EC 3.4.15.1 - Peptidyl-dipeptidase A

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IntEnz Enzyme Nomenclature
EC 3.4.15.1

Names

Accepted name:
peptidyl-dipeptidase A
Other names:
ACE
DCP
PDH
angiotensin I-converting enzyme
angiotensin converting enzyme
carboxycathepsin
dipeptidase
dipeptide hydrolase [ambiguous]
dipeptidyl carboxypeptidase
dipeptidyl carboxypeptidase I
endothelial cell peptidyl dipeptidase
kininase II
peptidase P
peptidyl dipeptidase A
peptidyl dipeptidase I
peptidyl dipeptidase-4
peptidyl dipeptide hydrolase
peptidyl-dipeptide hydrolase
peptidyldipeptide hydrolase
Systematic name:
-

Reaction

Cofactor

Comments:

A Cl-dependent, zinc glycoprotein that is generally membrane-bound. A potent inhibitor is captopril. Important in elevation of blood pressure, through formation of angiotensin II (vasoconstrictor) and destruction of bradykinin (vasodilator). Two molecular forms exist in mammalian tissues, a widely-distributed somatic form of 150- to 180-kDa that contains two non-identical catalytic sites, and a testicular form of 90- to 100-kDa that contains only a single catalytic site. Type example of peptidase family M2.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , UniPathway
Protein domains and families: PROSITE:PDOC00129
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004246
CAS Registry Number: 9015-82-1
UniProtKB/Swiss-Prot: (12) [show] [UniProt]

References

  1. Soubrier, F., Alhenc-Gelas, F., Hubert, C., Allegrini, J., John, M., Tregear, G. and Corvol, P.
    Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning.
    Proc. Natl. Acad. Sci. USA 85: 9386-9390 (1988). [PMID: 89071703]
  2. Ehlers, M.R.W., Fox, E.A., Strydom, D.J. and Riordan, J.F.
    Molecular cloning of human testicular angiotensin-converting enzyme: the testis enzyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme.
    Proc. Natl. Acad. Sci. USA 86: 7741-7745 (1989). [PMID: 2554286]
  3. Wei, L., Clauser, E., Alhenc-Gelas, F. and Corvol, P.
    The two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors.
    J. Biol. Chem. 267: 13398-13405 (1992). [PMID: 1320019]
  4. Corvol, P., Williams, T.A. and Soubrier, F.
    Peptidyl dipeptidase A: angiotensin I-converting enzyme.
    Methods Enzymol. 248: 283-305 (1995). [PMID: 7674927]

[EC 3.4.15.1 created 1972, modified 1981, modified 1989, modified 1996, modified 2011]