Article ; Online: Molecular basis for the increased activity of ZMS-2 serine protease in the presence of metal ions and hydrogen peroxide.
Journal of inorganic biochemistry
2024 Volume 256, Page(s) 112566
Abstract: Serine proteases are important enzymes widely used in commercial products and industry. Recently, we identified a new serine protease from the desert bacterium Bacillus subtilis ZMS-2 that showed enhanced activity in the presence of ... ...
Abstract | Serine proteases are important enzymes widely used in commercial products and industry. Recently, we identified a new serine protease from the desert bacterium Bacillus subtilis ZMS-2 that showed enhanced activity in the presence of Zn |
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MeSH term(s) | Hydrogen Peroxide/chemistry ; Bacillus subtilis/enzymology ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Bacterial Proteins/genetics ; Zinc/chemistry ; Zinc/metabolism ; Serine Proteases/metabolism ; Serine Proteases/chemistry ; Serine Proteases/genetics ; Silver/chemistry ; Amino Acid Sequence |
Chemical Substances | Hydrogen Peroxide (BBX060AN9V) ; Bacterial Proteins ; Zinc (J41CSQ7QDS) ; Serine Proteases (EC 3.4.-) ; Silver (3M4G523W1G) |
Language | English |
Publishing date | 2024-04-21 |
Publishing country | United States |
Document type | Journal Article ; Research Support, Non-U.S. Gov't |
ZDB-ID | 162843-4 |
ISSN | 1873-3344 ; 0162-0134 |
ISSN (online) | 1873-3344 |
ISSN | 0162-0134 |
DOI | 10.1016/j.jinorgbio.2024.112566 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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