KEGG   ENZYME: 3.4.15.4Help
Entry
EC 3.4.15.4                 Enzyme                                 

Name
peptidyl-dipeptidase B;
dipeptidyl carboxyhydrolase;
atriopeptin convertase;
atrial di-(tri)peptidyl carboxyhydrolase;
peptidyldipeptidase B;
atrial dipeptidyl carboxyhydrolase;
atrial peptide convertase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Peptidyl-dipeptidases
BRITE hierarchy
Reaction(IUBMB)
Release of a C-terminal dipeptide or exceptionally a tripeptide
Comment
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
History
EC 3.4.15.4 created 1992
Reference
1  [PMID:6385859]
  Authors
Harris RB, Wilson IB.
  Title
Atrial tissue contains a metallo dipeptidyl carboxyhydrolase not present in ventricular tissue: partial purification and characterization.
  Journal
Arch. Biochem. Biophys. 233 (1984) 667-75.
Reference
2  [PMID:2999723]
  Authors
Harris RB, Wilson IB.
  Title
Conversion of atriopeptin II to atriopeptin I by atrial dipeptidyl carboxy hydrolase.
  Journal
Peptides. 6 (1985) 393-6.
Reference
3  [PMID:3146555]
  Authors
Soler DF, Harris RB.
  Title
Continuous fluorogenic substrates for atrial dipeptidyl carboxyhydrolase. Importance of Ser in the P1 position.
  Journal
Int. J. Pept. Protein. Res. 32 (1988) 35-40.
Reference
4  [PMID:2501770]
  Authors
Soler DF, Harris RB.
  Title
Atrial dipeptidyl carboxyhydrolase is a zinc-metallo proteinase which possesses tripeptidyl carboxyhydrolase activity.
  Journal
Peptides. 10 (1989) 63-8.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
147014-93-5

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