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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Activating Compound
Activating Compound on EC 3.4.23.49 - omptin
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Escherichia coli lipopolysaccharide
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LPS, required for omptin activity
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Urea
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optimal concentration: 4-5 M, inclusion bodies from Escherichia coli as substrate
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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
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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
OmpT protein active only in the presence of
lipopolysaccharide
purified OmpP protease active only in the presence of, similar to OmpT protein homologue
lipopolysaccharide
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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
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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
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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
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e.g. LPS K12, required for activity, lipid-protein interactions, complex activity analysis on model membranes and human mononuclear cells, overview
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lipopolysaccharides
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required for activity, protein-lipid interactions, overview
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