MME:Zn2+ (Neprilysin) hydrolyses AGT(34-42)

Stable Identifier
R-HSA-2022368
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
Neprilysin hydrolyzes Angiotensin-(1-9) to Angiotensin-(1-7)
ReviewStatus
5/5
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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

Fournie-Zaluski, MC, Roques, BP, Dale, GE, Oefner, C

Acta Crystallogr D Biol Crystallogr 2004
17704566 Structural studies of a bifunctional inhibitor of neprilysin and DPP-IV

Dale, GE, Oefner, C, Pierau, S, Schulz, H

Acta Crystallogr D Biol Crystallogr 2007
15283675 Evaluation of angiotensin-converting enzyme (ACE), its homologue ACE2 and neprilysin in angiotensin peptide metabolism

Hooper, NM, Turner, AJ, Grant, PJ, Thomas, DA, Rice, GI

Biochem J 2004
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Catalyst Activity

metallopeptidase activity of MME:Zn2+ [plasma membrane]

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