Reactome | Secreted ACE:Zn2+ hydrolyzes AGT(25-34) (Angiotensin-(1-10)) to AGT(25-32) (Angiotensin-(1-8))

Secreted ACE:Zn2+ hydrolyzes AGT(25-34) (Angiotensin-(1-10)) to AGT(25-32) (Angiotensin-(1-8))

Stable Identifier

R-HSA-2065355

Type

Reaction [transition]

Species

Homo sapiens

Compartment

extracellular region

Synonyms

Secreted Angiotensin-converting Enzyme Hydrolyzes Angiotensin I to Yield Angiotensin II

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

Secreted ACE:Zn2+ hydrolyzes AGT(25-34) (Angiotensin-(1-10)) to AGT(25-32) (Angiotensin-(1-8))

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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.

Literature References

PubMed ID	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 Wei, L, Clauser, E, Corvol, P, Soubrier, F, Michaud, A, Alhenc-Gelas, F	J Biol Chem	1991
2558510	Purification of angiotensin-converting enzyme from human intestine Amano, K, Hayakari, M, Murakami, S, Izumi, H	Adv Exp Med Biol	1989
6270633	Purification and characterization of human converting enzyme (kininase II) Weare, JA, Erdös, EG, Stewart, TA	Peptides	1981
6269175	Purification of human lung angiotensin-converting enzyme Fyhrquist, F, Grönhagen-Riska, C	Scand J Clin Lab Invest	1980
12540854	Crystal structure of the human angiotensin-converting enzyme-lisinopril complex Acharya, KR, Sturrock, ED, Schwager, SL, Natesh, R	Nature	2003
1851160	The two homologous domains of human angiotensin I-converting enzyme are both catalytically active Wei, L, Clauser, E, Corvol, P, Alhenc-Gelas, F	J Biol Chem	1991
10536878	Mixed-type inhibition of pulmonary angiotensin I-converting enzyme by captopril, enalaprilat and ramiprilat Bénéteau-Burnat, B, Baudin, B	J Enzyme Inhib	1999
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 Kirsch, RE, Maeder, DL, Ehlers, MR	Biochim Biophys Acta	1986