3.4.24.16: neurolysin
This is an abbreviated version!
For detailed information about neurolysin, go to the full flat file.
Word Map on EC 3.4.24.16
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3.4.24.16
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bradykinin
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metallopeptidase
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metalloendopeptidase
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dynorphins
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pro-ile
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neuropeptidase
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pro10-tyr11
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neuromedin
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hemopressins
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arg8-arg9
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non-at2
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neurotensin-degrading
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molecular biology
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pharmacology
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medicine
- 3.4.24.16
- bradykinin
- metallopeptidase
- metalloendopeptidase
- dynorphins
- pro-ile
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neuropeptidase
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pro10-tyr11
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neuromedin
- hemopressins
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arg8-arg9
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non-at2
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neurotensin-degrading
- molecular biology
- pharmacology
- medicine
Reaction
Preferential cleavage in neurotensin: Pro10-/-Tyr =
Synonyms
endopeptidase 24.16, endopeptidase 24.16B, endopeptidase 3.4.24.16, EP 24.16, ep24.16, EP24.16c, EP24.16m, MEP, Microsomal endopeptidase, mitochondrial peptidase, MOP, More, NEL, neurolisin, neurolysin, neurotensin endopeptidase, neurotensin-cleaving enzyme, Nln, oligopeptidase M, peptidase, neurotensin endo, peptidase, neurotensin endo-, SABP, soluble angiotensin II-binding protein, Soluble angiotensin-binding protein, thimet oligopeptidase II, thimet peptidase II
ECTree
3.4.24.16 neurolysinAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 3.4.24.16 - neurolysin
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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
agaricoglyceride A
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main active principle of the crude extract of Agaricus macrosporus shows strong activity against neurolysin
agaricoglyceride B
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agaricoglyceride C, agaricoglyceride D, known cometabolites agaricic ester show no activity against neurolysin up to 0.01 mM
dynorphin A1-13
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inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
dynorphin(1-8)
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degradation of 3-carboxy-7-methoxycoumaryl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
dynorphin(1-9)
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degradation of 3-carboxy-7-methoxycoumaryl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
HONHCO-CH2-CH(CH2-C6H5)CO-Ile-Ala
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potent and selective inhibitor of neurolysin
kinetensin
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degradation of 3-carboxy-7-methoxycoumaryl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
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LVVYPWTQRY
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inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
molecular inhibitors of Gbetagama-dimer function
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strain-dependent increases in EP24.16 activity are substantially attenuated by betaARK.ct by 86.4%
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molecular inhibitors of Gialpha-subunit function
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force-dependent increase in cellular EP24.16 activity is strongly attenuated by Gialpha1-G202T by 69.6% and Gialpha2-G203T by 101.7%, whereas Gialpha2-G202T has no significant effect
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N-(1(R,S)-carboxy-3-phenylpropyl)-Ala-Ala-Tyr-p-aminobenzoate
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inhibits EP24.16 resulting in a 1000fold increase in type-2 BK receptor sensitivity to bradykinin as measured by inositol phosphate accumulation
NF023
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attenuates the strain-dependent elevation of endopeptidase activity by 82.2%
Pro-Phe-PSI(PO2CH2)Leu-Pro-NH2
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potent and selective inhibitor of neurolysin
Pro-Xaa dipeptides
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most potent inhibitors, Xaa-Pro dipeptides are ineffective
PTX
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completely attenuates the cyclic strain-dependent increase in endopeptidase activity
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PVNFKFLSH
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inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
VVYPWTQRY
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inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
acetyl-neurotensin(8-13)
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inhibits degradation of 3-carboxy-7-methoxycoumaryl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
angiotensin I
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inhibits degradation of 3-carboxy-7-methoxycoumaryl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
angiotensin I
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inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
angiotensin II
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degradation of 3-carboxy-7-methoxycoumaryl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
angiotensin II
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inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
bradykinin
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degradation of 3-carboxy-7-methoxycoumaryl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
bradykinin
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inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)
JA-2
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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
Mcc-Pro-Leu
Nln-mediated hydrolysis of Mcc-Pro-Leu-Gly-Pro-D-Lys-Dnp yields a degradation product that triggers product inhibition
Mcc-Pro-Leu
Nln-mediated hydrolysis of QFS yields a degradation product that triggers a relatively product inhibition
Mcc-Pro-Leu
Nln-mediated hydrolysis of Mcc-Pro-Leu-Gly-Pro-D-Lys-Dnp yields a degradation product that triggers a product inhibition
Mcc-Pro-Leu
Nln-mediated hydrolysis of QFS yields a degradation product that triggers a relatively product inhibition
Mcc-Pro-Leu
Nln-mediated hydrolysis of Mcc-Pro-Leu-Gly-Pro-D-Lys-Dnp yields a degradation product that triggers a relatively product inhibition
Neuromedin N
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degradation of 3-carboxy-7-methoxycoumaryl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
neurotensin
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inhibits degradation of 3-carboxy-7-methoxycoumaryl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
neurotensin(9-13)
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the shortest neurotensin partial sequence that is able to fully inhibit neurotensin degradation
Pro-Ile
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selective inhibitor of neurolysin, inhibition by milimolar concentrations
Pro-Ile
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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
Substance P
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degradation of 3-carboxy-7-methoxycoumaryl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
Xenopsin
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degradation of 3-carboxy-7-methoxycoumaryl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
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
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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
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additional information
additional information
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putative intracellular peptides as competetive inhibitors of (o-aminobenzoyl)-GFSHFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) hydrolysis by EP24.16
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additional information
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inhibitor of neurolysin potentiates the neurotensin-induced anti-nociception
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additional information
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no inhibition by bestatin, captopril, leupeptin, and E64, poor inhibition by PMSF and Z-Pro-prolinal
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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
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additional information
inhibitor synthesis and evaluation, different kinetic inhibition models, binding structures, modeling, overview
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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
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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
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