Glutamyl endopeptidase is in at least some species part of a
zymogen activation cascade, with its activity being dependent on proteolytic activation of a pre-form of the protease. GluV8 of
S. aureus, for example, is dependent of activation by the
metalloprotease aureolysin, and is itself needed for activation of staphopain B. GluSE, GluSW and SprE have been observed to be activated by a metalloprotease in a similar fashion. Proteases of this group hydrolyzes peptide bonds after the negatively charged glutamic acid or aspartic acid, with a higher preference to the former. The pH optimum has been found to lie slightly above neutral pH (7-8) for GluV8 and GluBL. == See also ==