Cleavage of the outer membrane protein OmpX by protealysin regulates Serratia proteamaculans invasion
Sign Up to like & getrecommendations! Published in 2020 at "FEBS Letters"
DOI: 10.1002/1873-3468.13897
Abstract: Protealysin is a thermolysin‐like protease of Serratia proteamaculans capable of specifically cleaving actin, which correlates with the invasive activity of these bacteria. Here, we show that inactivation of the protealysin gene does not inhibit invasion… read more here.
Keywords: serratia proteamaculans; protein ompx; protealysin; outer membrane ... See more keywords
Activity modulation of the oligopeptidase B from Serratia proteamaculans by site-directed mutagenesis of amino acid residues surrounding catalytic triad histidine.
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DOI: 10.1016/j.biochi.2017.05.013
Abstract: Oligopeptidase B (OpdB; EC 3.4.21.83) is a trypsin-like peptidase belonging to the family of serine prolyl oligopeptidases; two-domain structure of the enzyme includes C-terminal peptidase catalytic domain and N-terminal seven-bladed β-propeller domain. Importance of the… read more here.
Keywords: serratia proteamaculans; amino acid; surrounding catalytic; catalytic triad ... See more keywords
Identification and Characterization of a New Serratia proteamaculans Strain That Naturally Produces Significant Amount of Extracellular Laccase
Sign Up to like & getrecommendations! Published in 2022 at "Frontiers in Microbiology"
DOI: 10.3389/fmicb.2022.878360
Abstract: Natural biodegradation processes hold promises for the conversion of agro-industrial lignocellulosic biomaterials into biofuels and fine chemicals through lignin-degrading enzymes. The high cost and low stability of these enzymes remain a significant challenge to economic… read more here.
Keywords: significant amount; identification characterization; serratia proteamaculans; strain naturally ... See more keywords