An oxalate decarboxylase-like cupin domain containing protein is involved in imparting acid stress tolerance in Bacillus amyloliquefaciens MBNC-Reference-Cited by-同舟云学术

An oxalate decarboxylase-like cupin domain containing protein is involved in imparting acid stress tolerance in Bacillus amyloliquefaciens MBNC

Published:2024-01-08 Issue:2 Volume:40 Page:
ISSN:0959-3993
Container-title:World Journal of Microbiology and Biotechnology
language:en
Short-container-title:World J Microbiol Biotechnol

Author:

Chowdhury Naimisha,Naorem Romen Singh,Hazarika Dibya Jyoti,Goswami Gunajit,Dasgupta Abhisek,Bora Sudipta Sankar,Boro Robin Chandra,Barooah Madhumita^ORCID

Funder

Department of Biotechnology, Ministry of Science and Technology, India

Publisher

Springer Science and Business Media LLC

Link

https://link.springer.com/content/pdf/10.1007/s11274-023-03870-3.pdf

Reference59 articles.

1. Botella E, Devine SK, Hubner S et al (2014) PhoR autokinase activity is controlled by an intermediate in wall teichoic acid metabolism that is sensed by the intracellular PAS domain during the PhoPR-mediated phosphate limitation response of Bacillus subtilis. Mol Microbiol 94:1242–1259. https://doi.org/10.1111/mmi.12833

2. Chao Y, Lahodzich AV (2021) Analysis of the efficiency factors of electrotransformation of Bacillus subtilis to inactivate the aroK gene by the method of homologous recombination. J Belarusian State Univ Biol 2:64–73

3. Chowdhury N, Goswami G, Boro RC, Barooah M (2021) A pH-dependent gene expression enables Bacillus amyloliquefaciens MBNC to adapt to acid stress. Curr Microbiol 78:3104–3114. https://doi.org/10.1007/s00284-021-02573-y

4. Conter C, Oppici E, Dindo M et al (2019) Biochemical properties and oxalate-degrading activity of oxalate decarboxylase from Bacillus subtilis at neutral pH. IUBMB Life iu(2027). https://doi.org/10.1002/iub.2027

5. Davies JS, Coombes D, Horne CR et al (2019) Functional and solution structure studies of amino sugar deacetylase and deaminase enzymes from Staphylococcus aureus. FEBS Lett 593:52–66. https://doi.org/10.1002/1873-3468.13289