ArticleJournal of bacteriology2007
Substrate specificity of the Escherichia coli outer membrane protease OmpP.
Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Bio-inspired biomaterial coating for enzyme responsive release of antimicrobial peptides.Materials today. Bio · 2025Article
- A production platform for disulfide-bonded peptides in the periplasm of Escherichia coli.Microbial cell factories · 2024Article
- Protamine cleavage specificity of the avian pathogenFrontiers in veterinary science · 2024Article
- Article
- Omptin Proteases of Enterobacterales Show Conserved Regulation by the PhoPQ Two-Component System but Exhibit Divergent Protection from Antimicrobial Host Peptides and Complement.Infection and immunity · 2023Article
- Serotype-dependent adhesion of Shiga toxin-producingFrontiers in microbiology · 2022Article
- Cellular Self-Digestion and Persistence in Bacteria.Microorganisms · 2021Review
- A Real-Time Thermal Sensor System for Quantifying the Inhibitory Effect of Antimicrobial Peptides on Bacterial Adhesion and Biofilm Formation.Sensors (Basel, Switzerland) · 2021Article
- Role of the lipid bilayer in outer membrane protein folding in Gram-negative bacteria.The Journal of biological chemistry · 2020Review
- A Highly Productive, One-Pot Cell-Free Protein Synthesis Platform Based on Genomically Recoded Escherichia coli.Cell chemical biology · 2019Article
- Identification and characterization of OmpT-like proteases in uropathogenic Escherichia coli clinical isolates.MicrobiologyOpen · 2019Article
- Evaluation of immune response to recombinantIranian journal of veterinary research · 2019Article
- Transcriptional Landscape of aFrontiers in microbiology · 2018Article
- Antimicrobial Peptide Conformation as a Structural Determinant of Omptin Protease Specificity.Journal of bacteriology · 2015Article
- Host defense peptide resistance contributes to colonization and maximal intestinal pathology by Crohn's disease-associated adherent-invasive Escherichia coli.Infection and immunity · 2014Article
- Cloning, expression and purification of binding domains of lethal factor and protective antigen of Bacillus anthracis in Escherichia coli and evaluation of their related murine antibody.Molecular biology reports · 2014Article
- Degradation of C-terminal tag sequences on domain antibodies purified from E. coli supernatant.mAbs · 2014Article
- Fibrinolytic and coagulative activities of Yersinia pestis.Frontiers in cellular and infection microbiology · 2013Review
- A dual tag system for facilitated detection of surface expressed proteins in Escherichia coli.Microbial cell factories · 2012Article
- Molecular adaptation of a plant-bacterium outer membrane protease towards plague virulence factor Pla.BMC evolutionary biology · 2011Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Escherichia coli OmpP is an F episome-encoded outer membrane protease that exhibits 71% amino acid sequence identity with OmpT. These two enzymes cleave substrate polypeptides primarily between pairs of basic amino acids. We found that, like OmpT, purified OmpP is active only in the presence of lipopolysaccharide. With optimal peptide substrates, OmpP exhibits high catalytic efficiency (k(cat)/K(m) = 3.0 x 10(6) M(-1)s(-1)). Analysis of the extended amino acid specificity of OmpP by substrate phage revealed that both Arg and Lys are strongly preferred at the P1 and P1' sites of the enzyme. In addition, Thr, Arg, or Ala is preferred at P2; Leu, Ala, or Glu is preferred at P4; and Arg is preferred at P3'. Notable differences in OmpP and OmpT specificities include the greater ability of OmpP to accept Lys at the P1 or P1', site as well as the prominence of Ser at P3 in OmpP substrates. Likewise, the OmpP P1 site could better accommodate Ser; as a result, OmpP was able to cleave a peptide substrate between Ser-Arg about 120 times more efficiently than was OmpT. Interestingly, OmpP and OmpT cleave peptides with three consecutive Arg residues at different sites, a difference in specificity that might be important in the inactivation of cationic antimicrobial peptides. Accordingly, we show that the presence of an F' episome results in increased resistance to the antimicrobial peptide protamine both in ompT mutants and in wild-type E. coli cells.
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Registered trials
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