| LAP | 1) Leukocyte Alkaline Phosphatase 2) Leucine Amino-Peptidase |
|---|---|
| PEP | peptidase; phospho(enol)pyruvate; peer evaluation program; phosphoenolpyruvate; pigmentation, edema,... |
| Pep | peptidase |
| PEPA | peptidase A |
| PEPB | peptidase B |
| DP IV | Dipeptidyl Peptidase IV |
|---|---|
| DPP IV | Dipeptidyl Peptidase IV |
| DPP | Dipeptidyl peptidase |
| DPPI | Dipeptidyl peptidase I |
| DPP II | Dipeptidyl peptidase II |
| peptidase P | <enzyme> A hydrolase cleaving C-terminal dipeptides from a variety of substrates, including angiotensin I, which is converted to angiotensin II and histidylleucine. An important step in the metabolism of certain vasopressor agents. It is a chloride-dependent, zinc glycoprotein that is generally membrane-bound and active at neutral pH. Only single dipeptides are released from angiotensin I and bradykinin because of the lack of activity on bonds involving proline. It may also have endopeptidase activity on some substrates. Registry number: EC 3.4.15.1 Synonym: carboxycathepsin, dipeptidyl carboxypeptidase, kinase II, peptidase P. (22 Sep 2002) |
|---|
| alkaline D-peptidase | <enzyme> A penicillin-recognizing enzyme from bacillus cereus; has beta-lactamase activity; genbank d86380 Registry number: EC 3.4.99.- Synonym: ADP gene product, alkaline d-stereospecific endopeptidase (26 Jun 1999) |
|---|---|
| aspartyllysine peptidase | <enzyme> From human intestinal brush border; stabilised by zn+2 Registry number: EC 3.4.13.- Synonym: zn-stable aspartyllysine peptidase (26 Jun 1999) |
| C5a peptidase | <enzyme> Streptococcus pyogenes enzyme inactivates complement 5a by cleaving at lysine 68, removing a six-amino acid fragment Pharmacological action: complement inactivators Registry number: EC 3.4.99.- Synonym: streptococcus c5a peptidase, gbs c5a-ase, group b streptococci c5a-ase, scpa protein (26 Jun 1999) |
| matrix processing peptidase | <enzyme> From matrix fraction of rat liver mitochondria; cleaves mitochondrial protein precursors; inhibited by metal chelators and reactived by mn2+; classified as EC 3.4.24.64 Registry number: EC 3.4.24.- Synonym: mitochondrial processing peptidase, mitochondrial processing protease, alpha-mpp, beta-mpp, p-52 protein, rat, p-55 protein, rat, mas1 protein, yeast, mas2 protein, yeast (26 Jun 1999) |
| peptidase | <enzyme> Alternative name for a protease. (18 Nov 1997) |
| peptidase D | <enzyme> An enzyme cleaving aminoacyl-l-proline bonds in dipeptides containing a C-terminal prolyl residue; a deficiency of this enzyme results in hyperimidodipeptiduria. Synonym: imidodipeptidase, peptidase D, prolidase. (05 Mar 2000) |
| mitochondrial intermediate peptidase | <enzyme> Removes the octapeptide from the amino terminus of the intermediate protein processed from the protein precursor of certain mitochondrial proteins by the mitochondrial processing peptidase; smip from schizophyllum commune; rmip from rat; ymip from saccharomyces cerevisiae Registry number: EC 3.4.24.59 Synonym: mip peptidase, smip peptidase, rmip peptidase, ymip peptidase (26 Jun 1999) |
| procollagen peptidase | <enzyme> The proteases that remove the terminal extension peptides of procollagen, deficiency of these enzymes leads to dermatosparaxis or Ehlers Danlos syndrome. (18 Nov 1997) |
| 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) |
| 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) |
제품명 |
판매사 |
보험코드 | 성분/함량 | 구분/보험급여 |
|---|
제품명 |
판매사 |
보험코드 | 성분/함량 | 구분/보험급여 |
|---|