Reactome: A Curated Pathway Database

Secreted ACE hydrolyzes Angiotensin-(1-10) to Angiotensin-(1-8) (R-HSA-2065355)

Species Homo sapiens

Summation

Secreted angiotensin-converting enzyme (ACE) cleaves 2 amino acid residues from the C-terminus of angiotensin-(1-10) (angiotensin I) to yield angiotensin-(1-8) (angiotensin II) (Wei et al. 1991). This reaction is inhibited by drugs used to treat hypertension (angiotensin converting enzyme inhibitors, ACEI) including captopril (Gronhagen-Riska and Fyhrquist 1980, Stewart et al. 1981, Ehlers et al. 1986, Hayakari et al. 1989, Wei et al. 1991, Baudin and Beneteau-Burnat 1999), enalaprilat (metablized from the prodrug enalapril, Wei et al. 1991, Baudin and Beneteau-Burnat 1999), lisinopril ( Ehlers et al. 1991, Natesh et al. 2003), and ramiprilat (metabolized from the prodrug ramipril, Baudin and Beneteau-Burnat 1999). ACE is secreted ("shed") from membranes of endothelial cells by cleavage in the C-terminal region that removes the membrane anchor.

Locations in the PathwayBrowser
Additional Information
Compartment extracellular region
GO Biological Process angiotensin maturation (0002003)
Components of this entry
Input entries
Output entries
Catalyst Activity
PhysicalEntity Activity Active Units
ACE(30-1232) metallodipeptidase activity (0070573)
This entry is regulated by
Regulation type Name
NegativeRegulation
PositiveRegulation
Literature References
pubMedId Title Journal Year
1848554 Expression and characterization of recombinant human angiotensin I-converting enzyme. Evidence for a C-terminal transmembrane anchor and for a proteolytic processing of the secreted recombinant and plasma enzymes J Biol Chem 1991
1851160 The two homologous domains of human angiotensin I-converting enzyme are both catalytically active J Biol Chem 1991
2558510 Purification of angiotensin-converting enzyme from human intestine Adv Exp Med Biol 1989
6269175 Purification of human lung angiotensin-converting enzyme Scand J Clin Lab Invest 1980
3017438 Rapid affinity chromatographic purification of human lung and kidney angiotensin-converting enzyme with the novel N-carboxyalkyl dipeptide inhibitor N-[1(S)-carboxy-5-aminopentyl]glycylglycine Biochim Biophys Acta 1986
6270633 Purification and characterization of human converting enzyme (kininase II) Peptides 1981
1848554 Expression and characterization of recombinant human angiotensin I-converting enzyme. Evidence for a C-terminal transmembrane anchor and for a proteolytic processing of the secreted recombinant and plasma enzymes J Biol Chem 1991
1851160 The two homologous domains of human angiotensin I-converting enzyme are both catalytically active J Biol Chem 1991
10536878 Mixed-type inhibition of pulmonary angiotensin I-converting enzyme by captopril, enalaprilat and ramiprilat J Enzyme Inhib 1999
12540854 Crystal structure of the human angiotensin-converting enzyme-lisinopril complex Nature 2003