Table 2.
Selected examples of bacterial proteases, their preferred cleavage sites and example inhibitors
| Enzyme | Source | Cleavage site | Inhibitor |
|---|---|---|---|
| Serine and Cysteine proteases | |||
| Glutamyl endopeptidase I | Staphylococcus aureus | Glu-Phe or Glu-Val | None |
| Exfoliative toxin A | S. aureus | Glu-X | |
| IgA1-specific protease | Haemophilus influenzae Neisseria meningitidis | Pro-Ser, Pro-Thr | None specific |
| C5a peptidase | Streptococcus agalactiae Streptococcus pyogenes | His-Lys | None specific |
| Trepolisin | Treponema denticola | Phe-X | None specific |
| Prolyl tripeptidyl-peptidase | P. gingivalis | X-Y-Pro-X | None specific |
| Omptin | E. coli Yersinia pestis | Arg-Arg, Arg-Lys | thiol-blocking agents |
| Clostripain C11 | Clostridium histolyticum | Arg-X, Lys-X | oxidizing agents, thiol-blocking agents, heavy metal ions |
| Gingipain R | |||
| Gingipain K | P. gingivalis | Arg-X Lys-X |
thiol-blocking agents 1-(3-phenylpropionyl) piperidine-carboxylic acid-[4-amino-1(S)-(benzothiazole-2-carbonyl)butyl] amide, |
| Sortase | ubiquitous in Gram-positive bacteria | Leu-Pro-X-Thr-Gly | methanethiosulfonates or organo-mercurials |
| Clp peptidases | Ubiquitous | Met-Ala | ATP-dependent |
| Metalloproteinase | |||
| Pseudolysin | Pseudomonas aeruginosa | Phe-X or Gly-Leu | EDTA, EGTA, phenanthroline |
| Vibrio collagenase | Vibrio parahaemolyticus | X-Gly | |
| Clostridium collagenases | Clostridium perfringens | X-Gly | sulfonylated amino acid hydroxamates |
| Aeruginolysin | Ps. aeruginosa | Leu-Gly or Gly-Gly | |
| Mirabilysin | Proteus mirabilis | Leu-Gly (in IgA) | |
| Fragilysin | Bacteroides fragilis | Leu-Gly Gly-Leu | EDTA, DTPA |
| Sialoglycoprotein endopeptidase | H. influenzae | Arg-Asp | |