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Literature summary for 3.4.23.49 extracted from

  • Okuno, K.; Yabuta, M.; Ooi, T.; Kinoshita, S.
    Utilization of Escherichia coli outer-membrane endoprotease OmpT variants as processing enzymes for production of peptides from designer fusion proteins (2004), Appl. Environ. Microbiol., 70, 76-86.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.23.49

Application

Application Comment Organism
biotechnology utilization of outer-membrane endoprotease OmpT variants as processing enzymes for production of peptides from designer fusion proteins, e.g. useful in motilin production, overview Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of wild-type and mutant enzymes strain W3110 M25 Escherichia coli

Protein Variants

Protein Variants Comment Organism
D97A site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview Escherichia coli
D97C site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview Escherichia coli
D97F site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview Escherichia coli
D97H 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 Escherichia coli
D97L 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 Escherichia coli
D97M 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 Escherichia coli
D97N site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview Escherichia coli
D97Q site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview Escherichia coli
D97S site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview Escherichia coli
D97T site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview Escherichia coli

Localization

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

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 consensus sequence of OmpT is R/K-A, the enzyme is highly selective for a basic amino acid residue at position P1, but less exclusive at P1', where several non-basic amino acids are tolerated, enzyme residue Asp97 is responsible for interaction with P1' position substrate residue Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
a fusion-motilin peptide + H2O proteolytic cleavage by mutant D97M at R-R-R-A-R*-motilin Escherichia coli ?
-
 ?
dynorphin A + H2O proteolytic cleavage, commercial peptide substrate Escherichia coli ?
-
 ?
human adrenocorticotropic hormone + H2O proteolytic cleavage by mutant D97L at Ser24, release of the hormone Escherichia coli ?
-
 ?
human calcitonin precursor + H2O proteolytic cleavage by mutant D97H at an N-terminal Cys Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
endoprotease
-
 Escherichia coli
ompT
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Escherichia coli