> 18029786

Contribution of salt bridges to alkaliphily of Bacillus alkaline xylanase.

Hirohito Umemoto1, Mayuko Inami, Rie Yatsunami, Toshiaki Fukui, Takashi Kumasaka, Nobuo Tanaka, Satoshi Nakamura.   

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.

Entities:  

Mesh:

Substances:

Year:  2007        PMID: 18029786     DOI: 10.1093/nass/nrm231

Source DB:  PubMed          Journal:  Nucleic Acids Symp Ser (Oxf)        ISSN: 0261-3166


  1 in total

1.  Improvement of alkalophilicity of an alkaline xylanase Xyn11A-LC from Bacillus sp. SN5 by random mutation and Glu135 saturation mutagenesis.

Authors:  Wenqin Bai; Yufan Cao; Jun Liu; Qinhong Wang; Zhenhu Jia
Journal:  BMC Biotechnol       Date:  2016-11-08       Impact factor: 2.563

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.