Peptidyl-dipeptidase B
| Peptidyl-dipeptidase B | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.15.4 | ||||||||
| CAS no. | 147014-93-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Peptidyl-dipeptidase B (EC 3.4.15.4, dipeptidyl carboxyhydrolase, atriopeptin convertase, atrial di-(tri)peptidyl carboxyhydrolase, peptidyldipeptidase B, atrial dipeptidyl carboxyhydrolase, atrial peptide convertase) is an enzyme.[1][2][3][4] It catalyses the following chemical reaction
- Release of a C-terminal dipeptide or exceptionally a tripeptide
This membrane-bound, zinc metallopeptidase is located in mammalian atrial myocytes.
References
- ^ Harris, R.B.; Wilson, I.B. (1984). "Atrial tissue contains a metallo dipeptidyl carboxyhydrolase not present in ventricular tissue: partial purification and characterization". Arch. Biochem. Biophys. 233: 667–675. doi:10.1016/0003-9861(84)90493-4. PMID 6385859.
- ^ Harris, R.B.; Wilson, I.B. (1985). "Conversion of atriopeptin II to atriopeptin I by atrial dipeptidyl carboxy hydrolase". Peptides (Fayetteville). 6: 393–396. doi:10.1016/0196-9781(85)90102-0. PMID 2999723.
- ^ Soler, D.F.; Harris, R.B. (1988). "Continuous fluorogenic substrates for atrial dipeptidyl carboxyhydrolase. Importance of Ser in the P1 position". Int. J. Peptide Protein Res. 32: 35–40. PMID 3146555.
- ^ Soler, D.F.; Harris, R.B. (1989). "Atrial dipeptidyl carboxyhydrolase is a zinc-metallo proteinase which possesses tripeptidyl carboxyhydrolase activity". Peptides (Fayetteville). 10: 63–68. doi:10.1016/0196-9781(89)90077-6. PMID 2501770.
External links
- Peptidyl-dipeptidase+B at the U.S. National Library of Medicine Medical Subject Headings (MeSH)