Reactome | MME:Zn2+ (Neprilysin) hydrolyses AGT(25-33) (Angiotensin-(1-9)) to AGT(25-31) (Angiotensin-(1-7)

MME:Zn2+ (Neprilysin) hydrolyses AGT(25-33) (Angiotensin-(1-9)) to AGT(25-31) (Angiotensin-(1-7)

Stable Identifier

R-HSA-2022368

Type

Reaction [transition]

Species

Homo sapiens

Compartment

extracellular region, plasma membrane

Synonyms

Neprilysin hydrolyzes Angiotensin-(1-9) to Angiotensin-(1-7)

ReviewStatus

5/5

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MME:Zn2+ (Neprilysin) hydrolyses AGT(25-33) (Angiotensin-(1-9)) to AGT(25-31) (Angiotensin-(1-7)

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Neprilysin (MME aka neutral endopeptidase NEP) hydrolyzes angiotensin-(1-9) (AGT(34-42)) to yield angiotensin-(1-7) (Rice et al. 2004). The hydrolysis of angiotensin-(1-9) catalyzed by neprilysin is more efficient than that catalyzed by angiotensin-converting enzyme (ACE) (Rice et al. 2004). MME is the major enzyme involved in the metabolic inactivation of a number of bioactive signaling peptides including the enkephalins, substance P, endothelin, bradykinin, atrial natriuretic factor, and the incretin hormone glucagon-like peptide 1. MME requires zinc as cofactor (Oefner et al. 2004, Oefner et al. 2007).

Literature References

PubMed ID	Title	Journal	Year
14747736	Structural analysis of neprilysin with various specific and potent inhibitors Oefner, C, Roques, BP, Fournie-Zaluski, MC, Dale, GE	Acta Crystallogr D Biol Crystallogr	2004
17704566	Structural studies of a bifunctional inhibitor of neprilysin and DPP-IV Oefner, C, Pierau, S, Schulz, H, Dale, GE	Acta Crystallogr D Biol Crystallogr	2007
15283675	Evaluation of angiotensin-converting enzyme (ACE), its homologue ACE2 and neprilysin in angiotensin peptide metabolism Rice, GI, Thomas, DA, Grant, PJ, Turner, AJ, Hooper, NM	Biochem J	2004