| pyroglutamyl-peptidase I | <enzyme> An enzyme that catalyses the release of a n-terminal pyroglutamyl group from a polypeptide provided the next residue is not proline. It is inhibited by thiol-blocking reagents and occurs in mammalian tissues, microorganisms, and plants. Registry number: EC 3.4.19.3 (12 Dec 1998) |
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| PZ-PLGPA peptidase | <enzyme> Endopeptidase from treponema denticola Registry number: EC 3.4.21.- (26 Jun 1999) |
| signal peptidase | A peptide present on proteins that are destined either to be secreted or to be membrane components. It is usually at the N terminus and normally absent from the mature protein. Normally refers to the sequence (ca 20 amino acids) that interacts with signal recognition particle and directs the ribosome to the endoplasmic reticulum where co translational insertion takes place. Could also refer to sequences that direct post translational uptake by organelles. Signal peptides are highly hydrophobic but with some positively charged residues. The signal sequence is normally removed from the growing peptide chain by signal peptidase, a specific protease located on the cisternal face of the endoplasmic reticulum. See: signal recognition particle. (18 Nov 1997) |
| signal peptidase complex | A peptide present on proteins that are destined either to be secreted or to be membrane components. It is usually at the N terminus and normally absent from the mature protein. Normally refers to the sequence (ca 20 amino acids) that interacts with signal recognition particle and directs the ribosome to the endoplasmic reticulum where co translational insertion takes place. Could also refer to sequences that direct post translational uptake by organelles. Signal peptides are highly hydrophobic but with some positively charged residues. The signal sequence is normally removed from the growing peptide chain by signal peptidase, a specific protease located on the cisternal face of the endoplasmic reticulum. See: signal recognition particle. (18 Nov 1997) |
| N-acetylaspartylglutamate peptidase | <enzyme> Produces glutamate plus n-acetylaspartate; found throughout rat CNS Registry number: EC 3.4.13.- Synonym: naag peptidase (26 Jun 1999) |
| N-benzyloxycarbonylglycyl-glycyl-arginyl peptidase | <enzyme> Enzyme from bacteroides gingivalis is a cysteine proteinase; enzyme from human serum which acts on the same substrate is a serine proteinase Registry number: EC 3.4.22.- Synonym: n-cbz-gly-gly-arg peptidase, cgga peptidase (26 Jun 1999) |
| stromal processing peptidase | <enzyme> Involved in processing chloroplast stromal proteins Registry number: EC 3.4.24.- (26 Jun 1999) |
| dipeptidyl peptidase | A hydrolase occurring in two forms: Dipeptidyl peptidase I, dipeptidyl transferase, cleaving dipeptides from the amino end of polypeptides, dipeptidyl peptidase II, with properties similar to those of I, has a different specificity. (05 Mar 2000) |
| thylakoid processing peptidase | <enzyme> Signal type peptidase with stringent substrate requirements at the -3 and -1 positions; removes amino-terminal peptide extension which transports proteins across the thylakoid membrane Registry number: EC 3.4.99.- (26 Jun 1999) |
| tri-alanyl peptidase | <enzyme> Biliary tract enzyme Registry number: EC 3.4.- (26 Jun 1999) |
| type IV prepilin peptidase | <enzyme> Product of the pulc-o pullulanase secretion gene operon; involved in processing prepilin signal peptide; may also function as an n-methyltransferase Registry number: EC 3.4.99.- Synonym: pulo protein, pulo gene product, pulo peptidase (26 Jun 1999) |
| FALGPA peptidase | <enzyme> An endopeptidase from treponema denticola that cleaves furylacryloyl-leu-gly-pro-ala; also active on bradykinin Registry number: EC 3.4.24.- Synonym: falgpa-peptidase (26 Jun 1999) |
| lysine-C peptidase | <enzyme> Used in amino acid sequence determinations Registry number: EC 3.4.99.- Synonym: lysine specific peptidase (26 Jun 1999) |