3.4.23.49: omptin
This is an abbreviated version!
For detailed information about omptin, go to the full flat file.
Word Map on EC 3.4.23.49
-
3.4.23.49
-
furin
-
usp7
-
ubiquitin-specific
-
endoproteolytic
-
convertase
-
proproteins
-
deubiquitinating
-
prohormone
-
subtilisin-like
-
dibasic
-
yersinia
-
pestis
-
deubiquitinase
-
trans-golgi
-
propeptide
-
farnesylated
-
subtilisins
-
plague
-
kex2-like
-
lys-arg
-
proinsulins
-
prelamin
-
proregions
-
furin-like
-
flexneri
-
monobasic
-
deubiquitylation
-
exoprotease
-
zmpste24
-
isoprenylated
-
arg-arg
-
pharmacology
-
food industry
-
biotechnology
-
medicine
- 3.4.23.49
- furin
- usp7
-
ubiquitin-specific
-
endoproteolytic
-
convertase
- proproteins
-
deubiquitinating
-
prohormone
-
subtilisin-like
-
dibasic
- yersinia
- pestis
-
deubiquitinase
-
trans-golgi
- propeptide
-
farnesylated
- subtilisins
- plague
-
kex2-like
- lys-arg
- proinsulins
-
prelamin
-
proregions
-
furin-like
- flexneri
-
monobasic
-
deubiquitylation
-
exoprotease
- zmpste24
-
isoprenylated
- arg-arg
- pharmacology
- food industry
- biotechnology
- medicine
Reaction
Has a virtual requirement for Arg in the P1 position and a slightly less stringent preference for this residue in the P1' position, which can also contain Lys, Gly or Val. =
Synonyms
bacterial outer-membrane protease, Citrobacter rodentium outer-membrane protease, CroP, E. coli protease VII, EC 3.4.21.87, endoprotease, Gene ompT proteins, More, OmpP, OmpP protease, ompT, OmpT protease, OmpT protein, Omptin, omptin protease, outer membrane protease, Outer membrane protein 3B, outer-membrane protease, outer-membrane protease T, PgtE, Pla, plaA, protease 7, Protease A, Protease VII, Protein a, Proteins, specific or class, gene ompT, SopA
ECTree
Advanced search results
Inhibitors
Inhibitors on EC 3.4.23.49 - omptin
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
calf thymus histone H2B
-
growth inhibitory activity against bacterial gene expressing Escherichia coli with calculated 50% growth inhibitory concentrations of 3.8 microM. Histone H2B penetrates the cell membrane of JCM5491 OmpT+ cells
-
calf thymus histone H3
-
growth inhibitory activity against bacterial gene expressing Escherichia coli with calculated 50% growth inhibitory concentrations of 10 microM. Histones H3 and H4 remain on the cell surface and subsequently disrupt the cell membrane structure with bleb formation in a manner similar to general antimicrobial peptides
-
calf thymus histone H4
-
growth inhibitory activity against bacterial gene expressing Escherichia coli with calculated 50% growth inhibitory concentrations of 12.7 microM. Histones H3 and H4 remain on the cell surface and subsequently disrupt the cell membrane structure with bleb formation in a manner similar to general antimicrobial peptides
-
-
classical protease inhibitors are ineffective against CroP activity, but the serine protease inhibitor aprotinin displays inhibitory potency in the micromolar range. Aprotinin acts as a competitive inhibitor of CroP activity and interferes with the cleavage of the murine cathelicidin-related antimicrobial peptide. Structural model of the aprotinin-omptin complex in which Lys15 of aprotinin forms salt bridges with conserved negatively charged residues of the omptin active site, molecular docking, overview. Aprotinin inhibits CRAMP proteolytic degradation by CroP. Docking model of the aprotinin-omptin complex. Lys15 of aprotinin interacts with Glu27 and Asp208 (OmpT numbering), which are the two negatively charged residues that form the S1 specificity pocket of omptins
Aprotinin
ability of EHEC EDL933 cells to cleave the FRET substrate in the presence of increasing concentrations of aprotinin, about 90% inhibition at 0.2 mM. Docking model of the aprotinin-omptin complex. Lys15 of aprotinin interacts with Glu27 and Asp208 (OmpT numbering), which are the two negatively charged residues that form the S1 specificity pocket of omptin
diisopropylfluorophosphate
-
significant inhibition only at high concentrations
-
i.e. LPS, rough, dependent on, interacts with the beta-barrel in the outer membrane, function and mechanism overview, smooth LPS sterically inhibits the enzyme via its O-side chain
lipopolysaccharide
-
i.e. LPS, rough, dependent on, interacts with the beta-barrel in the outer membrane, function and mechanism overview, smooth LPS sterically inhibits the enzyme via its O-side chain
lipopolysaccharide
-
i.e. LPS, rough, dependent on, interacts with the beta-barrel in the outer membrane, function and mechanism overview, smooth LPS sterically inhibits the enzyme via its O-side chain
lipopolysaccharide
-
i.e. LPS, rough, dependent on, interacts with the beta-barrel in the outer membrane, function and mechanism overview, smooth LPS sterically inhibits the enzyme via its O-side chain
lipopolysaccharide
-
i.e. LPS, rough, dependent on, interacts with the beta-barrel in the outer membrane, function and mechanism overview, smooth LPS sterically inhibits the enzyme via its O-side chain
additional information
molecular docking study with protease inhibitors, overview. No interaction with lopinavir and tipranavir
-