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Literature summary extracted from

  • McCarter, J.D.; Stephens, D.; Shoemaker, K.; Rosenberg, S.; Kirsch, J.F.; Georgiou, G.
    Substrate specificity of the Escherichia coli outer membrane protease OmpT (2004), J. Bacteriol., 186, 5919-5925.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.23.49 gene ompT, phage display metod used for substrate specificity analysis, expression in Escherichia coli AN1 cells Escherichia coli K-12

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.23.49 additional information
-
 additional information kinetics for phage display generated peptide substrates, overview Escherichia coli K-12

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.23.49 outer membrane
-
 Escherichia coli K-12 19867
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.23.49 human plasminogen + H2O Escherichia coli K-12 proteolytic cleavage site CPGR*VVGGC, activation ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.23.49 Escherichia coli K-12
-
 gene ompT
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.23.49 recombinant enzyme from Escherichia coli AN1 cells Escherichia coli K-12

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.23.49 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. the enzyme contains a Ser-Asp-His catalytic triad, active site, the consensus sequence of OmpT is R/K*-R/K, the enzyme is highly selective for a basic amino acid residue at position P1, but less exclusive at P1', where several amino acids are tolerated e,g, Lys, Val, and Gly, at P2' common residues are Ala or Val, at P3 and P4 the enzyme prefers Trp or Arg Escherichia coli K-12
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.23.49 additional information
-
-
 Escherichia coli K-12

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.23.49 alpha-neoendorphin + H2O proteolytic cleavage site GFLR*KYPK Escherichia coli K-12 ?
-
 ?
3.4.23.49 dynorphin A(1-13) + H2O proteolytic cleavage site GFLR*RIRPK Escherichia coli K-12 Tyr-Gly-Gly-Phe-Leu-Arg + Arg-Ile-Arg-Pro-Lys-Leu-Lys
-
 ?
3.4.23.49 gamma-interferon + H2O proteolytic cleavage sites KTGK*RKRSQ and FRGR*RASQ Escherichia coli K-12 ?
-
 ?
3.4.23.49 human creatin kinase + H2O proteolytic cleavage site DIYK*KLRDK Escherichia coli K-12 ?
-
 ?
3.4.23.49 human plasminogen + H2O proteolytic cleavage site CPGR*VVGGC, activation Escherichia coli K-12 ?
-
 ?
3.4.23.49 Mastoparan + H2O proteolytic cleavage site ALAK*KIL Escherichia coli K-12 ?
-
 ?
3.4.23.49 additional information substrate specificity analysis Escherichia coli K-12 ?
-
 ?
3.4.23.49 Parathyroid hormone + H2O proteolytic cleavage sites EWLR*KKLQD and WLRK*KLQDV Escherichia coli K-12 ?
-
 ?
3.4.23.49 rabbit creatine kinase + H2O proteolytic cleavage sites DLYK*KLRDK and RGER*RAVEK Escherichia coli K-12 ?
-
 ?
3.4.23.49 T7 RNA polymerase + H2O proteolytic cleavage sites QLNK*RVGHV, HVYK*KAFMQ, and DRAR*KSRRI Escherichia coli K-12 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.23.49 ompT
-
 Escherichia coli K-12

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.23.49 37
-
 assay at Escherichia coli K-12

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.23.49 additional information
-
 additional information
-
 Escherichia coli K-12

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.23.49 7.2
-
 assay at Escherichia coli K-12