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Peptidyl-dipeptidase B

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Peptidyl-dipeptidase B
Identifiers
EC no.3.4.15.4
CAS no.147014-93-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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NCBIproteins

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

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  1. ^ Harris RB, Wilson IB (September 1984). "Atrial tissue contains a metallo dipeptidyl carboxyhydrolase not present in ventricular tissue: partial purification and characterization". Archives of Biochemistry and Biophysics. 233 (2): 667–75. doi:10.1016/0003-9861(84)90493-4. PMID 6385859.
  2. ^ Harris RB, Wilson IB (1985). "Conversion of atriopeptin II to atriopeptin I by atrial dipeptidyl carboxy hydrolase". Peptides. 6 (3): 393–6. doi:10.1016/0196-9781(85)90102-0. PMID 2999723.
  3. ^ Soler DF, Harris RB (July 1988). "Continuous fluorogenic substrates for atrial dipeptidyl carboxyhydrolase. Importance of Ser in the P1 position". International Journal of Peptide and Protein Research. 32 (1): 35–40. PMID 3146555.
  4. ^ Soler DF, Harris RB (1989). "Atrial dipeptidyl carboxyhydrolase is a zinc-metallo proteinase which possesses tripeptidyl carboxyhydrolase activity". Peptides. 10 (1): 63–8. doi:10.1016/0196-9781(89)90077-6. PMID 2501770.
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