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Literature summary for 3.4.21.83 extracted from

  • Mattiuzzo, M.; De Gobba, C.; Runti, G.; Mardirossian, M.; Bandiera, A.; Gennaro, R.; Scocchi, M.
    Proteolytic activity of Escherichia coli oligopeptidase B against proline-rich antimicrobial peptides (2014), J. Microbiol. Biotechnol., 24, 160-167.
    View publication on PubMed
Search for more literature for 3.4.21.83

Organism

Organism UniProt Comment Textmining
Escherichia coli P24555
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl 7-amide + H2O
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 Escherichia coli benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
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 ?
additional information oligopeptidase B can efficiently hydrolyze in vitro cationic antimicrobial peptides up to 30 residues in length, even though they contained several prolines, shortening them to inactive fragments. Two consecutive basic residues are a preferred cleavage site for the peptidase. In the case of a single basic residue, there is no cleavage if proline residues are present in the P1 and P2 positions Escherichia coli ?
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RRRPRPPRLPRPRPR + 2 H2O proline-rich peptide Bac(1-16) Escherichia coli L-Arg-L-Arg + RPRPPR + LPRPRPR
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RRRPRPPYLPRPRPPPFF + H2O proline-rich peptide PR-39(1-18) Escherichia coli L-Arg-L-Arg + RPRPPYLPRPRPPPFF
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General Information

General Information Comment Organism
physiological function overexpression of peptidase makes the bacterial cells specifically less susceptible to several proline-rich antimicrobial peptides known to penetrate into the bacterial cytosol, and its level of activity directly correlates with the degree of resistance Escherichia coli