MME:Zn2+ hydrolyses AGT(34-43)

Stable Identifier
R-HSA-2022396
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
Neprilysin hydrolyzes Angiotensin-(1-10) to Angiotensin-(1-7), Neprilysin Hydrolyzes Angiotensin I to Yield Angiotensin-(1-7)
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Neprilysin (MME aka neutral endopeptidase NEP) hydrolyzes angiotensin-(1-10) (AGT(34-43), angiotensin I) directly to angiotensin-(1-7) (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
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
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
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
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Event Information
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Catalyst Activity

metallopeptidase activity of MME:Zn2+ [plasma membrane]

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