| EC |
3.4.15.4 |
| Accepted name: |
peptidyl-dipeptidase B |
| Reaction: |
Release of a C-terminal dipeptide or exceptionally a tripeptide |
| Other name(s): |
dipeptidyl carboxyhydrolase; atriopeptin convertase; atrial di-(tri)peptidyl carboxyhydrolase; peptidyldipeptidase B; atrial dipeptidyl carboxyhydrolase; atrial peptide convertase |
| Comments: |
A membrane-bound, zinc metallopeptidase located in mammalian atrial, but not ventricular, myocytes. Although it is capable of converting the 126-residue atriopeptin III directly to atriopeptin I by releasing a C-terminal tripeptide Phe-Arg-Tyr, it is generally restricted to the release of dipeptides. In contrast to peptidyl-dipeptidase A (EC 3.4.15.1) it displays no Cl- dependence and shows no action on angiotensin I. Conversely, peptidyl-dipeptidase A is unable to release Phe-Arg from the C-terminus of atriopeptin II |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 147014-93-5 |
| References: |
| 1. |
Harris, R.B. and Wilson, I.B. Atrial tissue contains a metallo dipeptidyl carboxyhydrolase not present in ventricular tissue: partial purification and characterization. Arch. Biochem. Biophys. 233 (1984) 667–675. [DOI] [PMID: 6385859] |
| 2. |
Harris, R.B. and Wilson, I.B. Conversion of atriopeptin II to atriopeptin I by atrial dipeptidyl carboxy hydrolase. Peptides (Fayetteville) 6 (1985) 393–396. [DOI] [PMID: 2999723] |
| 3. |
Soler, D.F. and Harris, R.B. Continuous fluorogenic substrates for atrial dipeptidyl carboxyhydrolase. Importance of Ser in the P1 position. Int. J. Peptide Protein Res. 32 (1988) 35–40. [DOI] [PMID: 3146555] |
| 4. |
Soler, D.F. and Harris, R.B. Atrial dipeptidyl carboxyhydrolase is a zinc-metallo proteinase which possesses tripeptidyl carboxyhydrolase activity. Peptides (Fayetteville) 10 (1989) 63–68. [DOI] [PMID: 2501770] |
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| [EC 3.4.15.4 created 1992] |
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