Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P24555 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl 7-amide + H2O | - |
Escherichia coli | benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin | - |
? | |
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 | ? | - |
? | |
RRRPRPPRLPRPRPR + 2 H2O | proline-rich peptide Bac(1-16) | Escherichia coli | L-Arg-L-Arg + RPRPPR + LPRPRPR | - |
? | |
RRRPRPPYLPRPRPPPFF + H2O | proline-rich peptide PR-39(1-18) | Escherichia coli | L-Arg-L-Arg + RPRPPYLPRPRPPPFF | - |
? |
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 |