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
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3.4.23.49
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furin
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usp7
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ubiquitin-specific
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endoproteolytic
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convertase
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proproteins
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deubiquitinating
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prohormone
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subtilisin-like
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dibasic
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yersinia
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pestis
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deubiquitinase
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trans-golgi
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propeptide
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farnesylated
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subtilisins
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plague
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kex2-like
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lys-arg
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proinsulins
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prelamin
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proregions
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furin-like
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flexneri
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monobasic
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deubiquitylation
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exoprotease
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zmpste24
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isoprenylated
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arg-arg
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pharmacology
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food industry
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biotechnology
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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
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Application
Application on EC 3.4.23.49 - omptin
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biotechnology
food industry
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the peptidase shows maximal milk clotting activity at 60-65 °C and maintenance of enzymatic activity above 80% in the presence of 20 mM CaCl2
medicine
pharmacology
studies on treatment of infection by antibiotic-resistant bacteria
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engineering of enzyme variants with targeted, high substrate specificity
biotechnology
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utilization of outer-membrane endoprotease OmpT variants as processing enzymes for production of peptides from designer fusion proteins, e.g. useful in motilin production, overview
biotechnology
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OmpT protease could be a possible factor responsible for reducing the expression of GFP at 37°C for wildtype GFP clone in K12 hosts like DH5alpha, JM109, LE 392
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use in therapeutic peptide production, efficient cleavage of substrates with basic amino acids at the P4 and P6 positions, able to cleave efficiently a fusion protein carrying human glucagon-like peptide I, releases mature protein from an Escherichia coli expressed fusion protein carrying human atrial natriuretic peptide, a drug for acute congestive heart failure
medicine
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the different contributions of EHEC and EPEC strains OmpT to the degradation and inactivation of antimicrobial peptide LL-37 may be due to their adaptation to their respective niches within the host, the colon and small intestine, respectively, where the environmental cues and abundance of antimicrobial peptides are different
medicine
the enzyme is a target for vaccine development. B-cell epitope mapping with human sera, three-dimensional modeling, omptins allergenicity and antigenicity prediction, overview
medicine
the enzyme is a target for vaccine development. B-cell epitope mapping with human sera, three-dimensional modeling, omptins allergenicity and antigenicity prediction, overview
medicine
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the enzyme is a target for vaccine development. B-cell epitope mapping with human sera, three-dimensional modeling, omptins allergenicity and antigenicity prediction, overview
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medicine
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the enzyme is a target for vaccine development. B-cell epitope mapping with human sera, three-dimensional modeling, omptins allergenicity and antigenicity prediction, overview
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medicine
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the different contributions of EHEC and EPEC strains OmpT to the degradation and inactivation of antimicrobial peptide LL-37 may be due to their adaptation to their respective niches within the host, the colon and small intestine, respectively, where the environmental cues and abundance of antimicrobial peptides are different
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medicine
Escherichia coli EPEC / E2348/69
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the different contributions of EHEC and EPEC strains OmpT to the degradation and inactivation of antimicrobial peptide LL-37 may be due to their adaptation to their respective niches within the host, the colon and small intestine, respectively, where the environmental cues and abundance of antimicrobial peptides are different
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