EC 3.4.17.23 - Angiotensin-converting enzyme 2

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IntEnz Enzyme Nomenclature
EC 3.4.17.23

Names

Accepted name:
angiotensin-converting enzyme 2
Other names:
ACE-2
ACE2
hACE2
angiotensin converting enzyme 2
angiotensin converting enzyme-2
Tmem27
Systematic name:
-

Reaction

Comments:

A transmembrane glycoprotein with an extracellular catalytic domain. Angiotensin-converting enzyme 2 functions as a carboxypeptidase, cleaving a single C-terminal residue from a distinct range of substrates [2]. Catalytic efficiency is 400-fold higher with angiotensin II (1-8) as a substrate than with angiotensin I (1-10). Angiotensin-converting enzyme 2 also efficiently hydrolyzes des-Arg9-bradykinin, but it does not hydrolyze bradykinin [1]. In peptidase family M2.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00129
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Vickers, C., Hales, P., Kaushik, V., Dick, L., Gavin, J., Tang, J., Godbout, K., Parsons, T., Baronas, E., Hsieh, F., Acton, S., Patane, M., Nichols, A., Tummino, P.
    Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase.
    J. Biol. Chem. 277: 14838-14843 (2002). [PMID: 11815627]
  2. Lambert, D. W., Hooper, N. M., Turner, A. J.
    Angiotensin-converting enzyme 2 and new insights into the renin-angiotensin system.
    Biochem. Pharmacol. 75: 781-786 (2008). [PMID: 17897633]
  3. Towler, P., Staker, B., Prasad, S. G., Menon, S., Tang, J., Parsons, T., Ryan, D., Fisher, M., Williams, D., Dales, N. A., Patane, M. A., Pantoliano, M. W.
    ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis.
    J. Biol. Chem. 279: 17996-18007 (2004). [PMID: 14754895]

[EC 3.4.17.23 created 2009]