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Literature summary for 3.4.23.49 extracted from

  • Wood, S.E.; Sinsinbar, G.; Gudlur, S.; Nallani, M.; Huang, C.F.; Liedberg, B.; Mrksich, M.
    A bottom-up proteomic approach to identify substrate specificity of outer-membrane protease OmpT (2017), Angew. Chem. Int. Ed. Engl., 56, 16531-16535 .
    View publication on PubMed
Search for more literature for 3.4.23.49

Protein Variants

Protein Variants Comment Organism
G216K/K217G site-directed mutagenesis, mutation to remove the dibasic proteolysis site. The mutant has a circa 30% lower activity than wild-type OmpT Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0094
-
 Ac-GLLGDFFRRVKEKIGC pH and temperature not specified in the publication Escherichia coli
0.0184
-
 Ac-GLLGDFFRKSKEKIGC pH and temperature not specified in the publication Escherichia coli
0.0225
-
 Ac-GLLGDFARRAKEKIGC pH and temperature not specified in the publication Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
LL37 + H2O Escherichia coli a human antimicrobial peptide of the cathelicidin family ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P09169
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ac-GLLGDFARRAKEKIGC + H2O LL37 substrate mutant Escherichia coli Ac-GLLGDFAR + RAKEKIGC
-
 ?
Ac-GLLGDFFRKSKEKIGC + H2O LL37 substrate mutant, enzyme mutant G216K/K217G shows negligible activity Escherichia coli Ac-GLLGDFF + RKSKEKIGC
-
 ?
Ac-GLLGDFFRRVKEKIGC + H2O LL37 substrate mutant Escherichia coli Ac-GLLGDFFR + RVKEKIGC
-
 ?
LL37 + H2O a human antimicrobial peptide of the cathelicidin family Escherichia coli ?
-
 ?
LL37 + H2O a human antimicrobial peptide of the cathelicidin family, wild-type LL37 sequence has 2 dibasic sites that can be cleaved by OmpT Escherichia coli ?
-
 ?
additional information analysis of protease activity for the preferred residues at the cleavage site (P1, P1') and nearest-neighbor positions (P2, P2') and their positional interdependence revealed FRRV as the optimal peptide with the highest OmpT activity. Substituting FRRV into a fragment of LL37, a natural substrate of OmpT, leads to a greater than 400fold improvement in OmpT catalytic efficiency. Wild-type and mutant OmpT display significant differences in their substrate specificities. Substrate consensus sequence screening, substrate specificity, overview. Twelve tetrapeptides display higher activity for wild-type OmpT than does the ARRA peptide, which has an activity of 91.0%, kinetic comparison of peptide substrates that are inserted into the LL37 fragment Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
bacterial outer-membrane protease
-
 Escherichia coli
ompT
-
 Escherichia coli
outer-membrane protease
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.3
-
 Ac-GLLGDFFRKSKEKIGC pH and temperature not specified in the publication Escherichia coli
12.9
-
 Ac-GLLGDFARRAKEKIGC pH and temperature not specified in the publication Escherichia coli
57.6
-
 Ac-GLLGDFFRRVKEKIGC pH and temperature not specified in the publication Escherichia coli

General Information

General Information Comment Organism
additional information acidic residues in the active site are the catalytic pairs Asp83-Asp85 and His212-Asp210 Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
16.3
-
 Ac-GLLGDFFRKSKEKIGC pH and temperature not specified in the publication Escherichia coli
573.3
-
 Ac-GLLGDFARRAKEKIGC pH and temperature not specified in the publication Escherichia coli
6127.7
-
 Ac-GLLGDFFRRVKEKIGC pH and temperature not specified in the publication Escherichia coli