AOPEP:Zn2+ hydrolyses AGT(35-41) to AGT(36-41)

Stable Identifier
Reaction [transition]
Homo sapiens
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Aminopeptidase O (AOPEP, AP-O) is a member of the M1 family of zinc metallopeptidases or gluzincins. AOPEP contains a large catalytic gluzincin domain which has the archetypal metalloprotease zinc-binding site ending in a family-specific Glu residue (HEXXHX[18]E) typical to this family. AOPEP is able to catalyse the hydrolsis of an arginine residue (L-Arg) from angiotensin III (AGT(35-41)) to form angiotensin IV (AGT(36-41)), a bioactive peptide of the renin-angiotensin pathway. AOPEP does not contain a recognisable signal sequence or type II transmembrane domain, indicating that it likely belongs to the cytoplasmic subfamily of gluzincins (Diaz-Perales et al. 2005). AOPEP mRNA transcripts are predominantly detected in the pancreas, placenta, liver, testis, and heart. Expression of the AOPEP in heart and testis could suggest involvement in the regulation of cardiac and male reproductive physiology (Diaz-Perales et al. 2005).

Literature References
PubMed ID Title Journal Year
15687497 Identification of human aminopeptidase O, a novel metalloprotease with structural similarity to aminopeptidase B and leukotriene A4 hydrolase

Fueyo, A, Quesada, V, Sánchez, LM, López-Otin, C, Suárez, MF, Díaz-Perales, A, Ugalde, AP

J Biol Chem 2005
Catalyst Activity

aminopeptidase activity of AOPEP:Zn2+ [cytosol]

Orthologous Events
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