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Literature summary for 3.4.23.49 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
Search for more literature for 3.4.23.49

Cloned(Commentary)

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

KM Value [mM]

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

Localization

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli K-12
-
 gene ompT
-

Purification (Commentary)

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

Reaction

Reaction Comment Organism Reaction ID
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]

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
ompT
-
 Escherichia coli K-12

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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