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
Specific Activity
Specific Activity 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.
additional information
additional information
comparative proteome analysis of chloramphenicol-resistant Escherichia coli, two-dimensional electrophoresis, MALDI-TOF mass spectroscopy and Western blotting performed, differential protein expression profiles with and without chloramphenicol treatment shown, antimicrobial susceptibility tested, OmpT protease identified as critically altered protein in chloramphenicol-resistant Escherichia coli, mutant analysis performed
additional information
effects of OmpT protease on colony-forming ability and production of fibrous protein polymers determined, involvement of OmpT protease in protein quality control within the cell discussed
additional information
phage display applied to analyse substrate specificity of OmpP protease in comparison to OmpT protease, different substrate specificities between OmpP and OmpT proteases determined and discussed as important for inactivation of cationic antimicrobial peptides, cleavage products determined by mass spectrometry, sequence comparison and structural models of OmpP and OmpT proteins shown, effects of ompP and ompT protein on protamine resistance determined
additional information
phage display applied to analyse substrate specificity of OmpP protease in comparison to OmpT protease, different substrate specificities between OmpP and OmpT proteases determined and discussed as important for inactivation of cationic antimicrobial peptides, cleavage products determined by mass spectrometry, sequence comparison and structural models of OmpP and OmpT proteins shown, effects of ompP and ompT protein on protamine resistance determined
additional information
-
phage display applied to analyse substrate specificity of OmpP protease in comparison to OmpT protease, different substrate specificities between OmpP and OmpT proteases determined and discussed as important for inactivation of cationic antimicrobial peptides, cleavage products determined by mass spectrometry, sequence comparison and structural models of OmpP and OmpT proteins shown, effects of ompP and ompT protein on protamine resistance determined
additional information
phage display applied to analyse substrate specificity of OmpT protease in comparison to OmpP protease, different substrate specificities between OmpT and OmpP proteases determined and discussed as important for inactivation of cationic antimicrobial peptides, cleavage products determined by mass spectrometry, sequence comparison and structural models of OmpP and OmpT proteins shown, effects of ompP and ompT protein on protamine resistance determined
additional information
phage display applied to analyse substrate specificity of OmpT protease in comparison to OmpP protease, different substrate specificities between OmpT and OmpP proteases determined and discussed as important for inactivation of cationic antimicrobial peptides, cleavage products determined by mass spectrometry, sequence comparison and structural models of OmpP and OmpT proteins shown, effects of ompP and ompT protein on protamine resistance determined
additional information
-
phage display applied to analyse substrate specificity of OmpT protease in comparison to OmpP protease, different substrate specificities between OmpT and OmpP proteases determined and discussed as important for inactivation of cationic antimicrobial peptides, cleavage products determined by mass spectrometry, sequence comparison and structural models of OmpP and OmpT proteins shown, effects of ompP and ompT protein on protamine resistance determined
additional information
strains expressing OmpT protease shown to cleave colicin E1 at the residues K84 and K95 in the N-terminal translocation domain, leading to the removal of the TolQA box essential for cytotoxicity of colicin E1, in vivo data indicating effects of OmpT protease on colicin E1 cell-killing activity shown
additional information
structural and functional relationships for wild-type and mutated OmpT proteins investigated, relevant case of the Michaelis complex of the outer-membrane protease T (OmpT) analyzed by a hybrid molecular mechanics/coarse-grained (MM/CG) approach, structural explanation for decreased catalytic activity of the mutants S99A and H212A given
additional information
-
structural and functional relationships for wild-type and mutated OmpT proteins investigated, relevant case of the Michaelis complex of the outer-membrane protease T (OmpT) analyzed by a hybrid molecular mechanics/coarse-grained (MM/CG) approach, structural explanation for decreased catalytic activity of the mutants S99A and H212A given
additional information
studies on development of a new substrate phage system, construction of a random hexapeptide library described, selection of the phage display library with OmpT protease to demonstrate application of the infectivity-modulated phage display IMOP