IntEnz

EC 3.4.15.1 - Peptidyl-dipeptidase A

IntEnz Enzyme Nomenclature
EC 3.4.15.1

Names

Reaction

• Release of a C-terminal dipeptide, oligopeptide┼Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II.

Cofactor

• Zn²⁺

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

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]