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Literature summary for 3.4.23.49 extracted from

  • Brannon, J.R.; Thomassin, J.L.; Gruenheid, S.; Le Moual, H.
    Antimicrobial peptide conformation as a structural determinant of omptin protease specificity (2015), J. Bacteriol., 197, 3583-3591 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information generation of a deletion mutant DELTAcroP Citrobacter rodentium
additional information generation of a deletion mutant DELTAompT Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Aprotinin inhibits CroP in a competitive manner Citrobacter rodentium
Aprotinin inhibits OmpT in a competitive manner Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
human LL-37 + H2O Escherichia coli a cathelicidin ?
-
?
human LL-37 + H2O Citrobacter rodentium a cathelicidin ?
-
?
human LL-37 + H2O Citrobacter rodentium ATCC 51459 a cathelicidin ?
-
?
human LL-37 + H2O Citrobacter rodentium DBS 100 a cathelicidin ?
-
?
human LL-37 + H2O Escherichia coli EDL933 a cathelicidin ?
-
?
murine cathelicidin-related antimicrobial peptide + H2O Escherichia coli CRAMP ?
-
?
murine cathelicidin-related antimicrobial peptide + H2O Citrobacter rodentium CRAMP ?
-
?
murine cathelicidin-related antimicrobial peptide + H2O Citrobacter rodentium ATCC 51459 CRAMP ?
-
?
murine cathelicidin-related antimicrobial peptide + H2O Citrobacter rodentium DBS 100 CRAMP ?
-
?
murine cathelicidin-related antimicrobial peptide + H2O Escherichia coli EDL933 CRAMP ?
-
?
plasminogen + H2O Escherichia coli
-
plasmin + ?
-
?
plasminogen + H2O Escherichia coli EDL933
-
plasmin + ?
-
?

Organism

Organism UniProt Comment Textmining
Citrobacter rodentium
-
-
-
Citrobacter rodentium ATCC 51459
-
-
-
Citrobacter rodentium DBS 100
-
-
-
Escherichia coli P58603
-
-
Escherichia coli EDL933 P58603
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Abz-SLGRKIQIK(Dnp)-NH2 + H2O
-
Escherichia coli Abz-SLGR + KIQIK(Dnp)-NH2
-
?
Abz-SLGRKIQIK(Dnp)-NH2 + H2O
-
Citrobacter rodentium Abz-SLGR + KIQIK(Dnp)-NH2
-
?
Abz-SLGRKIQIK(Dnp)-NH2 + H2O
-
Citrobacter rodentium ATCC 51459 Abz-SLGR + KIQIK(Dnp)-NH2
-
?
Abz-SLGRKIQIK(Dnp)-NH2 + H2O
-
Citrobacter rodentium DBS 100 Abz-SLGR + KIQIK(Dnp)-NH2
-
?
Abz-SLGRKIQIK(Dnp)-NH2 + H2O
-
Escherichia coli EDL933 Abz-SLGR + KIQIK(Dnp)-NH2
-
?
human LL-37 + H2O a cathelicidin Escherichia coli ?
-
?
human LL-37 + H2O a cathelicidin Citrobacter rodentium ?
-
?
human LL-37 + H2O a cathelicidin Citrobacter rodentium ATCC 51459 ?
-
?
human LL-37 + H2O a cathelicidin Citrobacter rodentium DBS 100 ?
-
?
human LL-37 + H2O a cathelicidin Escherichia coli EDL933 ?
-
?
additional information Citrobacter rodentium CroP cleaves CRAMP more rapidly than LL-37. Comparison of the substrate specificity and substrate sequence specificity of the omptins OmpT from Escherichia coli and CroP from Citrobacter rodentium. The enzymes have the same preference for cleaving at dibasic sites, but show important difference in substrate recognition, overview. LL-37 is alpha-helical and CRAMP is unstructured under the experimental conditions. By altering the alpha-helicity of LL-37 and CRAMP, decreasing LL-37 alpha-helicity increases its rate of cleavage by CroP. Conversely, increasing CRAMP alpha-helicity decreased its cleavage rate. CroP preferentially cleaves unstructured antimicrobial peptides (AMPs) Citrobacter rodentium ?
-
?
additional information EHEC OmpT degrades LL-37 and CRAMP at similar rates. Comparison of the substrate specificity and substrate sequence specificity of the omptins OmpT from Escherichia coli and CroP from Citrobacter rodentium. The enzymes have the same preference for cleaving at dibasic sites, but show important difference in substrate recognition, overview. LL-37 is alpha-helical and CRAMP is unstructured under the experimental conditions Escherichia coli ?
-
?
additional information Citrobacter rodentium CroP cleaves CRAMP more rapidly than LL-37. Comparison of the substrate specificity and substrate sequence specificity of the omptins OmpT from Escherichia coli and CroP from Citrobacter rodentium. The enzymes have the same preference for cleaving at dibasic sites, but show important difference in substrate recognition, overview. LL-37 is alpha-helical and CRAMP is unstructured under the experimental conditions. By altering the alpha-helicity of LL-37 and CRAMP, decreasing LL-37 alpha-helicity increases its rate of cleavage by CroP. Conversely, increasing CRAMP alpha-helicity decreased its cleavage rate. CroP preferentially cleaves unstructured antimicrobial peptides (AMPs) Citrobacter rodentium ATCC 51459 ?
-
?
additional information Citrobacter rodentium CroP cleaves CRAMP more rapidly than LL-37. Comparison of the substrate specificity and substrate sequence specificity of the omptins OmpT from Escherichia coli and CroP from Citrobacter rodentium. The enzymes have the same preference for cleaving at dibasic sites, but show important difference in substrate recognition, overview. LL-37 is alpha-helical and CRAMP is unstructured under the experimental conditions. By altering the alpha-helicity of LL-37 and CRAMP, decreasing LL-37 alpha-helicity increases its rate of cleavage by CroP. Conversely, increasing CRAMP alpha-helicity decreased its cleavage rate. CroP preferentially cleaves unstructured antimicrobial peptides (AMPs) Citrobacter rodentium DBS 100 ?
-
?
additional information EHEC OmpT degrades LL-37 and CRAMP at similar rates. Comparison of the substrate specificity and substrate sequence specificity of the omptins OmpT from Escherichia coli and CroP from Citrobacter rodentium. The enzymes have the same preference for cleaving at dibasic sites, but show important difference in substrate recognition, overview. LL-37 is alpha-helical and CRAMP is unstructured under the experimental conditions Escherichia coli EDL933 ?
-
?
murine cathelicidin-related antimicrobial peptide + H2O CRAMP Escherichia coli ?
-
?
murine cathelicidin-related antimicrobial peptide + H2O CRAMP Citrobacter rodentium ?
-
?
murine cathelicidin-related antimicrobial peptide + H2O CRAMP, rapid, almost complete degradation Citrobacter rodentium ?
-
?
murine cathelicidin-related antimicrobial peptide + H2O CRAMP Citrobacter rodentium ATCC 51459 ?
-
?
murine cathelicidin-related antimicrobial peptide + H2O CRAMP, rapid, almost complete degradation Citrobacter rodentium ATCC 51459 ?
-
?
murine cathelicidin-related antimicrobial peptide + H2O CRAMP Citrobacter rodentium DBS 100 ?
-
?
murine cathelicidin-related antimicrobial peptide + H2O CRAMP, rapid, almost complete degradation Citrobacter rodentium DBS 100 ?
-
?
murine cathelicidin-related antimicrobial peptide + H2O CRAMP Escherichia coli EDL933 ?
-
?
plasminogen + H2O
-
Escherichia coli plasmin + ?
-
?
plasminogen + H2O
-
Escherichia coli EDL933 plasmin + ?
-
?

Synonyms

Synonyms Comment Organism
CroP
-
Citrobacter rodentium
ompT
-
Escherichia coli
omptin protease
-
Escherichia coli
omptin protease
-
Citrobacter rodentium
protease 7 UniProt Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
assay at room temperature Escherichia coli
22
-
assay at room temperature Citrobacter rodentium

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Escherichia coli
7.4
-
assay at Citrobacter rodentium

General Information

General Information Comment Organism
evolution the difference in CroP and OmpT substrate specificity suggests that omptins evolved in response to the substrates present in their host microenvironments Escherichia coli
evolution the difference in CroP and OmpT substrate specificity suggests that omptins evolved in response to the substrates present in their host microenvironments Citrobacter rodentium
physiological function Citrobacter rodentium inactivates antimicrobial peptides (AMPs) and activates plasminogen into plasmin, respectively. CroP preferentially cleaves unstructured antimicrobial peptides (AMPs) Citrobacter rodentium
physiological function Escherichia coli OmpT inactivates antimicrobial peptides (AMPs) and activates plasminogen into plasmin, respectively Escherichia coli