EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
3.4.24.B14 | 3-methoxysuccinyl-Gly-Leu-Phe-Met-7-amido-4-methylcoumarin + H2O |
- |
Rattus norvegicus |
3-methoxysuccinyl-Gly-Leu + Phe-Met-7-amido-4-methylcoumarin |
- |
? |
3.4.24.B14 | amyloid beta peptide + H2O |
- |
Homo sapiens |
? |
- |
? |
3.4.24.B14 | amyloid beta peptide1-42 + H2O |
- |
Homo sapiens |
? |
- |
? |
3.4.24.B14 | angiotensin + H2O |
cleavage sites: DRVY-/-IHP-/-FHL |
Rattus norvegicus |
? |
- |
? |
3.4.24.B14 | angiotensin I + H2O |
- |
Mus musculus |
? |
- |
? |
3.4.24.B14 | angiotensin I + H2O |
hydrolyzed to 92% |
Homo sapiens |
? |
- |
? |
3.4.24.B14 | Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O |
i.e. substance P(1-11), Arg-Pro-Lys-Pro-Gln-Gln-/-Phe-Phe-Gly-/-Leu-Met-NH2. Hydrolysis of substance P and derivatives occurs predominantly at the Gly9-/-Leu10 bond in the case of neprilysin and neprilysin 2. In addition neprilysin 2 cleaves at the Gln6-Phe7 bond |
Rattus norvegicus |
Arg-Pro-Lys-Pro-Gln-Gln + Phe-Phe-Gly + Leu-Met-NH2 |
- |
? |
3.4.24.B14 | Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O |
i.e. bradykinin |
Rattus norvegicus |
Arg-Pro-Pro-Gly-Phe-Ser-Pro + Phe-Arg |
- |
? |
3.4.24.B14 | Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + H2O |
i.e. angiotensin |
Rattus norvegicus |
Asp-Arg-Val-Tyr-Ile-His-Pro + Phe-His-Leu |
- |
? |
3.4.24.B14 | Asp-Tyr(sulfated)-Met-Gly-Trp-Met-Asp-Phe-NH2 + H2O |
i.e. cholecystokinin-8(sulfated). In cholecystokinins and derivatives, clear differences between neprilysin (EC 3.4.24.11) and neprilysin 2 can be observed: NEP2 does not attack the Asp7-/-Phe8-NH2 bond, a preferential cleavage site for neprilysin (EC 3.4.24.11, NEP) but cleaves the Gly4-/-Trp5 amide bond |
Rattus norvegicus |
Asp-Tyr(sulfated)-Met-Gly + Trp-Met-Asp-Phe-NH2 |
- |
? |