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Information on EC 3.4.24.16 - neurolysin and Organism(s) Rattus norvegicus and UniProt Accession P42676
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3.4.24.16 neurolysinSpecify your search results
Word Map
- 3.4.24.16
- bradykinin
- metallopeptidase
- metalloendopeptidase
- dynorphins
- pro-ile
-
neuropeptidase
-
pro10-tyr11
-
neuromedin
- hemopressins
-
arg8-arg9
-
non-at2
-
neurotensin-degrading
- molecular biology
- pharmacology
- medicine
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
neurolysin, ep24.16, endopeptidase 24.16, ep 24.16, mitochondrial peptidase, oligopeptidase m, soluble angiotensin-binding protein, microsomal endopeptidase, soluble angiotensin ii-binding protein, neurotensin endopeptidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
endopeptidase 24.16
endopeptidase 24.16B
-
-
-
-
MEP
-
-
-
-
Microsomal endopeptidase
MOP
-
-
-
-
neurotensin endopeptidase
-
-
-
-
oligopeptidase M
peptidase, neurotensin endo
-
-
-
-
peptidase, neurotensin endo-
-
-
-
-
SABP
-
-
-
-
Soluble angiotensin-binding protein
-
-
-
-
thimet oligopeptidase II
-
neurolysin is most likely to be confused with thimet oligopeptidase II, but it is distinguished by its lack of activation by thiol compounds, inhibition by millimolar concentrations of Pro-Ile, cleavage of neurotensin at the Pro-Tyr bond, and different mobility in column chromatography
additional information
endopeptidase 24.16
-
-
-
-
Microsomal endopeptidase
-
-
-
-
oligopeptidase M
-
-
-
-
additional information
-
neurolysin belongs to the M3 metallopeptidase family
additional information
-
the enzyme belongs to the zinc-dependent peptidases of the metallopeptidase M3 family
CAS REGISTRY NUMBER
COMMENTARY
149371-24-4
-
90463-53-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-aminobenzoyl-dynorphin A(1-8)-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
binding structure and conformational effects on the enzyme compared to inhibitor R2
-
-
?
2-aminobenzoyl-neurotensin-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
binding structure and conformational effects on the enzyme compared to inhibitor R2
-
-
?
(7-methoxy-coumarin-4-yl)acetyl-RPKPVE-Nva-WRK(2,4-dinitrophenyl)-NH2 + H2O
(7-methoxy-coumarin-4-yl)acetyl-RPKP + YA-Nva-WMK(2,4-dinitrophenyl)-NH2
-
substrate of matrix metalloproteinases MMP3
cleavage at the peptide bond between proline and tyrosine, withabout 1/10 efficiency in wild-type compared with the cleavage of the MMPs-2/9-specific peptide (7-methoxy-coumarin-4-yl)acetyl-RPKPYA-Nva-WMK(2,4-dinitrophenyl)-NH2
-
?
(7-methoxy-coumarin-4-yl)acetyl-RPKPYA-Nva-WMK(2,4-dinitrophenyl)-NH2 + H2O
(7-methoxy-coumarin-4-yl)acetyl-RPKP + YA-Nva-WMK(2,4-dinitrophenyl)-NH2
-
substrate of matrix metalloproteinases MMP-2/-9
cleavage at the peptide bond between proline and tyrosine
-
?
(7-methoxycoumarin-4-yl)acetyl-Gly-Gly-Phe-Ile-Arg-Arg-Ala-Lys-dinitrophenyl + H2O
(7-methoxycoumarin-4-yl)acetyl-Gly-Gly-Phe-Ile-Arg-Arg + Ala-Lys-dinitrophenyl
(7-methoxycoumarin-4-yl)acetyl-Gly-Gly-Phe-Leu-Arg-Arg-Ala-Lys-dinitrophenyl + H2O
peptide fragments
-
i.e. QF34, cleavage sites: Leu4-Arg5, Arg5-Arg6
-
-
?
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-Lys-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl) + H2O
?
-
-
-
?
acetyl-Arg-Arg-Pro-Tyr-Ile-Leu + H2O
acetyl-Arg-Arg-Pro + Tyr-Ile-Leu
-
i.e. acetyneurotensin(8-13)
-
?
Ala-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-Thr-Phe-Thr-Ser-Cys + H2O
?
-
i.e. somatostatin, cleavage sites: Phe6-Phe7, Thr10-Phe11
-
-
?
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 + Arg-Pro-Lys-Pro-Gln-Gln + Phe-Phe-Gly-Leu-Met-NH2 + Arg-Pro-Lys-Pro
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
i.e. angiotensin II
-
?
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + H2O
Asp-Arg-Val-Tyr-Ile-His-Pro + Phe-His-Leu
-
-
-
-
?
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu + H2O
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro + Tyr-Ile-Leu
Tyr-Gly-Gly-Phe-Leu-Arg-Arg + H2O
?
-
cleavage sites: Phe4-Leu5, Leu5-Arg6
-
-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile + H2O
?
-
cleavage sites: Leu-5-Arg6, Arg6-Arg7
-
-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile + H2O
Tyr-Gly-Gly-Phe-Leu + Arg-Arg-Ile
-
-
-
-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg + H2O
Tyr-Gly-Gly-Phe-Leu-Arg-Arg + Ile-Arg
-
-
-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln + H2O
peptide fragments
[(7-methoxycoumarin-4-yl)acetyl]-APAKFFRLK(Dnp)-NH2 + H2O
[(7-methoxycoumarin-4-yl)acetyl]-APAK + FFRLK(Dnp)-NH2
-
best substrate
-
-
?
[(7-methoxycoumarin-4-yl)acetyl]-DEVDAPK(Dnp)-NH2 + H2O
?
-
very low activity
-
-
?
[(7-methoxycoumarin-4-yl)acetyl]-GKPILFFRLK(Dnp)DR-NH2 + H2O
[(7-methoxycoumarin-4-yl)acetyl]-GKP + ILFFRLK(Dnp)DR-NH2
-
high activity
-
-
?
[(7-methoxycoumarin-4-yl)acetyl]-GKPILFFRLK(Dnp)DR-NH2 + H2O
[(7-methoxycoumarin-4-yl)acetyl]-GKPIL + FFRLK(Dnp)DR-NH2
-
high activity
-
-
?
[(7-methoxycoumarin-4-yl)acetyl]-GSPAFLAK(Dnp)DR-NH2 + H2O
[(7-methoxycoumarin-4-yl)acetyl]-GSPA + FLAK(Dnp)DR-NH2
-
low activity
-
-
?
[(7-methoxycoumarin-4-yl)acetyl]-RPKPYANvaWMK(Dnp)-NH2 + H2O
?
-
a substrate of MMP-2 and MMP-9
-
-
?
[(7-methoxycoumarin-4-yl)acetyl]-RPKPYANvaWMK(Dnp)-NH2 + H2O
[(7-methoxycoumarin-4-yl)acetyl]-RPKP + YANvaWMK(Dnp)-NH2
-
high activity
-
-
?
[(7-methoxycoumarin-4-yl)acetyl]-RPKPYANvaWMK(Dnp)-NH2 + H2O
[(7-methoxycoumarin-4-yl)acetyl]-RPKPY + ANvaWMK(Dnp)-NH2
-
high activity
-
-
?
[(7-methoxycoumarin-4-yl)acetyl]-RPPGFSAFK(Dnp)-OH + H2O
[(7-methoxycoumarin-4-yl)acetyl]-RPPGFSA + FK(Dnp)-OH
-
low activity
-
-
?
neurotensin + H2O
?
secreted neuropeptide, major cleavage is the Pro10-Tyr11 bond, but not the Arg8-Arg9 bond. Neurotensin in which Tyr 11 is replaced by a D-Tyr11 or D-Phe11 residue fully resists degradation both in vitro as well as in vivo, after intracerebroventricular administration in rat
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Gly-Gly-Phe-Ile-Arg-Arg-Ala-Lys-dinitrophenyl + H2O
(7-methoxycoumarin-4-yl)acetyl-Gly-Gly-Phe-Ile-Arg-Arg + Ala-Lys-dinitrophenyl
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Gly-Gly-Phe-Ile-Arg-Arg-Ala-Lys-dinitrophenyl + H2O
(7-methoxycoumarin-4-yl)acetyl-Gly-Gly-Phe-Ile-Arg-Arg + Ala-Lys-dinitrophenyl
-
i.e. QF37, cleavage site: Arg6-Ala7
-
?
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 + Arg-Pro-Lys-Pro-Gln-Gln + Phe-Phe-Gly-Leu-Met-NH2 + Arg-Pro-Lys-Pro
-
-
-
-
?
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 + Arg-Pro-Lys-Pro-Gln-Gln + Phe-Phe-Gly-Leu-Met-NH2 + Arg-Pro-Lys-Pro
-
cleavage sites: Gln5-Gln6, Phe8-Gly9
-
-
?
neurotensin + H2O
?
-
neurolysin regulates the amount of bioactive peptide neurotensin, which functions in the modulation of central dopaminergic and cholinergic circuits, thermoregulation, intestinal motility, and blood pressure regulation. In cancer cells, neurotensin accelerates cell progression
-
-
?
neurotensin + H2O
?
-
determination of specific cleavage sites, overview
-
-
?
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu + H2O
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro + Tyr-Ile-Leu
-
-
-
-
?
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu + H2O
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro + Tyr-Ile-Leu
-
-
-
?
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu + H2O
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro + Tyr-Ile-Leu
-
-
-
-
?
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu + H2O
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro + Tyr-Ile-Leu
-
-
-
?
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu + H2O
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro + Tyr-Ile-Leu
-
-
-
?
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu + H2O
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro + Tyr-Ile-Leu
-
-
-
?
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu + H2O
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro + Tyr-Ile-Leu
-
-
-
-
?
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu + H2O
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro + Tyr-Ile-Leu
-
i.e. neurotensin
-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln + H2O
peptide fragments
-
i.e. dynorphin A(1-17), cleavage sites: Lys11-Leu12, Leu12-Lys13
-
-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln + H2O
peptide fragments
-
cleavage sites: Lys11-Leu12, Leu12-Lys13
-
-
?
additional information
?
-
models of substrate binding in the neurolysin active site channel, overview
-
-
?
additional information
?
-
QFS and neurotensin compete for their hydrolysis by enzyme Nln
-
-
?
additional information
?
-
-
the enzyme can participate in the physiological inactivation of neurotensin
-
-
?
additional information
?
-
-
EC 3.4.24.16 and EC 3.4.24.15 are responsible for the inactivation of neurotensin, somatostatin, and other neuropeptides in the brain
-
-
?
additional information
?
-
-
the enzyme is likely involved in the physiological termination of the neurotensinergic signal in the central nervous system and in the gastrointestinal tract
-
-
?
additional information
?
-
-
the enzyme cleaves several bioactive peptides at sites similar or different from thimet oligopeptidase, EC 3.4.24.15
-
-
?
additional information
?
-
-
the enzyme is involved in the inactivation of numerous neuropeptides
-
-
?
additional information
?
-
-
activity of the recombinant enzyme with fluorescence-quenching peptides, cleavage site and amino acid preference, overview
-
-
?
additional information
?
-
-
cleavage sites of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
residues His425, Ala426, Cys428, Pro193, Gln482, Asp410, Thr495, Leu397, and Thr471 are involved in substrate recognition, as well as the tyrosine-rich loop 604GGYDGQYYGY613, overview, poor activity with the MMP-3 substrate [(7-methoxycoumarin-4-yl)acetyl]-RPKPVENvaWRK(Dnp[2,4-dinitrophenyl])-NH2
-
-
?
additional information
?
-
-
residues R470, R491, N496, and T499 determine the substrate specificity of thimet oligopeptidase different from closely related thimet oligopeptidase, EC 3.4.24.15
-
-
?
additional information
?
-
-
the catalytic site, with the active site sequence motif HEXXH, is located in a deep channel that provides access only to short peptides, but NEL shows a broad substrate specificity, in part due to the presence of a flexible loop lined with the enzyme binding site of the peptidase
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
neurotensin + H2O
?
-
neurolysin regulates the amount of bioactive peptide neurotensin, which functions in the modulation of central dopaminergic and cholinergic circuits, thermoregulation, intestinal motility, and blood pressure regulation. In cancer cells, neurotensin accelerates cell progression
-
-
?
additional information
?
-
-
the enzyme can participate in the physiological inactivation of neurotensin
-
-
?
additional information
?
-
-
EC 3.4.24.16 and EC 3.4.24.15 are responsible for the inactivation of neurotensin, somatostatin, and other neuropeptides in the brain
-
-
?
additional information
?
-
-
the enzyme is likely involved in the physiological termination of the neurotensinergic signal in the central nervous system and in the gastrointestinal tract
-
-
?
additional information
?
-
-
the enzyme cleaves several bioactive peptides at sites similar or different from thimet oligopeptidase, EC 3.4.24.15
-
-
?
additional information
?
-
-
the enzyme is involved in the inactivation of numerous neuropeptides
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
Zn2+
Zn2+
-
dependent on, neurolysin contains a His-Glu-Xaa-Xaa-His zinc binding motif in its active domain that traps a zinc molecule using two histidine residues
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-adamantan-2-yl-3-[2-[2,3-bis-(2-chloro-phenyl)-pyrazolidin-1-yl]-2-oxo-ethyl]-urea
racemic
3-[(2S)-1-[(3R)-3-(2-chlorophenyl)-2-(2-fluorophenyl)pyrazolidin-1-yl]-1-oxopropan-2-yl]-1-(adamantan-2-yl)urea
R-stereomer, allosteric inhibition of neurolysin, mixed-type inhibition kinetics, the bound inhibitor disrupts activity by preventing a hinge-like motion associated with substrate binding and catalysis. The inhibitor reverses a substrate-associated conformational change
Mcc-Pro-Leu
Nln-mediated hydrolysis of QFS yields a degradation product that triggers a relatively product inhibition
agaricoglyceride A
-
main active principle of the crude extract of Agaricus macrosporus shows strong activity against neurolysin
agaricoglyceride B
-
agaricoglyceride C, agaricoglyceride D, known cometabolites agaricic ester show no activity against neurolysin up to 0.01 mM
dynorphin A1-13
-
inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
dynorphin(1-8)
-
degradation of 3-carboxy-7-methoxycoumaryl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
dynorphin(1-9)
-
degradation of 3-carboxy-7-methoxycoumaryl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
HONHCO-CH2-CH(CH2-C6H5)CO-Ile-Ala
-
potent and selective inhibitor of neurolysin
JA-2
-
i.e. N-[1-(R,S)-carboxy-3-phenylpropyl]Ala-Aib-Tyrp-aminobenzoate, the aromatic ring of Tyr605 was an important anchor for its interaction with wild-type TOP
kinetensin
-
degradation of 3-carboxy-7-methoxycoumaryl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
-
LVVYPWTQRY
-
inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
N-(1(R,S)-carboxy-3-phenylpropyl)-Ala-Ala-Tyr-p-aminobenzoate
-
inhibits EP24.16 resulting in a 1000fold increase in type-2 BK receptor sensitivity to bradykinin as measured by inositol phosphate accumulation
Pro-Phe-PSI(PO2CH2)Leu-Pro-NH2
-
potent and selective inhibitor of neurolysin
Pro-Xaa dipeptides
-
most potent inhibitors, Xaa-Pro dipeptides are ineffective
PVNFKFLSH
-
inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
VVYPWTQRY
-
inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
acetyl-neurotensin(8-13)
-
inhibits degradation of 3-carboxy-7-methoxycoumaryl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
angiotensin I
-
inhibits degradation of 3-carboxy-7-methoxycoumaryl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
angiotensin I
-
inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
angiotensin II
-
degradation of 3-carboxy-7-methoxycoumaryl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
angiotensin II
-
inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
bradykinin
-
degradation of 3-carboxy-7-methoxycoumaryl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
bradykinin
-
inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
Neuromedin N
-
degradation of 3-carboxy-7-methoxycoumaryl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
neurotensin
-
inhibits degradation of 3-carboxy-7-methoxycoumaryl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
neurotensin(9-13)
-
the shortest neurotensin partial sequence that is able to fully inhibit neurotensin degradation
Pro-Ile
-
causes a 100fold leftward shift in the concentration response curve for bradykinin-induced inositol phosphate generation, moreover leads to a potentiation of bradykinin-induced reduction in protein kinase B activity
Pro-Ile
-
selective inhibitor of neurolysin, inhibition by milimolar concentrations
Substance P
-
degradation of 3-carboxy-7-methoxycoumaryl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
Xenopsin
-
degradation of 3-carboxy-7-methoxycoumaryl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
additional information
inhibitor synthesis and evaluation, different kinetic inhibition models, binding structures, modeling, overview
-
additional information
Pro-Ile is unable to affect endopeptidases 24.11 and 24.15, proline endopeptidase, angiotensin-converting enzyme, leucine aminopeptidase, diglutamyl aminopeptidase, and trypsin
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
catalytic activity of recombinant Nln increases over time upon incubation in fresh mouse blood. The recombinant protein easily reaches the systemiccirculation remaining both catalytically active and physically intact
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.002 - 0.0022
(7-methoxycoumarin-4-yl)acetyl-Gly-Gly-Phe-Ile-Arg-Arg-Ala-Lys-dinitrophenyl
0.0043
(7-methoxycoumarin-4-yl)acetyl-Gly-Gly-Phe-Leu-Arg-Arg-Ala-Lys-dinitrophenyl
-
-
additional information
additional information
-
Km-values for the reaction with angiotensin I analogs
-
6
(7-methoxy-coumarin-4-yl)acetyl-RPKPVE-Nva-WRK(2,4-dinitrophenyl)-NH2
-
mutant Y610L, 37°C
14
(7-methoxy-coumarin-4-yl)acetyl-RPKPVE-Nva-WRK(2,4-dinitrophenyl)-NH2
-
wild-type, 37°C
7.7
(7-methoxy-coumarin-4-yl)acetyl-RPKPYA-Nva-WMK(2,4-dinitrophenyl)-NH2
-
wild-type, 37°C
19
(7-methoxy-coumarin-4-yl)acetyl-RPKPYA-Nva-WMK(2,4-dinitrophenyl)-NH2
-
mutant Y610L, 37°C
0.002
(7-methoxycoumarin-4-yl)acetyl-Gly-Gly-Phe-Ile-Arg-Arg-Ala-Lys-dinitrophenyl
-
-
0.0022
(7-methoxycoumarin-4-yl)acetyl-Gly-Gly-Phe-Ile-Arg-Arg-Ala-Lys-dinitrophenyl
-
-
0.0006
2-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.0007
2-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y606F
0.0031
2-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y606A
0.0498
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-Lys-dinitrophenyl
-
abvove
0.0009
Abz-GFSAFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant G608A
0.0011
Abz-GFSAFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.0058
Abz-GFSAFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y606F
0.0078
Abz-GFSAFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y606A
0.0024
Abz-GFSEFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.0053
Abz-GFSEFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y606A
0.0015
Abz-GFSFFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.0025
Abz-GFSFFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant G608A
0.0098
Abz-GFSFFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y606F
0.0101
Abz-GFSFFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y606A
0.0018
Abz-GFSHFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.0059
Abz-GFSHFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant G608A
0.0104
Abz-GFSHFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y606F
0.0106
Abz-GFSHFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y606A
0.0008
Abz-GFSIFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant G608A
0.0008
Abz-GFSIFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.0048
Abz-GFSIFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y606F
0.0018
Abz-GFSLFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.0019
Abz-GFSLFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant G608A
0.0048
Abz-GFSLFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y606F
0.0061
Abz-GFSLFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y606A
0.0016
Abz-GFSQFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.0054
Abz-GFSQFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant G608A
0.0096
Abz-GFSQFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y606F
0.0008
Abz-GFSRFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant G608A
0.0013
Abz-GFSRFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.0019
Abz-GFSRFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y606F
0.0026
Abz-GFSRFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y606A
0.0083
Abz-GFSRFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant G608A
0.0056
Abz-GFSSFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant G608A
0.0074
Abz-GFSSFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y606A
0.0074
Abz-GFSSFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y606F
0.0111
Abz-GFSSFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.0008
Abz-GFSWFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.0022
Abz-GFSWFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y606A
0.0029
Abz-GFSWFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant G608A
0.0012
Abz-GFSyFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant G608A
0.0038
Abz-GFSyFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y606F
0.0065
Abz-GFSyFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y606A
0.0096
Abz-GFSyFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11.9
(7-methoxycoumarin-4-yl)acetyl-Gly-Gly-Phe-Ile-Arg-Arg-Ala-Lys-dinitrophenyl
-
-
2.1
(7-methoxycoumarin-4-yl)acetyl-Gly-Gly-Phe-Leu-Arg-Arg-Ala-Lys-dinitrophenyl
-
-
additional information
additional information
-
turnover-numbers for the reaction with angiotensin I analogs
-
0.76
(7-methoxy-coumarin-4-yl)acetyl-RPKPVE-Nva-WRK(2,4-dinitrophenyl)-NH2
-
wild-type, 37°C
1.1
(7-methoxy-coumarin-4-yl)acetyl-RPKPVE-Nva-WRK(2,4-dinitrophenyl)-NH2
-
mutant Y610L, 37°C
1.9
(7-methoxy-coumarin-4-yl)acetyl-RPKPYA-Nva-WMK(2,4-dinitrophenyl)-NH2
-
mutant Y610L, 37°C
2.1
(7-methoxy-coumarin-4-yl)acetyl-RPKPYA-Nva-WMK(2,4-dinitrophenyl)-NH2
-
wild-type, 37°C
0.006
2-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y606A
0.1
2-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y606F
0.3
2-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
2.6
Abz-GFSAFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.7
Abz-GFSEFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
3.4
Abz-GFSFFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
2.5
Abz-GFSHFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.2
Abz-GFSIFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
3.5
Abz-GFSLFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
3.6
Abz-GFSQFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
4.8
Abz-GFSRFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
7.5
Abz-GFSSFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.3
Abz-GFSWFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00535
angiotensin I
-
inhibition of hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
0.00795
angiotensin II
-
inhibition of hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
0.00811
bradykinin
-
inhibition of hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
0.000022
dynorphin A1-13
-
inhibition of hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
0.00201
LVVYPWTQRY
-
inhibition of hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
0.00343
PVNFKFLSH
-
inhibition of hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
0.00704
VVYPWTQRY
-
inhibition of hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0066
1-adamantan-2-yl-3-[2-[2,3-bis-(2-chloro-phenyl)-pyrazolidin-1-yl]-2-oxo-ethyl]-urea
Rattus norvegicus
pH 7.5, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
quantitative determination of cleavage activity of neurolysin toward MMP-specific fluorescence-quenching peptides
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
pH-dependence of wild-type and mutant enzymes, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
shorter form of neurolysin, lacking the cleavable mitochondrial targeting sequence, remains in the cytosol
-
the transfectants exhibit a membrane-associated form of endopeptidase-24.16, the catalytic site of which clearly faces the extracellular domain
-
the enzyme is not attached by a glycosyl-phosphatidylinositol anchor in the emembrane, the enzyme can not be released from the membrane upon trypsinolysis
-
longer form of neurolysin that contains a cleavable mitochondrial targeting sequence at the N-terminus
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
neuropeptidases specialize in the hydrolysis of the small bioactive peptides that play a variety of signaling roles in the nervous and endocrine systems. Neuropeptidase neurolysin helps control the levels of the dopaminergic circuit modulator neurotensin and is a member of a fold group that includes the antihypertensive target angiotensin converting enzyme
physiological function
the enzyme serves as non-AT1, non-AT2 binding site for angiotensins in the rodent brain and testis, the binding of neurolysin is inhibited by enzyme substrates, peptide screening and competitive binding assays, detailed overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NEUL_RAT
704
0
80254
Swiss-Prot
Mitochondrion (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
additional information
-
Gly608 of NEL contributes to the flexibility of the loops formed by residues 600-612, i.e. GHLAGGYDGQYYG, in NEL, overview
additional information
-
structural comparison between neurolysin and MMP-9, overview
additional information
-
structure analysis and comparisons, modelling, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
no modification
no modification
-
the enzyme contains no glycosyl-phosphatidylinositol anchor
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme with bound inhibitor R2, hanging drop vapor diffusion, mixing 2 ml of 48 mM protein in the presence of 5fold stoichiometric excess of inhibitor R2 with 1 ml of well solution containing 0.1 M HEPES, pH 7.0, 0.1 M LiSO4,2 mM 2-mercaptoethanol, and 12-15% PEG 4000, 4°C, X-ray diffraction structure determination and analysis at 2.8 A resolution
purified recombinant mutant R470E/T499R, hanging drop vapour diffusion method, 4°C, 0.001 ml of 10 mg/ml protein is mixed with 0.001 ml of well solution containing 100 mM sodium cacodylate, pH 6.5, 100 mM magnesium acetate, 2 mM 2-mercaptoethanol, and 12-14% w/v polyethylene glycol 6000, cryoprotection by 25% glycerol, X-ray diffraction structure determination and analysis at 2.2 A resolution
-
recombinant enzyme from Escherichia coli, hanging-drop vapor-diffusion method
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E475A
site-directed mutagenesis, mutation of the catalytic glutamate residue, a catalytically compromised enzyme mutant that sediments more rapidly in the presence of saturating amounts of the dynorphin A(1-8) substrate compared to the wild-type enzyme
H160A
site-directed mutagenesis, mutation of a surface histidine involved in a divalent cation-mediated lattice contact in the original neurolysin crystals
G608A
-
site-directed mutagenesis, the mutation does not affect the overall fold of the protein, the mutant shows altered substrate specificity and kinetics with fluorogenic peptide substrates compared to the wild-type enzyme
R470E/T499R
-
site-directed mutagenesis of the substrate recognition residues leads to a swap of substrate specificity from thimet oligopeptidase to neurolysin, EC 3.4.24.16, the mutant cleaves neurolysin sites, overview
Y606A
-
site-directed mutagenesis, the mutation does not affect the overall fold of the protein, the mutant shows altered substrate specificity and kinetics with fluorogenic peptide substrates compared to the wild-type enzyme
Y606F
Y610L
-
marked change in substrate specificity with 3fold higher binding efficiency to matrix metalloproteinase MMP-2/9 substrate (7-methoxy-coumarin-4-yl)acetyl-RPKPYA-Nva-WMK(2,4-dinitrophenyl)-NH2 with glutamic acid at the P2' amino acid position
Y606F
-
site-directed mutagenesis, the mutation does not affect the overall fold of the protein, the mutant shows altered substrate specificity and kinetics with fluorogenic peptide substrates compared to the wild-type enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
up to two cycles of freezing and thawing of the purified rNln do not significantly affect the purified recombinant enzyme's specific activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
a gradual decrease of the specific activity is observed in preparations kept longer than 6 months at -80°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography, ultrafiltration, and gel filtration to homogeneity, large scale production of rNln
recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli strain DH5alpha by glutathione affinity chromatography to homogeneity
-
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli
expression of GST-tagged wild-type and mutant enzymes in Escherichia coli strain DH5alpha
-
expression of neurolysin gene fron brain ligated to the C-terminal half of the alpha-agglutinin gene with a FLAG tag sequence in Saccharomyces cerevisiae at the cell surface, construction of a molecular displaying plasmid
-
expression of the FLAG-tagged brain enzyme in Saccharomyces cerevisiae strain BJ2168 on the cell surface, subcloning in Escherichia coli strain DH5alpha
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
overexpressed in human kidney cells, HK293 cells. The transfectants exhibit a membrane-associated form of endopeptidase-24.16, the catalytic site of which clearly faces the extracellular domain. Transfected cells are unable to secrete the enzyme
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
-
neurolysin can be used as a molecular tool for analysis of properties of cancer-producing matrix metalloproteinases MMP-2 and MMP-9, quantitative determination of cleavage activity of neurolysin toward MMPspecific fluorescence-quenching peptides, overview
additional information
additional information
-
agaricoglycerides are devoid of activity in a large number of biochemical and cellular assays, emphasizing their selectivity towards neurolysin
additional information
-
EP12.16 modulates intracellular, peptidergic signaling cascades through the type-2 BK receptor in physiologically relevant nociceptive system
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dahms, P.; Mentlein, R.
Purification of the main somatostatin-degrading proteases from rat and pig brains, their action on other neuropeptides, and their identification as endopeptidases 24.15 and 24.16
Eur. J. Biochem.
208
145-154
1992
Rattus norvegicus, Sus scrofa
Barrett, A.J.; Brown, M.A.; Dando, P.M.; Knight, C.G.; McKie, N.; Rawlings, N.D.; Serizawa, A.
Thimet oligopeptidase and oligopeptidase M or neurolysin
Methods Enzymol.
248
529-556
1995
Rattus norvegicus
Checler, F.; Vincent, J.P.; Kitabgi, P.
Purification and characterization of a novel neurotensin-degrading peptidase from rat brain synaptic membranes
J. Biol. Chem.
261
11274-11281
1986
Rattus norvegicus
Checler, F.; Barelli, H.; Vincent, J.P.
Tissue distribution of a novel neurotensin-degrading metallopeptidase. An immunological approach using monospecific polyclonal antibodies
Biochem. J.
257
549-554
1989
Rattus norvegicus
Barelli, H.; Vincent, J.P.; Checler, F.
Peripheral inactivation of neurotensin. Isolation and characterization of a metallopeptidase from rat ileum
Eur. J. Biochem.
175
481-489
1988
Rattus norvegicus
Rodd, D.; Hersh, L.B.
Endopeptidase 24.16B. A new variant of endopeptidase 24.16
J. Biol. Chem.
270
10056-10061
1995
Rattus norvegicus
Dauch, P.; Vincent, J.P.; Checler, F.
Specific inhibition of endopeptidase 24.16 by dipeptides
Eur. J. Biochem.
202
269-276
1991
Rattus norvegicus
Checler, F.; Barelli, H.; Dauch, P.; Vincent, B.; Dive, V.; Beaudet, A.; Daniel, E.E.; Fox-Threlkeld, J.E.T.; Masuo, Y.; Vincent, J.P.
Recent advances on endopeptidase-3.4.24.16
Biochem. Soc. Trans.
21
692-697
1993
Rattus norvegicus
Mentlein, R.; Dahms, P.
Endopeptidases 24.16 and 24.15 are responsible for the degradation of somatostatin, neurotensin, and other neuropeptides by cultivated rat cortical astrocytes
J. Neurochem.
62
27-36
1994
Rattus norvegicus
Vincent, B.; Dauch, P.; Vincent J.P.; Checler, F.
Stably transfected human cells overexpressing rat brain endopeptidase 3.4.24.16: biochemical characterization of the activity and expression of soluble and membrane-associated counterparts
J. Neurochem.
68
837-845
1997
Rattus norvegicus
Serizawa, A.; Dando, P.M.; Barrett, A.J.
Characterization of a mitochondrial metallopeptidase reveals neurolysin as a homologue of thimet oligopeptidase
J. Biol. Chem.
276
2092-2098
1995
Rattus norvegicus
Dauch, P.; Vincent, J.P.; Checler, F.
Molecular cloning and expression of rat brain endopeptidase 3.4.24.16
J. Biol. Chem.
270
27266-27271
1995
Rattus norvegicus
Barelli, H.; Vincent, J.P.; Checler, F.
Rat kidney endopeptidase 24.16. Purification, physico-chemical characteristics and differential specificity towards opiates, tachykinins and neurotensin-related peptides
Eur. J. Biochem.
211
79-90
1993
Rattus norvegicus
Lian, W.; Chen, G.; Wu, D.; Brown, C.K.; Madauss, K.; Hersh, L.B.; Rodgers, D.W.
Crystallization and preliminary analysis of neurolysin
Acta Crystallogr. Sect. D
56
1644-1646
2000
Rattus norvegicus
-
Rioli, V.; Gozzo, F.C.; Heimann, A.S.; Linardi, A.; Krieger, J.E.; Shida, C.S.; Almeida, P.C.; Hyslop, S.; Eberlin, M.N.; Ferro, E.S.
Novel natural peptide substrates for endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme
J. Biol. Chem.
278
8547-8555
2003
Rattus norvegicus
Barrett, A.J.; Dando, P.M.
Neurolysin
Handbook of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press
1
356-360
2004
Oryctolagus cuniculus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
-
Stadler, M.; Hellwig, V.; Mayer-Bartschmid, A.; Denzer, D.; Wiese, B.; Burkhardt, N.
Novel analgesic triglycerides from cultures of Agaricus macrosporus and other basidiomycetes as selective inhibitors of neurolysin
J. Antibiot.
58
775-786
2005
Rattus norvegicus
Jeske, N.A.; Berg, K.A.; Cousins, J.C.; Ferro, E.S.; Clarke, W.P.; Glucksman, M.J.; Roberts, J.L.
Modulation of bradykinin signaling by EP24.15 and EP24.16 in cultured trigeminal ganglia
J. Neurochem.
97
13-21
2006
Rattus norvegicus
Kadonosono, T.; Kato, M.; Ueda, M.
Metallopeptidase, neurolysin, as a novel molecular tool for analysis of properties of cancer-producing matrix metalloproteinases-2 and -9
Appl. Microbiol. Biotechnol.
75
1285-1291
2007
Rattus norvegicus
Kadonosono, T.; Kato, M.; Ueda, M.
Substrate specificity of rat brain neurolysin disclosed by molecular display system and putative substrates in rat tissues
Appl. Microbiol. Biotechnol.
75
1353-1360
2007
Rattus norvegicus
Machado, M.F.; Rioli, V.; Dalio, F.M.; Castro, L.M.; Juliano, M.A.; Tersariol, I.L.; Ferro, E.S.; Juliano, L.; Oliveira, V.
The role of Tyr605 and Ala607 of thimet oligopeptidase and Tyr606 and Gly608 of neurolysin in substrate hydrolysis and inhibitor binding
Biochem. J.
404
279-288
2007
Rattus norvegicus
Bertazolli-Filho, R.; Coca-Prados, M.; Haddad, A.; Laicine, E.M.
Molecular analysis of neurolysin expression in the rat and bovine ciliary body
Curr. Eye Res.
32
751-756
2007
Bos taurus, Rattus norvegicus
Lim, E.J.; Sampath, S.; Coll-Rodriguez, J.; Schmidt, J.; Ray, K.; Rodgers, D.W.
Swapping the substrate specificities of the neuropeptidases neurolysin and thimet oligopeptidase
J. Biol. Chem.
282
9722-9732
2007
Rattus norvegicus
Kadonosono, T.; Kato-Murai, M.; Ueda, M.
Alteration of substrate specificity of rat neurolysin from matrix metalloproteinase-2/9-type to -3-type specificity by comprehensive mutation
Protein Eng. Des. Sel.
21
507-513
2008
Rattus norvegicus
Lorenzon, R.Z.; Cunha, C.E.; Marcondes, M.F.; Machado, M.F.; Juliano, M.A.; Oliveira, V.; Travassos, L.R.; Paschoalin, T.; Carmona, A.K.
Kinetic characterization of the Escherichia coli oligopeptidase A (OpdA) and the role of the Tyr(607) residue
Arch. Biochem. Biophys.
500
131-136
2010
Rattus norvegicus
Swindle, J.D.; Santos, K.L.; Speth, R.C.
Pharmacological characterization of a novel non-AT1, non-AT2 angiotensin binding site identified as neurolysin
Endocrine
44
525-531
2013
Rattus norvegicus (P42676), Rattus norvegicus Sprague-Dawley (P42676)
Hines, C.S.; Ray, K.; Schmidt, J.J.; Xiong, F.; Feenstra, R.W.; Pras-Raves, M.; de Moes, J.P.; Lange, J.H.; Melikishvili, M.; Fried, M.G.; Mortenson, P.; Charlton, M.; Patel, Y.; Courtney, S.M.; Kruse, C.G.; Rodgers, D.W.
Allosteric inhibition of the neuropeptidase neurolysin
J. Biol. Chem.
289
35605-35619
2014
Rattus norvegicus (P42676)
Wangler, N.J.; Jayaraman, S.; Zhu, R.; Mechref, Y.; Abbruscato, T.J.; Bickel, U.; Karamyan, V.T.
Preparation and preliminary characterization of recombinant neurolysin for in vivo studies
J. Biotechnol.
234
105-115
2016
Rattus norvegicus (P42676)
EXTERNAL LINKS (specific for EC-Number 3.4.24.16)
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