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3-methoxysuccinyl-Gly-Leu-Phe-Met-7-amido-4-methylcoumarin + H2O
3-methoxysuccinyl-Gly-Leu + Phe-Met-7-amido-4-methylcoumarin
-
-
-
?
amyloid beta peptide + H2O
?
-
-
-
?
amyloid beta peptide1-42 + H2O
?
-
-
-
?
angiotensin + H2O
?
-
cleavage sites: DRVY-/-IHP-/-FHL
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
Arg-Pro-Lys-Pro-Gln-Gln + Phe-Phe-Gly + Leu-Met-NH2
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
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro + Phe-Arg
i.e. bradykinin
-
-
?
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + H2O
Asp-Arg-Val-Tyr-Ile-His-Pro + Phe-His-Leu
i.e. angiotensin
-
-
?
Asp-Tyr(sulfated)-Met-Gly-Trp-Met-Asp-Phe-NH2 + H2O
Asp-Tyr(sulfated)-Met-Gly + Trp-Met-Asp-Phe-NH2
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
-
-
?
Asp-Tyr-Met-Gly-Trp-Met + H2O
Asp-Tyr-Met-Gly + Trp-Met
i.e. cholecystokinin-(1-6)
-
-
?
Asp-Tyr-Met-Gly-Trp-Met-Asp-Phe-NH2 + H2O
Asp-Tyr-Met-Gly + Trp-Met-Asp-Phe-NH2
i.e. cholecystokinin-8(non-sulfated)
-
-
?
atrial natriuretic peptide + H2O
?
-
-
?
cholecystokinin(1-6) + H2O
?
-
cleavage site: DYMG-/-WM
-
-
?
cholecystokinin-8 + H2O
?
-
cleavage site: DYMG-/-WMDF-NH2
-
-
?
Drosophila tachykinin-1 + H2O
APTSS + FIGMR-amide
Drosophila tachykinin-2 + H2O
APLAFYG + Leu-Arg-amide
Drosophila tachykinin-3 + H2O
APTG + FTGMR-amide
Drosophila tachykinin-4 + H2O
APVNS + FVGMR-amide
Drosophila tachykinin-5 + H2O
APNG + FLGMR-amide
Drosophila tachykinin-6 + H2O
QQR + Phe + ADFNSKFVAVR-amide
-
17% activity compared to Locusta tachykinin-1
-
-
?
endothelin-1 + H2O
?
-
-
?
Gly-Gly-Phe-Met + H2O
Gly-Gly + Phe-Met
i.e. Des-[Tyr1, Met5]enkephalin
-
-
?
Gly-Trp-Met-Asp-Phe-NH2 + H2O
Gly + Trp-Met-Asp-Phe-NH2
i.e. cholecystokinin-(4-8)
-
-
?
gonadotropin-releasing hormone + H2O
?
GPSGFYGVR-NH2 + H2O
GPSGFYG + VR-NH2
Q9XZ01
-
-
-
?
Leu5-enkephalin + H2O
?
-
cleavage site: YGG-/-FL
-
-
?
Leu5-enkephalin-NH2 + H2O
?
-
cleavage site: YGG-/-FL-NH2
-
-
?
Locusta tachykinin-1 + H2O
GPSGFYG + Val-amide
-
100% activity
-
-
?
locustatachykinin 1 + H2O
?
-
-
-
-
?
NEP fluorogenic substrate + H2O
?
hydrolyzed to 39%
-
-
?
Phe-Gly-Leu-Met-NH2 + H2O
Phe-Gly + Leu-Met-NH2
i.e. substance P(8-11)
-
-
?
Phe-Phe-Gly-Leu-Met-NH2 + H2O
Phe-Phe-Gly + Leu-Met-NH2
i.e. substance P(7-11)
-
-
?
succinyl-Ala-Ala-Phe-4-methylcoumarin 7-amide + H2O
succinyl-Ala-Ala + Phe-4-methylcoumarin 7-amide
-
-
-
-
?
succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala + Phe-7-amido-4-methylcoumarin
succinyl-Ala-Ala-Val-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala + Val-7-amido-4-methylcoumarin
-
-
-
?
Tyr-Gly-Ala-Phe-Met + H2O
Tyr-Gly-Ala + Phe-Met
i.e. [L-Ala3,Met5]enkephalin
-
-
?
Tyr-Gly-Gly-Phe-Leu + H2O
Tyr-Gly-Gly + Phe-Leu
i.e. [Leu5]enkephalin
-
-
?
Tyr-Gly-Gly-Phe-Leu-NH2 + H2O
Tyr-Gly-Gly + Phe-Leu-NH2
i.e. [Leu5]enkephalin-NH2
-
-
?
Tyr-Gly-Gly-Phe-Met + H2O
Tyr-Gly-Gly + Phe-Met
i.e. [Met5]enkephalin. Regarding enkephalins and related opioid peptides, neprilysin (EC 3.4.24.11, NEP) and neprilysin 2 (NEP2) cleave the same Gly-/-Phe bond in all susceptible peptides, and hydrolysis by NEP2 and NEP is strongly reduced when the C-terminal carboxylate is amidated. Differences are: Ala instead of Gly in P1 significantly enhances hydrolysis by NEP2 but not NEP, whereas Leu instead of Met in P2' has an opposite influence (whereas affinity is enhanced) on NEP2. In contrast, neither affinity nor hydrolysis was significantly affected by the latter change in the case of NEP (EC 3.4.24.11)
-
-
?
Tyr-Gly-Gly-Phe-Met-NH2 + H2O
Tyr-Gly-Gly + Phe-Met-NH2
i.e. [Met5]enkephalin-NH2
-
-
?
additional information
?
-
angiotensin I + H2O
?
hydrolyzed to 92%
-
-
?
angiotensin I + H2O
?
-
-
?
bradykinin + H2O
?
hydrolyzed to 57%
-
-
?
bradykinin + H2O
?
-
cleavage sites: RPPGFSP-/-FR
-
-
?
Drosophila tachykinin-1 + H2O
APTSS + FIGMR-amide
-
3% activity compared to Locusta tachykinin-1
-
-
?
Drosophila tachykinin-1 + H2O
APTSS + FIGMR-amide
-
3% activity compared to Locusta tachykinin-1
-
-
?
Drosophila tachykinin-2 + H2O
APLAFYG + Leu-Arg-amide
-
33% activity compared to Locusta tachykinin-1
-
-
?
Drosophila tachykinin-2 + H2O
APLAFYG + Leu-Arg-amide
-
33% activity compared to Locusta tachykinin-1
-
-
?
Drosophila tachykinin-3 + H2O
APTG + FTGMR-amide
-
1% activity compared to Locusta tachykinin-1
-
-
?
Drosophila tachykinin-3 + H2O
APTG + FTGMR-amide
-
1% activity compared to Locusta tachykinin-1
-
-
?
Drosophila tachykinin-4 + H2O
APVNS + FVGMR-amide
-
8% activity compared to Locusta tachykinin-1
-
-
?
Drosophila tachykinin-4 + H2O
APVNS + FVGMR-amide
-
8% activity compared to Locusta tachykinin-1
-
-
?
Drosophila tachykinin-5 + H2O
APNG + FLGMR-amide
-
2% activity compared to Locusta tachykinin-1
-
-
?
Drosophila tachykinin-5 + H2O
APNG + FLGMR-amide
-
2% activity compared to Locusta tachykinin-1
-
-
?
gonadotropin-releasing hormone + H2O
?
-
-
-
?
gonadotropin-releasing hormone + H2O
?
cleavage site: pEHWSYG-/-LRPG-NH2
-
-
?
protein + H2O
peptides
-
-
?
protein + H2O
peptides
-
-
?
protein + H2O
peptides
broad substrate specificity
-
?
Substance P + H2O
?
completely hydrolyzed
-
-
?
Substance P + H2O
?
-
-
?
Substance P + H2O
?
-
cleavage sites: RPKPQQ-/-FFG-/-LM-NH2
-
-
?
succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala + Phe-7-amido-4-methylcoumarin
-
-
-
-
?
succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala + Phe-7-amido-4-methylcoumarin
-
-
-
?
additional information
?
-
-
NEP2 plays a role in renal function and spermatogenesis
-
-
?
additional information
?
-
neprilysin-2 shows a much restriceted substrate specificity compared to neprilysin
-
-
?
additional information
?
-
-
neprilysin-2 shows a much restriceted substrate specificity compared to neprilysin
-
-
?
additional information
?
-
human neprilysin-2 has a more restricted substrate specificity compared to human neprilysin, EC 3.4.24.11, with less activity against several vasoactive peptides
-
-
?
additional information
?
-
-
does not cleave dansyl-D-Ala-Gly-p-nitro-Phe-Gly
-
-
?
additional information
?
-
in vivo in cells membrane-bound isoforms mNEP2-alpha and mNEP2-beta have similar activity against amyloid beta peptide Ab40 and Ab42 compared to neprilysin, EC 3.4.24.11
-
-
?
additional information
?
-
in vitro membrane-bound isoform mNEP2-alpha has slower and weaker amyloid beta peptide Ab40 degrading properties when compared to neprilysin, EC 3.4.24.11, and shows little to no effect on amyloid beta peptide Ab42. Membrane-bound isozymes mNEP2-beta and gamma have nearly undetectable activity against amyloid beta peptide
-
-
?
additional information
?
-
the following synthetic substrates are not hydrolysed by either isoform of NEP2: succinyl-Gly-Pro-7-amido-4-methylcoumarin, 3-methoxysuccinyl-Ala-Ala-Pro-Met-7-amido-4-methylcoumarin, 3-methoxysuccinyl-ASp-Tyr-Met-7-amido-4-methylcoumarin, benzyloxycarbony-Arg-7-amido-4-methylcoumarin, tert-butyloxycarbonyl-Val-Gly-Arg-7-amido-4-methylcoumarin, benzyloxycarbonyl-Arg-7-amido-4-methylcoumarin, tert-butyloxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin and tert-butyloxycarbonyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
-
-
?
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1,10-phenanthroline
inhibition of the soluble isozyme SEP
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2
-
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu
-
Asp-Tyr(sulfated)-Met-Gly-Trp-Met-Asp-Phe-NH2
-
Asp-Tyr-Met-Gly-Trp-Met
-
Asp-Tyr-Met-Gly-Trp-Met-Asp-Phe-NH2
-
calcium ionophore A23187
-
0.001 mM
EDTA
1 mM, complete inhibition
gonadotropin-releasing hormone
-
N-[(2S)-3-phenyl-2-(sulfanylmethyl)propanoyl]-L-tryptophan
-
Phe-Phe-Gly-Leu-Met-NH2
-
succinyl-Ala-Ala-Phe-4-methylcoumarin 7-amide
-
37°C, pH 7.2, wild-type enzyme
tunicamycin
-
inhibition of N-glycosylation by tunicamycin reduces the enzymatic activity of extracellular NEP2 to about 50% and the molecular size of intracellular NEP2
Tyr-Gly-Gly-Phe-Leu-NH2
-
Tyr-Gly-Gly-Phe-Met-NH2
-
fasidotrilat
fasidotrilat interacts with the Arg661 of hNEP-2 with more consistent bidentate hydrogen bonding and with weaker His658 with monodentate hydrogen bonding. The extended conformation of the inhibitor in the hNEP2 pocket might be the reason for its weak interactions
omapatrilat
-
phosphoramidon
-
-
phosphoramidon
approximately 8-fold more potent against neprilysin (EC 3.4.24.11) than neprilysin-2
phosphoramidon
weak interactions with hNEP-2
phosphoramidon
inhibition of the soluble isozyme SEP
phosphoramidon
the inhibitor induces a dramatic increase in amyloid-beta peptide levels
thiorphan
-
weak inhibition
thiorphan
far more potent against neprilysin (EC 3.4.24.11) than neprilysin-2
thiorphan
Arg66a acts to support the ligand binding in NEP-2
thiorphan
inhibition of the soluble isozyme SEP
thiorphan
the inhibitor induces a dramatic increase in amyloid-beta peptide levels
additional information
molecular docking studies, overview. For substrate and inhibitor binding, Arg661 and Zn694 are identified as the most conserved residues
-
additional information
-
molecular docking studies, overview. For substrate and inhibitor binding, Arg661 and Zn694 are identified as the most conserved residues
-
additional information
no inhibition by captopril
-
additional information
-
disruption of the Golgi apparatus with brefeldin A markedly reduces extracellular NEP2 activity in parallel with intracellular NEP2 protein level in HEK293 cells; nocodazole and cytochalasin B barely affect NEP2 activity
-
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0.023 - 0.035
3-methoxysuccinyl-Gly-Leu-Phe-Met-7-amido-4-methylcoumarin
0.04 - 1
succinyl-Ala-Ala-Phe-4-methylcoumarin 7-amide
0.027 - 0.05
succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin
0.04 - 0.1
succinyl-Ala-Ala-Val-7-amido-4-methylcoumarin
0.023
3-methoxysuccinyl-Gly-Leu-Phe-Met-7-amido-4-methylcoumarin
37°C, membrane-bound form of NEP2
0.035
3-methoxysuccinyl-Gly-Leu-Phe-Met-7-amido-4-methylcoumarin
37°C, secreted soluble form of NEP2
0.04
succinyl-Ala-Ala-Phe-4-methylcoumarin 7-amide
-
37°C, pH 7.2, mutant enzyme L739G
0.044
succinyl-Ala-Ala-Phe-4-methylcoumarin 7-amide
-
37°C, pH 7.2, mutant enzyme L739G/S133G
0.045
succinyl-Ala-Ala-Phe-4-methylcoumarin 7-amide
-
37°C, pH 7.2, mutant enzyme R131M
0.062
succinyl-Ala-Ala-Phe-4-methylcoumarin 7-amide
-
37°C, pH 7.2. wild-type enzyme
0.185
succinyl-Ala-Ala-Phe-4-methylcoumarin 7-amide
-
37°C, pH 7.2, mutant enzyme S133G
1
succinyl-Ala-Ala-Phe-4-methylcoumarin 7-amide
-
37°C, pH 7.2, mutant enzyme N567G
0.027
succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin
37°C, membrane-bound form of NEP2
0.05
succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin
37°C, secreted soluble form of NEP2
0.04
succinyl-Ala-Ala-Val-7-amido-4-methylcoumarin
37°C, membrane-bound form of NEP2
0.1
succinyl-Ala-Ala-Val-7-amido-4-methylcoumarin
37°C, secreted soluble form of NEP2
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11.5
3-methoxysuccinyl-Gly-Leu-Phe-Met-7-amido-4-methylcoumarin
37°C
6
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2
37°C
2.5
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
37°C
3
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu
37°C
6.17
Asp-Tyr(sulfated)-Met-Gly-Trp-Met-Asp-Phe-NH2
37°C
34.5
Asp-Tyr-Met-Gly-Trp-Met
37°C
13.17
Asp-Tyr-Met-Gly-Trp-Met-Asp-Phe-NH2
37°C
4
Gly-Trp-Met-Asp-Phe-NH2
37°C
8.5
gonadotropin-releasing hormone
37°C
22.83
Phe-Gly-Leu-Met-NH2
37°C
50
Phe-Phe-Gly-Leu-Met-NH2
37°C
0.52 - 30.7
succinyl-Ala-Ala-Phe-4-methylcoumarin 7-amide
8.5
succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin
37°C
13.8
succinyl-Ala-Ala-Val-7-amido-4-methylcoumarin
37°C
41.7
Tyr-Gly-Ala-Phe-Met
37°C
2.7
Tyr-Gly-Gly-Phe-Leu
37°C
0.33
Tyr-Gly-Gly-Phe-Leu-NH2
37°C
9
Tyr-Gly-Gly-Phe-Met
37°C
0.33
Tyr-Gly-Gly-Phe-Met-NH2
37°C
0.52
succinyl-Ala-Ala-Phe-4-methylcoumarin 7-amide
-
37°C, pH 7.2, wild-type enzyme
1.2
succinyl-Ala-Ala-Phe-4-methylcoumarin 7-amide
-
37°C, pH 7.2, mutant enzyme W774A
1.97
succinyl-Ala-Ala-Phe-4-methylcoumarin 7-amide
-
37°C, pH 7.2, mutant enzyme S133G
3.5
succinyl-Ala-Ala-Phe-4-methylcoumarin 7-amide
-
37°C, pH 7.2, mutant enzyme P764Y
5.23
succinyl-Ala-Ala-Phe-4-methylcoumarin 7-amide
-
37°C, pH 7.2, mutant enzyme N567G
7.8
succinyl-Ala-Ala-Phe-4-methylcoumarin 7-amide
-
37°C, pH 7.2, mutant enzyme W774F
8.7
succinyl-Ala-Ala-Phe-4-methylcoumarin 7-amide
-
37°C, pH 7.2, wild-type enzyme
14.03
succinyl-Ala-Ala-Phe-4-methylcoumarin 7-amide
-
37°C, pH 7.2, wild-type enzyme
17.3
succinyl-Ala-Ala-Phe-4-methylcoumarin 7-amide
-
37°C, pH 7.2, mutant enzyme R131M
19
succinyl-Ala-Ala-Phe-4-methylcoumarin 7-amide
-
37°C, pH 7.2, mutant enzyme L739G/S133G
30.7
succinyl-Ala-Ala-Phe-4-methylcoumarin 7-amide
-
37°C, pH 7.2, mutant enzyme L739G
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0.008
angiotensin
-
37°C, pH 7.2, wild-type enzyme
0.004
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2
-
0.002
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
37°C
0.006
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu
37°C
0.021
Asp-Tyr(sulfated)-Met-Gly-Trp-Met-Asp-Phe-NH2
37°C
0.018
Asp-Tyr-Met-Gly-Trp-Met
37°C
0.05
Asp-Tyr-Met-Gly-Trp-Met-Asp-Phe-NH2
37°C
0.003
bradykinin
-
37°C, pH 7.2, wild-type enzyme
0.05
cholecystokinin(1-6)
-
37°C, pH 7.2, wild-type enzyme
0.01
cholecystokinin-8
-
37°C, pH 7.2, wild-type enzyme
0.000016 - 0.000019
fasidotrilat
0.014
Gly-Gly-Phe-Met
37°C
0.018
gonadotropin-releasing hormone
37°C
0.02
Leu-Met
-
37°C, pH 7.2, wild-type enzyme
0.175
Leu-Met-NH2
-
37°C, pH 7.2, wild-type enzyme
0.002
Leu5-enkephalin
-
37°C, pH 7.2, wild-type enzyme
0.02
Leu5-enkephalin-NH2
-
37°C, pH 7.2, wild-type enzyme
0.000008 - 0.000017
omapatrilat
0.09
Phe-Phe-Gly-Leu-Met-NH2
-
0.0000008 - 0.000002
phosphoramidon
0.011
Substance P
-
37°C, pH 7.2, wild-type enzyme
0.00012 - 0.00025
thiorphan
0.039
Trp-Met-Asp-Phe-NH2
37°C
0.03
Tyr-Gly-Ala-Phe-Met
37°C
0.0035
Tyr-Gly-Gly-Phe-Leu
37°C
0.021
Tyr-Gly-Gly-Phe-Leu-NH2
37°C
0.01
Tyr-Gly-Gly-Phe-Met
37°C
0.025
Tyr-Gly-Gly-Phe-Met-NH2
37°C
0.021
Val-Phe
-
37°C, pH 7.2, wild-type enzyme
0.13
Val-Phe-NH2
-
37°C, pH 7.2, wild-type enzyme
0.000016
fasidotrilat
37°C, secreted soluble form of NEP2
0.000019
fasidotrilat
37°C, membrane-bound form of NEP2
0.000008
omapatrilat
37°C, secreted soluble form of NEP2
0.000008
omapatrilat
pH and temperature not specified in the publication
0.000017
omapatrilat
37°C, membrane-bound form of NEP2
0.0000008
phosphoramidon
37°C, secreted soluble form of NEP2
0.000002
phosphoramidon
37°C, membrane-bound form of NEP2
0.00012
thiorphan
37°C, secreted soluble form of NEP2
0.00025
thiorphan
37°C, membrane-bound form of NEP2
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evolution
neprilysin-2 is also a zinc metalloendopeptidase belonging to the same M13 family as neprilysin
evolution
neprilysin-2 is also a zinc metalloendopeptidase belonging to the same M13 family as neprilysin
evolution
sequence comparisons of NEP (EC 3.4.24.11) and NEP-2
malfunction
-
mice deficient for the NEP2 gene show significant elevations in total amyloid-beta peptide species in the hippocampus and brainstem/diencephalon (1.5fold). Increases in amyloid-beta peptide accumulation are more dramatic in NEP2 knockout mice crossbred with APP transgenic mice. In NEP/NEP2 double-knockout mice, amyloid-beta peptide levels are marginally increased (1.5 to 2fold), compared with NEP-/-/NEP2+/+ controls. Treatment of these double-knockout mice with phosphoramidon results in elevations of amyloid-beta peptide, suggesting that yet other NEP-like amyloid-beta peptide -degrading endopeptidases are contributing to amyloid-beta peptide catabolism
malfunction
NEP2 knockout mice show reduced sperm function
malfunction
reduced enzyme activity in association with mild-cognitive impaired subjects and Alzheimer's disease subjects regardless of sex
metabolism
neprilysin-2 (NEP2), a NEP-like endopeptidase, cooperates with neprilysin (NEP, EC 3.4.24.11) to control amyloid-beta peptide levels in the brain
metabolism
neprilysin-2 (NEP2), a NEP-like endopeptidase, cooperates with neprilysin (NEP, EC 3.4.24.11) to control amyloid-beta peptide levels in the brain
metabolism
neprilysin-2 (NEP2) in the central nervous system controls Alzheimer's protein (amyloid-beta) deposition, and prevents its occurrence, while in the peripheral system, its closest homologue, neutral endopeptidase neprilysin (NEP, EC 3.4.24.11), regulates hypertension and heart related diseases
physiological function
NEP-like proteases, e.g. neprilysin-2, are important because of their potential involvement in the spike in amyloid beta peptide levels posttreatment with NEP inhibitors. Neprilysin-2 has importance in amyloid peptide regulation
physiological function
NEP-like proteases, e.g. neprilysin-2, are important because of their potential involvement in the spike in amyloid beta peptide levels posttreatment with NEP inhibitors. The enzyme might play a role in the metabolism of neuropeptides of the hypothalamo-pituitary axis
physiological function
neprilysin-2 (NEP2) in the central nervous system controls Alzheimer's protein (amyloid-beta) deposition, and prevents its occurrence
additional information
enzyme splice variants and their involvement in amloid beta peptide cleavage, overview
additional information
enzyme splice variants and their involvement in amyloid beta peptide cleavage, overview
additional information
molecular dynamics (MD) simulations of NEP-2 and modelling, overview. For substrate and inhibitor binding, Arg661 and Zn694 are identified as the most conserved residues
additional information
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molecular dynamics (MD) simulations of NEP-2 and modelling, overview. For substrate and inhibitor binding, Arg661 and Zn694 are identified as the most conserved residues
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