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
-
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
- 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
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
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Reference
Reference on EC 3.4.24.16 - neurolysin
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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
Rioli, V.; Kato, A.; Portaro, F.C.V.; Cury, G.K.; te Kaat, K.; Vincent, B.; Checler, F.; Camargo, A.C.M.; Glucksman, M.J.; Roberts, J.L.; Hirose, S.; Ferro, E.S.
Neuropeptide specificity and inhibition of recombinant isoforms of the endopeptidase 3.4.24.16 family: comparison with the related recombinant endopeptidase 3.4.24.15
Biochem. Biophys. Res. Commun.
250
5-11
1998
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
Yoshikawa, S.; Tashiro, T.; Takahashi, K.
Specificity of action on neuropeptides of an endopeptidase from the synaptosomal membranes of guinea pig brain
J. Biochem.
104
1007-1010
1988
Cavia porcellus
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
Vincent, B.; Vincent, J.P.; Checler, F.
Purification and characterization of human endopeptidase 3.4.24.16. Comparison with the porcine counterpart indicates a unique cleavage site on neurotensin
Brain Res.
709
51-58
1996
Homo sapiens, Sus scrofa
Vincent, B.; Beaudet, A.; Dauch, P.; Vincent, J.P.; Checler, F.
Distinct properties of neuronal and astrocytic endopeptidase 3.4.24.16: a study on differentiation, subcellular distribution, and secretion processes
J. Neurosci.
16
5049-5059
1996
Mus musculus
Krause, D.R.; Piva, T.J.; Brown, S.B.; Ellem, K.A.O.
Characterization and localization of mitochondrial oligopeptidase (MOP) (EC 3.4.24.16) activity in the human cervical adenocarcinoma cell line HeLa
J. Cell. Biochem.
66
297-308
1997
Homo sapiens
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
Barelli, H.; Fox-Threlkeld, J.E.T.; Dive, V.; Daniel, E.E.; Vincent, J.P.; Checler, F.
Role of endopeptidase 3.4.24.16 in the catabolism of neurotensin, in vivo, in the vascularly perfused dog ileum
Br. J. Pharmacol.
112
127-132
1994
Canis lupus familiaris
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
Millican, P.E.; Kenny, A.J.; Turner, A.J.
Purification and properties of a neurotensin-degrading endopeptidase from pig brain
Biochem. J.
276
583-591
1991
Sus scrofa
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
-
Oliveira, V.; Campos, M.; Hemerly, J.P.; Ferro, E.S.; Camargo, A.C.; Juliano, M.A.; Juliano, L.
Selective neurotensin-derived internally quenched fluorogenic substrates for neurolysin (EC 3.4.24.16): comparison with thimet oligopeptidase (EC 3.4.24.15) and neprilysin (EC 3.4.24.11)
Anal. Biochem.
292
257-265
2001
Sus scrofa
Oliveira, V.; Campos, M.; Melo, R.L.; Ferro, E.S.; Camargo, A.C.; Juliano, M.A.; Juliano, L.
Substrate specificity characterization of recombinant metallo oligo-peptidases thimet oligopeptidase and neurolysin
Biochemistry
40
4417-4425
2001
Sus scrofa
Oliveira, V.; Gatti, R.; Rioli, V.; Ferro, E.S.; Spisni, A.; Camargo, A.C.; Juliano, M.A.; Juliano, L.
Temperature and salts effects on the peptidase activities of the recombinant metallooligopeptidases neurolysin and thimet oligopeptidase
Eur. J. Biochem.
269
4326-4334
2002
Sus scrofa
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
Cotter, E.J.; von Offenberg Sweeney, N.; Coen, P.M.; Birney, Y.A.; Glucksman, M.J.; Cahill, P.A.; Cummins, P.M.
Regulation of endopeptidases EC3.4.24.15 and EC3.4.24.16 in vascular endothelial cells by cyclic strain: role of Gi protein signaling
Arterioscler. Thromb. Vasc. Biol.
24
457-463
2004
Bos taurus
Machado, M.F.; Cunha, F.M.; Berti, D.A.; Heimann, A.S.; Klitzke, C.F.; Rioli, V.; Oliveira, V.; Ferro, E.S.
Substrate phosphorylation affects degradation and interaction to endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme
Biochem. Biophys. Res. Commun.
339
520-525
2006
More
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
Homo sapiens, Mus musculus, Oryctolagus cuniculus, 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
Paschoalin, T.; Carmona, A.K.; Rodrigues, E.G.; Oliveira, V.; Monteiro, H.P.; Juliano, M.A.; Juliano, L.; Travassos, L.R.
Characterization of thimet oligopeptidase and neurolysin activities in B16F10-Nex2 tumor cells and their involvement in angiogenesis and tumor growth
Mol. Cancer
6
44
2007
Mus musculus, Mus musculus C57BL/6
Kitabgi, P.
Inactivation of neurotensin and neuromedin N by Zn metallopeptidases
Peptides
27
2515-2522
2006
Canis lupus familiaris, Homo sapiens, Mus musculus
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
Wangler, N.J.; Santos, K.L.; Schadock, I.; Hagen, F.K.; Escher, E.; Bader, M.; Speth, R.C.; Karamyan, V.T.
Identification of membrane-bound variant of metalloendopeptidase neurolysin (EC 3.4.24.16) as the non-angiotensin type 1 (non-AT1), non-AT2 angiotensin binding site
J. Biol. Chem.
287
114-122
2012
Mus musculus
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)
Rashid, M.; Wangler, N.J.; Yang, L.; Shah, K.; Arumugam, T.V.; Abbruscato, T.J.; Karamyan, V.T.
Functional up-regulation of endopeptidase neurolysin during post-acute and early recovery phases of experimental stroke in mouse brain
J. Neurochem.
129
179-189
2014
Mus musculus
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)
Teixeira, P.F.; Masuyer, G.; Pinho, C.M.; Branca, R.M.M.; Kmiec, B.; Wallin, C.; Waermlaender, S.K.T.S.; Berntsson, R.P.; Ankarcrona, M.; Graeslund, A.; Lehtioe, J.; Stenmark, P.; Glaser, E.
Mechanism of peptide binding and cleavage by the human mitochondrial peptidase neurolysin
J. Mol. Biol.
430
348-362
2018
Homo sapiens (Q9BYT8), Homo sapiens
Karamyan, V.T.
Peptidase neurolysin is an endogenous cerebroprotective mechanism in acute neurodegenerative disorders
Med. Hypotheses
131
109309
2019
Mus musculus (Q91YP2)
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