| thimet oligopeptidase | <enzyme> Endo-oligopeptidase was EC 3.4.22.19 1989-1992; cl-peptidase was EC 3.4.99.31 1978-1992; thiol-dependent metalloproteinase which cleaves bonds with hydrophobic residues at p1, p2 and p3' and a small residue at p1' in substrates with 5-15 residues Registry number: EC 3.4.24.15 Synonym: pz-peptidase b, pz-peptidase a, pz-peptidase, endo-oligopeptidase, proenkephalin converting enzyme, endo-oligopeptidase a, endopeptidase a, enkephalin-converting enzyme, endooligopeptidase a, endopeptidase 22.19, soluble metallo-endopeptidase, endopeptidase 24.15, thimet peptidase, tissue-endopeptidase degrading collagenase-synthetic substrate, cl-peptidase, metalloendopeptidase 24.15, zinc endopeptidase 24-15, endopeptidase 3.4.24.15 (26 Jun 1999) |
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| PepB oligopeptidase | <enzyme> 66.4% identical to pepf oligopeptidase; isolated from group b streptococci; genbank u49821; do not confuse with pepb protein Registry number: EC 3.4.- Synonym: pepb gene product, oligopeptidase (26 Jun 1999) |
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| PepF oligopeptidase | <enzyme> An oligopeptidase from lactococcus lactis; exhibits substrate specificity similar to thimet oligopeptidase; contains a his-glu-x-x-his motif characteristic of metallopeptidases; mw 70 kD; genbank z32522 Registry number: EC 3.4.24.- Synonym: pepf gene product, pepf1 gene product, pepf2 gene product (26 Jun 1999) |
| prolyl oligopeptidase | <enzyme> Cleaves dipeptides from n-terminal end of peptide chain if penultimate residue is proline; before 1992 prolyl endopeptidase (thiol-dependent) was EC 3.4.22.18 Registry number: EC 3.4.21.26 Synonym: post-proline cleaving enzyme, proline specific endopeptidase, post-proline endopeptidase, prolyl endopeptidase, proline endopeptidase, prolyl endopeptidase I, prolyl endopeptidase (thiol-dependent) (26 Jun 1999) |
| oligopeptidase | <enzyme> From bacillus spaericus; acts on dipeptides and some tri- or tetrapeptides with ala-ala Registry number: EC 3.4.- (26 Jun 1999) |
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