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
Advanced search results
Engineering
Engineering on EC 3.4.23.49 - omptin
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D208A
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introduced as silent mutation in plasmids, transformation with plasmids
D208G
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site-directed mutagenesis, the mutant enzyme shows increased specificity for the A-R cleavage site compared to the wild-type enzyme
D210A
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introduced as silent mutation in plasmids, transformation with plasmids
D43A
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introduced as silent mutation in plasmids, transformation with plasmids
D83A
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introduced as silent mutation in plasmids, transformation with plasmids
D85A
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introduced as silent mutation in plasmids, transformation with plasmids
D97A
D97C
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site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
D97F
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site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
D97H
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site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, preference for human calcitonin precursor, substrate specificity with fusion protein, overview
D97L
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site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, preference for human adrenocarticotropic hormone, substrate specificity with fusion protein, overview
D97M
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site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, preference for a fusion peptide substrate with the sequence R-R-R-A-R*-motilin, substrate specificity with fusion protein, overview
D97N
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site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
D97Q
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site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
D97S
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site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
D97T
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site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
E111A
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introduced as silent mutation in plasmids, transformation with plasmids
E136A
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introduced as silent mutation in plasmids, transformation with plasmids
E193A
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introduced as silent mutation in plasmids, transformation with plasmids
E250A
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introduced as silent mutation in plasmids, transformation with plasmids
E27A
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introduced as silent mutation in plasmids, transformation with plasmids
G216K/K217G
S223R
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site-directed mutagenesis, the mutant enzyme shows increased specificity for the A-R cleavage site and overall reduced activity compared to the wild-type enzyme
S99A/G216K/K217G
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recombinant ompT variant in order to abolish autoproteolysis
D206A
additional information
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introduced as silent mutation in plasmids, transformation with plasmids
D97A
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site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
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recombinant ompT variant in order to abolish autoproteolysis
G216K/K217G
site-directed mutagenesis, mutation to remove the dibasic proteolysis site. The mutant has a circa 30% lower activity than wild-type OmpT
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site-directed mutagenesis, inacticve catalytic site mutant
D206A
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site-directed mutagenesis, inacticve catalytic site mutant
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generation of a Citrobacter rodentium DELTAcroP strain
additional information
Citrobacter rodentium ATCC 51459
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generation of a deletion mutant DELTAcroP
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additional information
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swapping of ten amino acid residues at two surface loops of Pla and membrane protease Epo of the plant pathogenic Erwinia pyrifoliae introduces plasminogen activation capacity in Epo and inactivates the function in Pla
additional information
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random mutagenesis of gene ompT, screening for mutant variants with altered cleavage specificity, e.g. mutant variants 1.2.19 and 1.3.19 exhibits higher specificity for the cleavage site A-R and lower specificity for R-R than the wild-type
additional information
complementation of strain BL21 producing fusion protein GST-Sup35NM with the wild-type OmpT-gene restores colony-forming ability
additional information
referring to the classical Lpp-OmpA (LOA) display system, the signal peptide and nine amino acids of the mature outer membrane prolipoprotein Lpp are fused to the transmembrane domain comprising five beta-strands of truncated OmpT to generate a Lpp-OmpT (LOT) display system. The C-terminal fusion strategy is used to fuse a small peptide (His tag) and red fluorescent protein (mCherry) to the C-terminus of LOT. Exposed histidine tags present in recombinant proteins form complexes with transition metal ions such as Ni2+, Zn2+, Cu2+, and Fe3+. Adsorption analysis of cells expressing the chimeric mutant protein using Cu2+, adhesion of surface engineered cells to Cu2+-chelating sepharose beads, method evaluation, overview
additional information
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referring to the classical Lpp-OmpA (LOA) display system, the signal peptide and nine amino acids of the mature outer membrane prolipoprotein Lpp are fused to the transmembrane domain comprising five beta-strands of truncated OmpT to generate a Lpp-OmpT (LOT) display system. The C-terminal fusion strategy is used to fuse a small peptide (His tag) and red fluorescent protein (mCherry) to the C-terminus of LOT. Exposed histidine tags present in recombinant proteins form complexes with transition metal ions such as Ni2+, Zn2+, Cu2+, and Fe3+. Adsorption analysis of cells expressing the chimeric mutant protein using Cu2+, adhesion of surface engineered cells to Cu2+-chelating sepharose beads, method evaluation, overview
additional information
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construction of Salmonella enterica mutant DELTApgtE strain 14028R-1 from the isogenic virulent wild-type strain 14028R. Mutant strain 14028R-1 is inactive with factor H and B. Complementation of 14028R-1 with pgtE-encoding pMRK3 recovers the activity toward B and H
additional information
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construction of Salmonella enterica mutant DELTApgtE strain 14028R-1 from the isogenic virulent wild-type strain 14028R. Mutant strain 14028R-1 is inactive with factor H and B. Complementation of 14028R-1 with pgtE-encoding pMRK3 recovers the activity toward B and H
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