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Information on EC 3.4.24.16 - neurolysin
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EC Tree
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 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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
endopeptidase 24.16
endopeptidase 24.16B
-
-
-
-
endopeptidase 3.4.24.16
EP 24.16
ep24.16
MEP
-
-
-
-
Microsomal endopeptidase
MOP
-
-
-
-
neurotensin endopeptidase
-
-
-
-
neurotensin-cleaving enzyme
Nln
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
ep24.16
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
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Preferential cleavage in neurotensin: Pro10-/-Tyr
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
endopeptidase
-
hydrolysis of peptide bond
-
-
peptides, endopeptidase
-
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CAS REGISTRY NUMBER
COMMENTARY
149371-24-4
-
90463-53-9
-
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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
(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
-
-
?
(o-aminobenzoyl)-AFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-AFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-AF + SPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-AKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-AKPR + RPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
-
?
(o-aminobenzoyl)-DFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-DFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-DF + SPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-EFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-EFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-EF + SPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-ENKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-ENKPR + RPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-ENKPRRPYILQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-ENKPRRP + YILQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-KPRRPY + ILQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
36% cleavage at P-Y bond, 64% cleavage at Y-I bond
-
?
(o-aminobenzoyl)-ENKPRRPYIQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-ENKPRRP + YIQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-KPRRPY + IQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
79% cleavage at P-Y bond, 21% cleavage at Y-I bond
-
?
(o-aminobenzoyl)-ENKPRRPYQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-ENKPRRP + YQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-KPRRPY + Q-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-ENKPR + RPYQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
16% cleavage at P-Y bond, 40% cleavage at Y-Q bond, 44% cleavage at R-R
-
?
(o-aminobenzoyl)-FFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-FFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-FF + SPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GASPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GASP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GDSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GDSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GESPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GESP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFAPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFAP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFDPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFDP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFEPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFEP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFFPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFFP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFHPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFHP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFIPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFIP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFLPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFLP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFNPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFNP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFPPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFPP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFQPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFQP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFRPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFRP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSAFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSA + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSDFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSH + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSEFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSE + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSFFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSF + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSHFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSH + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSIFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSI + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSLFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSL + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSNFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSN + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPARQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + ARQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPDRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + DRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GF + SPDRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPERQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + ERQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GF + SPERQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFAQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FAQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GF + SPFAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFDQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FDQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFEQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FEQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GF + SPFEQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFFQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FFQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GF + SPFFQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFHQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FHQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GF + SPFHQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFIQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FIQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFLQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FLQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFNQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FNQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GF + SPFNQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFQQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FQQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GF + SPFQQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFR-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GF + SPFR-(N-(2,4-dinitrophenyl)ethylenediamine)
-
6% of the activity with (o-aminobenzoyl)-GFSPFRSSRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
?
(o-aminobenzoyl)-GFSPFRA-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRA-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFRE-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRE-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFRF-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRF-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFRI-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRI-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFRL-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRL-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFRN-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRN-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFRP-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRP-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
(o-aminobenzoyl)-GFSPFRR-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRR-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFRS-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRS-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFRSSRIGEIKEEQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSPFRS + SRIGEIKEEQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
10% of the activity with (o-aminobenzoyl)-GFSPFRSSRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
?
(o-aminobenzoyl)-GFSPFRSSRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSPFRS + SRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFSQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FSQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GF + SPFSQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPHRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + HRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPIRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + IRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GF + SPIRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPLRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + LRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GF + SPLRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPNRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + NRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPPRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + PRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPQRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + QRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPRRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + RRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPSRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + SRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSRFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSSFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSS + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSXFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSQ + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GGFLPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLPR + RPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GGFLRRAQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GGFLRRDQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RDQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GGFLRREQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + REQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GGFLRRFQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RFQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GGFLRR + FQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
cleavage at the R-R or at the R-X bond
-
?
(o-aminobenzoyl)-GGFLRRHQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RHQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GGFLRR + HQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
cleavage at the R-R or at the R-X bond
-
?
(o-aminobenzoyl)-GGFLRRIQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RIQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GGFLRR + IQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
cleavage at the R-R or at the R-X bond
-
?
(o-aminobenzoyl)-GGFLRRLQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RLQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GGFLRR + LQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
cleavage at the R-R or at the R-X bond
-
?
(o-aminobenzoyl)-GGFLRRNQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RNQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GGFLRR + NQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
cleavage at the R-R or at the R-X bond
-
?
(o-aminobenzoyl)-GGFLRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GGFLRRRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GGFLRRV-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RV-(N-(2,4-dinitrophenyl)ethylenediamine)
-
cleavage at the R-R or at the R-X bond
-
?
(o-aminobenzoyl)-GGFLRRVQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RVQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GGFLRRYQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GGFLR + RYQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-GGFLRR + YQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
cleavage at the R-R or at the R-X bond
-
?
(o-aminobenzoyl)-GHSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GHSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GISPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GISP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GLSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GLSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GNSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GNSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GPSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GPSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GQSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GQSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GRSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GRSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GSSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GSSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-HFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-HFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-IFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-IFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-IF + SPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-KPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-KPR + RPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-KPRRPYILQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-KPRRP + YILQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-KPRRPY + ILQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
37% cleavage at P-Y bond, 63% cleavage at Y-I bond
-
?
(o-aminobenzoyl)-LFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-LFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-LF + SPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-LYENKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-LYENKPR + RPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-LYENKPRRPYILQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-LYENKPRRP + YILQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-LYENKPRRPY + ILQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
65% cleavage at P-Y bond, 35% cleavage at Y-I bond
-
?
(o-aminobenzoyl)-NAPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-NAPR + RPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
-
?
(o-aminobenzoyl)-NFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-NFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-NF + SPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-NKARRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-NKAR + RPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
-
?
(o-aminobenzoyl)-NKPRRAQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-NKPR + RAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
-
?
(o-aminobenzoyl)-NKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-NKPR + RPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-QFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-QFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-QF + SPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-RFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-RFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-RF + SPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-RPPGFSPFR-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-RPPGF + SPFR-(N-(2,4-dinitrophenyl)ethylenediamine)
-
7% of the activity with (o-aminobenzoyl)-GFSPFRSSRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
?
(o-aminobenzoyl)-RPPGFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-RPPGFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
23% of the activity with (o-aminobenzoyl)-GFSPFRSSRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
?
(o-aminobenzoyl)-RPPGFSPFRSSRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-RPPGFSPFRS + SRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
38% of the activity with (o-aminobenzoyl)-GFSPFRSSRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
?
(o-aminobenzoyl)-SFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-SFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (o-aminobenzoyl)-SF + SPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
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-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-Lys-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl) + H2O
?
-
-
-
?
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
benzoyl-Gly-Ala-Ala-Phe-4-aminobenzoate + H2O
benzoyl-Gly + Ala-Ala-Phe-4-aminobenzoate
-
-
-
?
FSTSAQNN + H2O
?
octMdh1, Oct1 generated octapeptide from Mus musculus
-
-
?
Lys-Ile-Pro-Tyr-Ile-Leu + H2O
Lys-Ile-Pro + Tyr-Ile-Leu
-
i.e. neuromedin
-
?
MFLTRFVGRRFLAAASARS + H2O
MFLTR + FVG + RRFL + 2 L-Ala + ASA + RS
pL29, presequence from Arabidopsis thaliana
-
-
?
MFRRPVLQVLRQFVRH + H2O
MFR + RPVL + QVLR + QFVRH
pSSBP, human presequence
-
-
?
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr + H2O
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg + Arg-Pro-Tyr
-
i.e. neurotensin(1-11)
-
?
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
t-butyloxycarbonyl-Phe-Ala-Ala-Phe-4-aminobenzoate + H2O
t-butyloxycarbonyl-Phe + Ala-Ala-Phe-4-aminobenzoate
-
-
-
?
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-Arg + H2O
peptide fragments
-
i.e. dynorphin(1-9)
-
-
?
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
Tyr-Gly-Gly-Phe-Leu-Arg-Lys-Tyr-Pro + H2O
Tyr-Gly-Gly-Phe-Leu + Arg-Lys-Tyr-Pro + Tyr-Gly-Gly-Phe-Leu-Arg + Lys-Tyr-Pro
-
i.e. beta-neoendorphin, cleavage sites: Leu5-Arg6, Arg6-Lys7
-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Lys-Tyr-Pro-Lys + H2O
Tyr-Gly-Gly-Phe-Leu-Arg-Lys + Tyr-Pro-Lys
-
i.e. alpha-neoendorphin
-
?
Tyr-Gly-Gly-Phe-Met-Arg-Arg-Val-(NH2) + H2O
Tyr-Gly-Gly-Phe-Met + Arg-Arg-Val-(NH2)
-
i.e. metorphinamide
-
?
Tyr-Gly-Gly-Phe-Met-Arg-Arg-Val-Gly-Arg-Pro-Glu + H2O
Tyr-Gly-Gly-Phe + Met-Arg-Arg-Val-Gly + Arg-Pro-Glu + Tyr-Gly-Gly-Phe-Met-Arg + -Arg-Val-Gly
-
i.e. BAM-12P, cleavage sites: Phe4-Met5, Arg6-Arg7, Gly9-Arg10
-
?
Tyr-Pro-Phe-Pro-Gly-Pro-Ile + H2O
Tyr-Pro-Phe-Pro + Gly-Pro-Ile
-
i.e. beta-casomorphin, cleavage site: Pro4-Gly5
-
?
[(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
-
-
?
(o-aminobenzoyl)-GFSHFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSH + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
(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
-
?
(o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
20% of the activity with (o-aminobenzoyl)-GFSPFRSSRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
?
acetyl-Arg-Arg-Pro-Tyr-Ile-Leu + H2O
acetyl-Arg-Arg-Pro + Tyr-Ile-Leu
-
i.e. acetyneurotensin(8-13)
-
?
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
?
-
no cleavage
-
-
?
Ala-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-Thr-Phe-Thr-Ser-Cys + H2O
?
-
i.e. somatostatin, cleavage sites: Phe6-Phe7, Thr10-Phe11
-
-
?
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-Arg-Pro-Tyr-Ile-Leu + H2O
Arg-Arg-Pro + Tyr-Ile-Leu
-
i.e. neurotensin(8-13)
-
?
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
-
i.e. substance P, cleavage sites: Pro4-Gln5, Gln5-Gln6, Gln6-Phe7
-
?
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
-
-
?
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
-
-
?
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: Pro4-Gly5, Glyn5-Glyn6, and Phe8-Gly9
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe + Ser-Pro-Phe-Arg
-
i.e. bradykinin, cleavage site: Phe5-Ser6
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe + Ser-Pro-Phe-Arg
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe + Ser-Pro-Phe-Arg
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe + Ser-Pro-Phe-Arg
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe + Ser-Pro-Phe-Arg
-
i.e. bradykinin, cleavage site: Phe5-Ser6
-
?
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 + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
i.e. angiotensin II
-
?
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
-
i.e. angiotensin I, cleavage site: Pro7-Phe8
-
?
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + H2O
Asp-Arg-Val-Tyr-Ile-His-Pro + Phe-His-Leu
-
-
-
-
?
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + H2O
Asp-Arg-Val-Tyr-Ile-His-Pro + Phe-His-Leu
-
-
-
-
?
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + H2O
Asp-Arg-Val-Tyr-Ile-His-Pro + Phe-His-Leu
-
-
-
-
?
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + H2O
Asp-Arg-Val-Tyr-Ile-His-Pro + Phe-His-Leu
-
i.e. angiotensin I, cleavage site: Pro7-Phe8
-
?
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + H2O
Asp-Arg-Val-Tyr-Ile-His-Pro + Phe-His-Leu
-
i.e. angiotensin I, cleavage site: Pro7-Phe8
-
?
GlpLYENKPRRPYIL + H2O
GlpLYENKPRRP + YIL
neurotensin, secreted human neuropeptide
-
-
?
GlpLYENKPRRPYIL + H2O
GlpLYENKPRRP + YIL
neurotensin, secreted human neuropeptide, Nln cleaves the Pro10-Tyr11 bond, but not the Arg8-Arg9 bond
-
-
?
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
-
-
?
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
-
-
?
neurotensin + H2O
GlpLYENKPRRP + YIL
secreted neuropeptide, Nln cleaves the Pro10-Tyr11 bond, but not the Arg8-Arg9 bond
-
-
?
neurotensin + H2O
GlpLYENKPRRP + YIL
secreted neuropeptide, Nln cleaves the Pro10-Tyr11 bond, but not the Arg8-Arg9 bond
-
-
?
neurotensin + H2O
GlpLYENKPRRP + YIL
secreted neuropeptide, Nln cleaves the Pro10-Tyr11 bond, but not the Arg8-Arg9 bond
-
-
?
neurotensin + H2O
GlpLYENKPRRP + YIL
secreted neuropeptide, Nln cleaves the Pro10-Tyr11 bond, but not the Arg8-Arg9 bond
-
-
?
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
-
?
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
-
specific hydrolysis of the Pro10-Tyr11 bond
-
?
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
-
specific hydrolysis of the Pro10-Tyr11 bond
-
?
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
-
specific hydrolysis of the Pro10-Tyr11 bond
-
?
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
-
?
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
-
specific hydrolysis of the Pro10-Tyr11 bond
-
?
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
-
specific hydrolysis of the Pro10-Tyr11 bond
-
?
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
-
cleavage sites: Arg8-Arg9 and Pro10-Tyr11
-
-
?
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 + H2O
Tyr-Gly-Gly-Phe-Leu + Arg-Arg-Ile
-
-
-
-
?
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 + H2O
Tyr-Gly-Gly-Phe-Leu + Arg-Arg-Ile
-
i.e. dynorphin(1-8)
-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln + H2O
peptide fragments
-
-
-
-
?
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
-
-
?
(o-aminobenzoyl)-GFSHFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSH + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
additional information
-
-
-
-
?
additional information
?
-
-
the enzyme is involved in the inactivation of numerous neuropeptides
-
-
?
additional information
?
-
Mcc-Pro-Leu-Gly-Pro-D-Lys-Dnp and neurotensin compete for their hydrolysis by enzyme Nln
-
-
?
additional information
?
-
-
the enzyme contributes to the catabolism of neurotensin in the dog intestine
-
-
?
additional information
?
-
-
the enzyme is active in inactivation of neuropeptides, biological relevance, overview
-
-
?
additional information
?
-
-
marked specificity towards Pro-X bonds present in the interior parts of various neuropeptides and related peptides. No cleavage is observed at the first and second peptide bonds from the NH2-terimini or from the COOH-terminal extension of the peptides examined, suggesting that the enzyme requires both NH2- and COOH-terminal extensions of at least 3 residues from the scissile bond for its action. Not strictly specific for Pro-X bonds
-
-
?
additional information
?
-
-
possible implication of the enzyme in the specific degradation of neurotensin and other peptide neurotransmitters in the synaptic cleft
-
-
?
additional information
?
-
-
the enzyme is active in inactivation of neuropeptides, biological relevance, overview
-
-
?
additional information
?
-
QFS and neurotensin compete for their hydrolysis by enzyme Nln
-
-
?
additional information
?
-
the structure of mitochondrial peptidase neurolysin mutant hNLNE475Q in complex with the products of neurotensin cleavage reveals a closed conformation with an internal cavity that restricts substrate length and highlights the mechanism of enzyme opening/closing that is necessary for substrate binding and catalytic activity. hNLN cooperates with presequence protease (PreP or PITRM1) in the degradation of long targeting peptides and amyloid-beta peptide, Abeta1-40, associated with Alzheimer disease, particularly cleaving the hydrophobic fragment Abeta35-40. No cleavage of amyloid-beta1-40, pACD1 (presequence from Arabidopsis thaliana), SytII 40-60 (non-presequence of synaptotagmin from Rattus norvegicus), pCox4 (presequence from Saccharomyces cerevisiae), pOTC (human presequence), and pF1beta (presequence from NIcotiana plumbaginifolia), mass spectrometric analysis
-
-
?
additional information
?
-
-
the structure of mitochondrial peptidase neurolysin mutant hNLNE475Q in complex with the products of neurotensin cleavage reveals a closed conformation with an internal cavity that restricts substrate length and highlights the mechanism of enzyme opening/closing that is necessary for substrate binding and catalytic activity. hNLN cooperates with presequence protease (PreP or PITRM1) in the degradation of long targeting peptides and amyloid-beta peptide, Abeta1-40, associated with Alzheimer disease, particularly cleaving the hydrophobic fragment Abeta35-40. No cleavage of amyloid-beta1-40, pACD1 (presequence from Arabidopsis thaliana), SytII 40-60 (non-presequence of synaptotagmin from Rattus norvegicus), pCox4 (presequence from Saccharomyces cerevisiae), pOTC (human presequence), and pF1beta (presequence from NIcotiana plumbaginifolia), mass spectrometric analysis
-
-
?
additional information
?
-
-
the enzyme secreted from astrocytes would act in the extracellular space, thereby restricting diffusion of released neurotensin. The neuronal membrane-associated activity would be responsible for the physiological inactivation of the peptide either in the synaptic cleft, beside the neurotensin receptors, or inside early endosomal compartments in which receptor-ligand complexes would have been internalized
-
-
?
additional information
?
-
-
the enzyme is active in inactivation of neuropeptides, biological relevance, overview
-
-
?
additional information
?
-
-
the enzyme is involved in angiogenesis and tumor growth, overview
-
-
?
additional information
?
-
-
substrate and cleavage site specificity, overview, no activity with GFPPFRQ
-
-
?
additional information
?
-
-
membrane-bound variant of neurolysin functions as the non-angiotensin Type 1 (non-AT1), non-AT2 Angiotensin binding site
-
-
?
additional information
?
-
angiotensin I, dynorphin A(1-8) and metorphamide are no substrates of neurolysin
-
-
?
additional information
?
-
Nln hydrolyses several substrates that are affected by brain injury
-
-
?
additional information
?
-
Mcc-Pro-Leu-Gly-Pro-D-Lys-Dnp and neurotensin compete for their hydrolysis by enzyme Nln. Mcc-Pro-Leu-Gly-Pro-D-Lys-Dnp is particularly useful to study Nln distribution and ontogeny in murine brain
-
-
?
additional information
?
-
Nln hydrolyses several substrates that are affected by brain injury
-
-
?
additional information
?
-
Mcc-Pro-Leu-Gly-Pro-D-Lys-Dnp and neurotensin compete for their hydrolysis by enzyme Nln. Mcc-Pro-Leu-Gly-Pro-D-Lys-Dnp is particularly useful to study Nln distribution and ontogeny in murine brain
-
-
?
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
-
-
?
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
?
-
-
no activity with (o-aminobenzoyl)-LGMISLMKRPPGFSPFRSSRI-NH2
-
?
additional information
?
-
-
no activity with (o-aminobenzoyl)-PRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
?
additional information
?
-
Mcc-Pro-Leu-Gly-Pro-D-Lys-Dnp and neurotensin compete for their hydrolysis by enzyme Nln
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
FSTSAQNN + H2O
?
octMdh1, Oct1 generated octapeptide from Mus musculus
-
-
?
GlpLYENKPRRPYIL + H2O
GlpLYENKPRRP + YIL
neurotensin, secreted human neuropeptide
-
-
?
MFLTRFVGRRFLAAASARS + H2O
MFLTR + FVG + RRFL + 2 L-Ala + ASA + RS
pL29, presequence from Arabidopsis thaliana
-
-
?
MFRRPVLQVLRQFVRH + H2O
MFR + RPVL + QVLR + QFVRH
pSSBP, human presequence
-
-
?
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 is involved in the inactivation of numerous neuropeptides
-
-
?
additional information
?
-
-
the enzyme contributes to the catabolism of neurotensin in the dog intestine
-
-
?
additional information
?
-
-
the enzyme is active in inactivation of neuropeptides, biological relevance, overview
-
-
?
additional information
?
-
-
possible implication of the enzyme in the specific degradation of neurotensin and other peptide neurotransmitters in the synaptic cleft
-
-
?
additional information
?
-
-
the enzyme is active in inactivation of neuropeptides, biological relevance, overview
-
-
?
additional information
?
-
-
the enzyme secreted from astrocytes would act in the extracellular space, thereby restricting diffusion of released neurotensin. The neuronal membrane-associated activity would be responsible for the physiological inactivation of the peptide either in the synaptic cleft, beside the neurotensin receptors, or inside early endosomal compartments in which receptor-ligand complexes would have been internalized
-
-
?
additional information
?
-
-
the enzyme is active in inactivation of neuropeptides, biological relevance, overview
-
-
?
additional information
?
-
-
the enzyme is involved in angiogenesis and tumor growth, overview
-
-
?
additional information
?
-
-
membrane-bound variant of neurolysin functions as the non-angiotensin Type 1 (non-AT1), non-AT2 Angiotensin binding site
-
-
?
additional information
?
-
angiotensin I, dynorphin A(1-8) and metorphamide are no substrates of neurolysin
-
-
?
additional information
?
-
Nln hydrolyses several substrates that are affected by brain injury
-
-
?
additional information
?
-
Nln hydrolyses several substrates that are affected by brain injury
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
additional information
Zn2+
zinc metallopeptidase, residues His474, His478 and Glu503 take part in the coordination of the catalytic zinc ion
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
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)
molecular inhibitors of Gbetagama-dimer function
-
strain-dependent increases in EP24.16 activity are substantially attenuated by betaARK.ct by 86.4%
-
molecular inhibitors of Gialpha-subunit function
-
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
-
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
NF023
-
attenuates the strain-dependent elevation of endopeptidase activity by 82.2%
Pro-Phe-PSI(PO2CH2)Leu-Pro-NH2
-
potent and selective inhibitor of neurolysin
Pro-Xaa dipeptides
-
most potent inhibitors, Xaa-Pro dipeptides are ineffective
PTX
-
completely attenuates the cyclic strain-dependent increase in endopeptidase activity
-
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)
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
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
-
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
-
selective inhibitor of neurolysin, inhibition by milimolar concentrations
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
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
Pro-Ile is unable to affect endopeptidases 24.11 and 24.15, proline endopeptidase, angiotensin-converting enzyme, leucine aminopeptidase, diglutamyl aminopeptidase, and trypsin
-
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
-
additional information
additional information
-
putative intracellular peptides as competetive inhibitors of (o-aminobenzoyl)-GFSHFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) hydrolysis by EP24.16
-
additional information
-
inhibitor of neurolysin potentiates the neurotensin-induced anti-nociception
-
additional information
-
no inhibition by bestatin, captopril, leupeptin, and E64, poor inhibition by PMSF and Z-Pro-prolinal
-
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
-
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
Characterization and localization of mitochondrial oligopeptidase (MOP) (EC 3.4.24.16) activity in the human cervical adenocarcinoma cell line HeLa.
Brain Ischemia
Peptidase neurolysin functions to preserve the brain after ischemic stroke in male mice.
Carcinoma
The role of metalloendopeptidases in oropharyngeal carcinomas assessed by tissue microarray.
Carcinoma, Squamous Cell
The role of metalloendopeptidases in oropharyngeal carcinomas assessed by tissue microarray.
Colorectal Neoplasms
Discovery of Cell-Type-Specific and Disease-Related Enzymatic Activity Changes via Global Evaluation of Peptide Metabolism.
Hearing Loss
Loss of mitochondrial peptidase Clpp leads to infertility, hearing loss plus growth retardation via accumulation of CLPX, mtDNA and inflammatory factors.
Hypertension
Metalloendopeptidases EC 3.4.24.15 and EC 3.4.24.16 and bradykinin B2 receptors do not play important roles in renal wrap hypertension in rabbits.
Hypotension
A novel stable inhibitor of endopeptidases EC 3.4.24.15 and 3.4.24.16 potentiates bradykinin-induced hypotension.
Hypotension
Hemopressin: a novel bioactive peptide derived from the alpha1-chain of hemoglobin.
Hypotension
Neurotensin increases mortality and mast cells reduce neurotensin levels in a mouse model of sepsis.
Infarction, Middle Cerebral Artery
Functional up-regulation of endopeptidase neurolysin during post-acute and early recovery phases of experimental stroke in mouse brain.
Infertility
Loss of mitochondrial peptidase Clpp leads to infertility, hearing loss plus growth retardation via accumulation of CLPX, mtDNA and inflammatory factors.
Ischemic Stroke
Peptidase neurolysin functions to preserve the brain after ischemic stroke in male mice.
Ischemic Stroke
The role of peptidase neurolysin in neuroprotection and neural repair after stroke.
Leukemia, Myeloid, Acute
The role of mitochondrial proteases in leukemic cells and leukemic stem cells.
Melanoma
Characterization of thimet oligopeptidase and neurolysin activities in B16F10-Nex2 tumor cells and their involvement in angiogenesis and tumor growth.
Neoplasm Metastasis
Metallopeptidase, neurolysin, as a novel molecular tool for analysis of properties of cancer-producing matrix metalloproteinases-2 and -9.
Neoplasms
Characterization of thimet oligopeptidase and neurolysin activities in B16F10-Nex2 tumor cells and their involvement in angiogenesis and tumor growth.
Neoplasms
Metallopeptidase, neurolysin, as a novel molecular tool for analysis of properties of cancer-producing matrix metalloproteinases-2 and -9.
Neurodegenerative Diseases
Peptidase neurolysin is an endogenous cerebroprotective mechanism in acute neurodegenerative disorders.
Stroke
Functional up-regulation of endopeptidase neurolysin during post-acute and early recovery phases of experimental stroke in mouse brain.
Stroke
Peptidase neurolysin: Its function related to the brain renin-angiotensin system and pathophysiology of stroke. Letter to the Editor.
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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
-
-
0.0014
(o-aminobenzoyl)-AFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00115
(o-aminobenzoyl)-AKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.0023
(o-aminobenzoyl)-DFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00064
(o-aminobenzoyl)-EFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0058
(o-aminobenzoyl)-ENKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.00083
(o-aminobenzoyl)-FFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0023
(o-aminobenzoyl)-GASPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0684
(o-aminobenzoyl)-GDSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0318
(o-aminobenzoyl)-GESPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00087
(o-aminobenzoyl)-GFAPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0003
(o-aminobenzoyl)-GFDPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0031
(o-aminobenzoyl)-GFEPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0011
(o-aminobenzoyl)-GFFPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00033
(o-aminobenzoyl)-GFHPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00018
(o-aminobenzoyl)-GFIPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00019
(o-aminobenzoyl)-GFLPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00045
(o-aminobenzoyl)-GFNPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0037
(o-aminobenzoyl)-GFPPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.002
(o-aminobenzoyl)-GFQPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00039
(o-aminobenzoyl)-GFRPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0011
(o-aminobenzoyl)-GFSAFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0018
(o-aminobenzoyl)-GFSDFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.003
(o-aminobenzoyl)-GFSEFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0015
(o-aminobenzoyl)-GFSFFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0013
(o-aminobenzoyl)-GFSHFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00085
(o-aminobenzoyl)-GFSIFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0018
(o-aminobenzoyl)-GFSLFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0013
(o-aminobenzoyl)-GFSNFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00012
(o-aminobenzoyl)-GFSPARQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0032
(o-aminobenzoyl)-GFSPDRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00022
(o-aminobenzoyl)-GFSPERQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00095
(o-aminobenzoyl)-GFSPFAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00023
(o-aminobenzoyl)-GFSPFDQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0011
(o-aminobenzoyl)-GFSPFEQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.002
(o-aminobenzoyl)-GFSPFFQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0024
(o-aminobenzoyl)-GFSPFHQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00042
(o-aminobenzoyl)-GFSPFIQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0056
(o-aminobenzoyl)-GFSPFLQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0033
(o-aminobenzoyl)-GFSPFNQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00055
(o-aminobenzoyl)-GFSPFPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0061
(o-aminobenzoyl)-GFSPFQQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0011
(o-aminobenzoyl)-GFSPFRA-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00018
(o-aminobenzoyl)-GFSPFRE-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00022
(o-aminobenzoyl)-GFSPFRF-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00044
(o-aminobenzoyl)-GFSPFRI-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0014
(o-aminobenzoyl)-GFSPFRL-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00015
(o-aminobenzoyl)-GFSPFRN-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0017
(o-aminobenzoyl)-GFSPFRP-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00058
(o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00021
(o-aminobenzoyl)-GFSPFRR-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00065
(o-aminobenzoyl)-GFSPFRS-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0011
(o-aminobenzoyl)-GFSPFSQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00021
(o-aminobenzoyl)-GFSPHRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00091
(o-aminobenzoyl)-GFSPIRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0024
(o-aminobenzoyl)-GFSPLRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0002
(o-aminobenzoyl)-GFSPNRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0011
(o-aminobenzoyl)-GFSPPRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0013
(o-aminobenzoyl)-GFSPQRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00003
(o-aminobenzoyl)-GFSPRRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00078
(o-aminobenzoyl)-GFSPSRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0024
(o-aminobenzoyl)-GFSQFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00058
(o-aminobenzoyl)-GFSRFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0111
(o-aminobenzoyl)-GFSSFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0016
(o-aminobenzoyl)-GFSXFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00047
(o-aminobenzoyl)-GGFLPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.0005
(o-aminobenzoyl)-GGFLRRAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0033
(o-aminobenzoyl)-GGFLRRDQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0019
(o-aminobenzoyl)-GGFLRREQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0007
(o-aminobenzoyl)-GGFLRRFQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0017
(o-aminobenzoyl)-GGFLRRHQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0018
(o-aminobenzoyl)-GGFLRRIQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0007
(o-aminobenzoyl)-GGFLRRLQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0015
(o-aminobenzoyl)-GGFLRRNQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0012
(o-aminobenzoyl)-GGFLRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0023
(o-aminobenzoyl)-GGFLRRRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0022
(o-aminobenzoyl)-GGFLRRV-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0021
(o-aminobenzoyl)-GGFLRRVQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0006
(o-aminobenzoyl)-GGFLRRYQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C
0.0025
(o-aminobenzoyl)-GHSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0047
(o-aminobenzoyl)-GISPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0059
(o-aminobenzoyl)-GLSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0075
(o-aminobenzoyl)-GNSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0063
(o-aminobenzoyl)-GPSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0068
(o-aminobenzoyl)-GQSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0013
(o-aminobenzoyl)-GRSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0058
(o-aminobenzoyl)-GSSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00033
(o-aminobenzoyl)-HFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0012
(o-aminobenzoyl)-IFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0033
(o-aminobenzoyl)-KPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.0017
(o-aminobenzoyl)-LFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00044
(o-aminobenzoyl)-LYENKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.00103
(o-aminobenzoyl)-NAPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.0013
(o-aminobenzoyl)-NFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00138
(o-aminobenzoyl)-NKARRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.00056
(o-aminobenzoyl)-NKPARPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.00082
(o-aminobenzoyl)-NKPRAPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.00025
(o-aminobenzoyl)-NKPRRAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.00119
(o-aminobenzoyl)-NKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.00033
(o-aminobenzoyl)-QFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00032
(o-aminobenzoyl)-RFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00048
(o-aminobenzoyl)-SFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
0.00497
(o-aminobenzoyl)-AKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
1.35
(o-aminobenzoyl)-ENKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
1.3
(o-aminobenzoyl)-GASPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.34
(o-aminobenzoyl)-GDSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.8
(o-aminobenzoyl)-GFAPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.2
(o-aminobenzoyl)-GFDPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.07
(o-aminobenzoyl)-GFEPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.27
(o-aminobenzoyl)-GFIPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.24
(o-aminobenzoyl)-GFLPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.39
(o-aminobenzoyl)-GFQPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
2.6
(o-aminobenzoyl)-GFSAFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
2.5
(o-aminobenzoyl)-GFSDFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.19
(o-aminobenzoyl)-GFSEFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
3.4
(o-aminobenzoyl)-GFSFFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
4.8
(o-aminobenzoyl)-GFSHFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.22
(o-aminobenzoyl)-GFSIFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
3.5
(o-aminobenzoyl)-GFSLFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
8.8
(o-aminobenzoyl)-GFSNFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.4
(o-aminobenzoyl)-GFSPARQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
1.8
(o-aminobenzoyl)-GFSPFDQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
5.9
(o-aminobenzoyl)-GFSPFLQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
1.4
(o-aminobenzoyl)-GFSPFPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
1.1
(o-aminobenzoyl)-GFSPFRE-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
1.8
(o-aminobenzoyl)-GFSPFRF-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
1.9
(o-aminobenzoyl)-GFSPFRI-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
7.4
(o-aminobenzoyl)-GFSPFRL-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
1.9
(o-aminobenzoyl)-GFSPFRN-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.45
(o-aminobenzoyl)-GFSPFRR-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
2.1
(o-aminobenzoyl)-GFSPFRS-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.19
(o-aminobenzoyl)-GFSPHRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
0.15
(o-aminobenzoyl)-GFSPPRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
2.6
(o-aminobenzoyl)-GFSPQRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
0.42
(o-aminobenzoyl)-GFSPRRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
1.5
(o-aminobenzoyl)-GFSPSRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
0.31
(o-aminobenzoyl)-GFSRFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
7.5
(o-aminobenzoyl)-GFSSFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
3.6
(o-aminobenzoyl)-GFSXFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
3.2
(o-aminobenzoyl)-GGFLRRAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C, cleavage of the R-R bond
1
(o-aminobenzoyl)-GGFLRRDQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C, cleavage of the R-R bond
1.1
(o-aminobenzoyl)-GGFLRREQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C, cleavage of the R-R bond
1.8
(o-aminobenzoyl)-GGFLRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C, cleavage of the R-R bond
3.3
(o-aminobenzoyl)-GGFLRRRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C, cleavage of the R-R bond
2
(o-aminobenzoyl)-GGFLRRV-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C, cleavage of the R-R bond
1.4
(o-aminobenzoyl)-GGFLRRVQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C, cleavage of the R-R bond
0.95
(o-aminobenzoyl)-GHSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
2.6
(o-aminobenzoyl)-GISPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
6.2
(o-aminobenzoyl)-GLSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
1.3
(o-aminobenzoyl)-GNSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
2.2
(o-aminobenzoyl)-GPSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
1.9
(o-aminobenzoyl)-GQSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
5.4
(o-aminobenzoyl)-GRSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
1.2
(o-aminobenzoyl)-HFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
3.8
(o-aminobenzoyl)-LYENKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.00697
(o-aminobenzoyl)-NAPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.00576
(o-aminobenzoyl)-NKARRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.00123
(o-aminobenzoyl)-NKPARPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.014
(o-aminobenzoyl)-NKPRAPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.00124
(o-aminobenzoyl)-NKPRRAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
7
(o-aminobenzoyl)-NKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
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
0.1
(o-aminobenzoyl)-AFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
0.27
(o-aminobenzoyl)-AFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
0.02
(o-aminobenzoyl)-DFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
0.12
(o-aminobenzoyl)-DFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
0.01
(o-aminobenzoyl)-EFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
0.08
(o-aminobenzoyl)-EFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
0.03
(o-aminobenzoyl)-FFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
0.23
(o-aminobenzoyl)-FFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
0.84
(o-aminobenzoyl)-GESPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
6.08
(o-aminobenzoyl)-GESPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
1.28
(o-aminobenzoyl)-GFFPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
6.08
(o-aminobenzoyl)-GFFPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.52
(o-aminobenzoyl)-GFHPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
6.08
(o-aminobenzoyl)-GFHPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.64
(o-aminobenzoyl)-GFNPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
6.08
(o-aminobenzoyl)-GFNPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.62
(o-aminobenzoyl)-GFPPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
6.08
(o-aminobenzoyl)-GFPPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.97
(o-aminobenzoyl)-GFRPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
6.08
(o-aminobenzoyl)-GFRPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.03
(o-aminobenzoyl)-GFSPDRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
0.24
(o-aminobenzoyl)-GFSPDRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
0.14
(o-aminobenzoyl)-GFSPERQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
0.65
(o-aminobenzoyl)-GFSPERQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
1.3
(o-aminobenzoyl)-GFSPFAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
1.4
(o-aminobenzoyl)-GFSPFAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
0.29
(o-aminobenzoyl)-GFSPFEQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
1.6
(o-aminobenzoyl)-GFSPFEQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
0.4
(o-aminobenzoyl)-GFSPFFQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
1.4
(o-aminobenzoyl)-GFSPFFQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
0.88
(o-aminobenzoyl)-GFSPFHQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
1.4
(o-aminobenzoyl)-GFSPFHQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
6.08
(o-aminobenzoyl)-GFSPFHQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
0.61
(o-aminobenzoyl)-GFSPFIQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
6.08
(o-aminobenzoyl)-GFSPFIQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
0.64
(o-aminobenzoyl)-GFSPFNQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
1.1
(o-aminobenzoyl)-GFSPFNQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
6.08
(o-aminobenzoyl)-GFSPFNQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
0.56
(o-aminobenzoyl)-GFSPFQQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
0.73
(o-aminobenzoyl)-GFSPFQQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
6.08
(o-aminobenzoyl)-GFSPFQQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
6.08
(o-aminobenzoyl)-GFSPFQQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
0.83
(o-aminobenzoyl)-GFSPFRP-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
6.08
(o-aminobenzoyl)-GFSPFRP-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.31
(o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.31
(o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
0.31
(o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
1.1
(o-aminobenzoyl)-GFSPFSQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
1.3
(o-aminobenzoyl)-GFSPFSQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
0.53
(o-aminobenzoyl)-GFSPIRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
0.65
(o-aminobenzoyl)-GFSPIRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
6.08
(o-aminobenzoyl)-GFSPIRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
0.55
(o-aminobenzoyl)-GFSPLRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
1.3
(o-aminobenzoyl)-GFSPLRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
0.62
(o-aminobenzoyl)-GFSPNRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
6.08
(o-aminobenzoyl)-GFSPNRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
0.67
(o-aminobenzoyl)-GFSQFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
6.08
(o-aminobenzoyl)-GFSQFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
1.77
(o-aminobenzoyl)-GGFLPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
2.94
(o-aminobenzoyl)-GGFLPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.2
(o-aminobenzoyl)-GGFLRRFQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C, cleavage of the R-R bond
0.3
(o-aminobenzoyl)-GGFLRRFQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C, cleavage of the R-F bond
0.6
(o-aminobenzoyl)-GGFLRRHQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C, cleavage of the R-H bond
1.6
(o-aminobenzoyl)-GGFLRRHQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C, cleavage of the R-R bond
0.1
(o-aminobenzoyl)-GGFLRRIQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C, cleavage of the R-I bond
0.7
(o-aminobenzoyl)-GGFLRRIQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C, cleavage of the R-R bond
0.2
(o-aminobenzoyl)-GGFLRRLQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C, cleavage of the R-R bond
0.5
(o-aminobenzoyl)-GGFLRRLQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C, cleavage of the R-L bond
0.3
(o-aminobenzoyl)-GGFLRRNQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C, cleavage of the R-N bond
0.6
(o-aminobenzoyl)-GGFLRRNQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C, cleavage of the R-R bond
0.2
(o-aminobenzoyl)-GGFLRRYQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C, cleavage of the R-Y bond
0.3
(o-aminobenzoyl)-GGFLRRYQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4. 37°C, cleavage of the R-R bond
0.05
(o-aminobenzoyl)-IFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
0.45
(o-aminobenzoyl)-IFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
2.63
(o-aminobenzoyl)-KPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
3 - 6
(o-aminobenzoyl)-KPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.13
(o-aminobenzoyl)-LFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
0.35
(o-aminobenzoyl)-LFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
0.16
(o-aminobenzoyl)-NFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
1
(o-aminobenzoyl)-NFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
0.12
(o-aminobenzoyl)-QFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
0.39
(o-aminobenzoyl)-QFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
0.02
(o-aminobenzoyl)-RFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
0.27
(o-aminobenzoyl)-RFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
0.12
(o-aminobenzoyl)-SFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
0.77
(o-aminobenzoyl)-SFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
6.08
(o-aminobenzoyl)-SFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
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
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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)
additional information
additional information
additional information
-
peptide phosphorylation largely changes the kinetics of interaction and degredation by EP24.16
-
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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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
substrate specificity, and cell proliferation assay, overview
additional information
-
quantitative determination of cleavage activity of neurolysin toward MMP-specific fluorescence-quenching peptides
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
pH-dependence of wild-type and mutant enzymes, overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
membrane preparations of frontoparietal cortex, striatum, and hippocampus isolated from the ischemic hemisphere of mouse brain 24 h after reperfusion reveal a statistically significant over 2fold increase in quantity and activity of neurolysin compared with sham-operated controls, no effect on the cerebellar enzyme activity. Functional up-regulation of neurolysin in frontoparietal cortical membranes for at least 7 days after stroke appears not to be transcriptionally or translationally regulated, but rather depends on translocation of cytosolic neurolysin to the membranes and mitochondria
brenda
-
-
brenda
-
longitudinal smooth muscle membranes and circular smooth muscle membranes
brenda
additional information
membrane-bound Nln is up-regulated in mouse brain regions (frontoparietal cortex, striatum, and hippocampus) after stroke
brenda
additional information
upregulation of Nln does not appear to be transcriptionally or translationally regulated, but rather depends on translocation of cytosolic Nln to the membranes and mitochondria
brenda
additional information
-
membrane-bound Nln is up-regulated in mouse brain regions (frontoparietal cortex, striatum, and hippocampus) after stroke
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme secreted from astrocytes would act in the extracellular space, thereby restricting diffusion of released neurotensin
-
brenda
additional information
-
shorter form of neurolysin, lacking the cleavable mitochondrial targeting sequence, remains in the cytosol
brenda
-
synaptic and smooth muscle cell membranes in brain
brenda
-
the membrane-associated enzyme form increases during neuronal differentation and appears to be responsible for the overall augmentation of endopeptidase activity observed during neuronal maturation
brenda
-
the transfectants exhibit a membrane-associated form of endopeptidase-24.16, the catalytic site of which clearly faces the extracellular domain
brenda
-
the enzyme is not attached by a glycosyl-phosphatidylinositol anchor in the emembrane, the enzyme can not be released from the membrane upon trypsinolysis
brenda
-
longer form of neurolysin that contains a cleavable mitochondrial targeting sequence at the N-terminus
brenda
additional information
truncated enzyme NLN lacking the first 25 aa (region containing the mTP as predicted by TargetP) is not localized in the mitochondria
-
brenda
additional information
-
truncated enzyme NLN lacking the first 25 aa (region containing the mTP as predicted by TargetP) is not localized in the mitochondria
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
-
brain membranes of mice lacking neurolysin are nearly devoid of the non-AT1, non-AT2 angiotensin binding site
metabolism
a network of proteases may be required for complete degradation of peptides localized in mitochondria. Mechanism of peptide binding
physiological function
additional information
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 is involved in peptidergic systems that play a role in pathogenesis of stroke and resistance to ischemic injury and/or post-stroke brain recovery. Neurolysin may play a role in processes modulating the brain's response to stroke and its recovery after stroke
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
physiological function
neurolysin cleaves mitochondrial targeting peptides
physiological function
Nln secreted from B16F10-Nex2 melanoma cells might be able control angiogenesis. Nln hydrolyses several substrates that are affected by brain injury
physiological function
peptidase neurolysin is an endogenous cerebroprotective mechanism in acute neurodegenerative disorders. The enzyme is linked to neuronal cell death. Significant increase (about twofold) in quantity and activity of membrane Nln in ischemia-affected parts of the mouse brain. Enzyme Nln may play a role in processes modulating the brain's response to stroke
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
-
physiological function
-
Nln secreted from B16F10-Nex2 melanoma cells might be able control angiogenesis. Nln hydrolyses several substrates that are affected by brain injury
-
additional information
hNLN presents a prolate ellipsoidal shape consisting of two major domains that enclose the narrow catalytic channel. The enclosed cavity structure restricts substrate length. hNLN contains the conserved HExxH zinc-binding motif, which is a signature of the MA clan of metallopeptidases. In hNLN, the residues His474, His478 and Glu503 take part in the coordination of the catalytic zinc ion. NLN structure analysis, mechanism of peptide binding, detailed overview. The large hydrophobic side chains of Ile12NT2 and Leu13NT2 may be attracted by the strong hydrophobicity of the S3' (Leu558 and Phe599) and aromatic S4' residues (Phe226, Tyr339). A single hydrogen bond between Tyr610 and Tyr11NT2 contributes to the recognition of the peptide's main chain. In addition, Arg554 (S4') offers an anchor point for the carboxyl-terminus of NT2 via salt bridge formation. Overall, peptide stabilization occurs through mainchain interactions with the observed subsites within the catalytic cavity but with these interactions not imposing a strict substrate specificity
additional information
-
hNLN presents a prolate ellipsoidal shape consisting of two major domains that enclose the narrow catalytic channel. The enclosed cavity structure restricts substrate length. hNLN contains the conserved HExxH zinc-binding motif, which is a signature of the MA clan of metallopeptidases. In hNLN, the residues His474, His478 and Glu503 take part in the coordination of the catalytic zinc ion. NLN structure analysis, mechanism of peptide binding, detailed overview. The large hydrophobic side chains of Ile12NT2 and Leu13NT2 may be attracted by the strong hydrophobicity of the S3' (Leu558 and Phe599) and aromatic S4' residues (Phe226, Tyr339). A single hydrogen bond between Tyr610 and Tyr11NT2 contributes to the recognition of the peptide's main chain. In addition, Arg554 (S4') offers an anchor point for the carboxyl-terminus of NT2 via salt bridge formation. Overall, peptide stabilization occurs through mainchain interactions with the observed subsites within the catalytic cavity but with these interactions not imposing a strict substrate specificity
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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_BOVIN
704
0
80728
Swiss-Prot
Mitochondrion (Reliability: 1)
NEUL_HUMAN
704
0
80652
Swiss-Prot
Mitochondrion (Reliability: 1)
NEUL_MOUSE
704
0
80429
Swiss-Prot
Mitochondrion (Reliability: 1)
NEUL_PIG
704
0
80757
Swiss-Prot
Mitochondrion (Reliability: 1)
NEUL_PONAB
704
0
80798
Swiss-Prot
Mitochondrion (Reliability: 1)
NEUL_RABIT
704
0
80689
Swiss-Prot
Mitochondrion (Reliability: 1)
NEUL_RAT
704
0
80254
Swiss-Prot
Mitochondrion (Reliability: 1)
A0A1C3KY93_PLAMA
742
0
87789
TrEMBL
other Location (Reliability: 5)
A0A1G4GW15_PLAVI
744
0
85453
TrEMBL
Secretory Pathway (Reliability: 5)
A0A061IF43_CRIGR
681
0
77925
TrEMBL
other Location (Reliability: 4)
A0A1D3PAG7_PLAMA
743
0
88018
TrEMBL
other Location (Reliability: 5)
A0A2G9HMT5_9LAMI
189
0
21887
TrEMBL
other Location (Reliability: 1)
A0A1C3KR53_9APIC
752
0
88588
TrEMBL
Mitochondrion (Reliability: 5)
B9RMK4_RICCO
709
1
79979
TrEMBL
Mitochondrion (Reliability: 5)
A0A1G4HBD6_PLAVI
744
0
85481
TrEMBL
Secretory Pathway (Reliability: 5)
A0A1J1GST6_PLAGA
691
0
83091
TrEMBL
other Location (Reliability: 4)
G8NSE7_GRAMM
Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8)
664
0
74573
TrEMBL
-
A0A060RSR4_PLARE
755
0
91718
TrEMBL
other Location (Reliability: 5)
A0A0B2QRU6_GLYSO
708
1
79662
TrEMBL
other Location (Reliability: 4)
A0A653H6T1_9APIC
763
0
90806
TrEMBL
Mitochondrion (Reliability: 5)
A0A1J1H4J5_PLARL
688
0
82909
TrEMBL
other Location (Reliability: 3)
Q01Q81_SOLUE
Solibacter usitatus (strain Ellin6076)
715
0
79944
TrEMBL
-
F8A730_CELGA
Cellulomonas gilvus (strain ATCC 13127 / NRRL B-14078)
637
0
70625
TrEMBL
-
A0A2P6R0N9_ROSCH
708
1
80294
TrEMBL
Mitochondrion (Reliability: 5)
A0A1D3TGN7_9APIC
722
0
84757
TrEMBL
Mitochondrion (Reliability: 5)
E6PXI1_9ZZZZ
679
0
75467
TrEMBL
other Location (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
66000 - 70000
70000
75000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
additional information
hNLN presents a prolate ellipsoidal shape consisting of two major domains that enclose the narrow catalytic channel, NLN structure analysis, overview
additional information
-
hNLN presents a prolate ellipsoidal shape consisting of two major domains that enclose the narrow catalytic channel, NLN structure analysis, overview
additional information
-
three-dimensional structure, comparison to EC 3.4.24.15
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
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
no modification
no modification
-
the enzyme contains no glycosyl-phosphatidylinositol anchor
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme mutant NLNE475Q in complex with the products of neurotensin cleavage, X-ray diffraction structure determination and analysis at 2.7 A resolution
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
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E475Q
site-directed mutagenesis, the residue Glu475 coordinates a water molecule involved in the nucleophilic attack of the scissile bond and replacing this residue with glutamine (hNLNE475Q) results in a dramatic reduction of enzyme activity
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
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
H160A
site-directed mutagenesis, mutation of a surface histidine involved in a divalent cation-mediated lattice contact in the original neurolysin crystals
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
additional information
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
additional information
-
dominant-negative G protein mutants used to selectively disrupt Gialpha- and Gbetagamma-mediated signaling pathways attenuated strain-dependent increases for the enzyme
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
0.001 mM Zn2+ stabilizes
up to two cycles of freezing and thawing of the purified rNln do not significantly affect the purified recombinant enzyme's specific activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
a gradual decrease of the specific activity is observed in preparations kept longer than 6 months at -80°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a two-step purification procedure based on the molecular size and isoelectric point of the photoradiolabeled binding protein is conducted. Purified samples are subjected to two-dimensional gel electrophoresis followed by mass spectrometry identification of proteins in the two-dimensional gel sections containing radioactivity. LC-MS/MS analysis reveal protein candidates, of which the most abundant are immunoprecipitated after photoradiolabeling. Immunoprecipitation studies indicate that the angiotensin binding site is the membrane-bound variant of metalloendopeptidase neurolysin
-
recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli strain DH5alpha by glutathione affinity chromatography to homogeneity
-
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography, ultrafiltration, and gel filtration to homogeneity, large scale production of rNln
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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)
-
gene NLN
gene NLN, sequence comparisons and phylogenetic tree, transient transfection of HeLa cells with C-terminally myc-tagged full-length human NLN (hNLN1-704) followed by immunolocalization reveals a typical mitochondrial pattern. Transfection with a construct lacking the first 25 aa (region containing the mTP as predicted by TargetP) abolishes the mitochondrial localization of hNLN
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
-
recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
membrane-bound endopeptidase neurolysin is up-regulated in different parts of mouse brain affected by focal ischemia-reperfusion in a middle cerebral artery occlusion model of stroke, up-regulation of neurolysin occurs in post-ischemic brain regions
-
membrane-bound Nln is up-regulated in mouse brain regions (frontoparietal cortex, striatum, and hippocampus) after stroke
the enzyme is upregulated in mouse brain after stroke. Upregulation of Nln does not appear to be transcriptionally or translationally regulated, but rather depends on translocation of cytosolic Nln to the membranes and mitochondria
membrane-bound Nln is up-regulated in mouse brain regions (frontoparietal cortex, striatum, and hippocampus) after stroke
membrane-bound Nln is up-regulated in mouse brain regions (frontoparietal cortex, striatum, and hippocampus) after stroke
-
-
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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
pharmacology
the ability of Nln to process several neuropeptides suggests that it could potentially serve as a single therapeutic target to modulate the function of multiple targets, the noted neuropeptide systems, critically involved in various mechanisms of brain injury or cerebroprotection/restoration
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
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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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Rodd, D.; Hersh, L.B.
Endopeptidase 24.16B. A new variant of endopeptidase 24.16
J. Biol. Chem.
270
10056-10061
1995
Rattus norvegicus
brenda
Dauch, P.; Vincent, J.P.; Checler, F.
Specific inhibition of endopeptidase 24.16 by dipeptides
Eur. J. Biochem.
202
269-276
1991
Rattus norvegicus
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
-
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
-
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Kitabgi, P.
Inactivation of neurotensin and neuromedin N by Zn metallopeptidases
Peptides
27
2515-2522
2006
Canis lupus familiaris, Homo sapiens, Mus musculus
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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)
brenda
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
brenda
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)
brenda
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
brenda
Karamyan, V.T.
Peptidase neurolysin is an endogenous cerebroprotective mechanism in acute neurodegenerative disorders
Med. Hypotheses
131
109309
2019
Mus musculus (Q91YP2)
brenda
Checler, F.; Ferro, E.S.
Neurolysin from initial detection to latest advances
Neurochem. Res.
43
2017-2024
2018
Bos taurus (A2VDQ5), Homo sapiens (Q9BYT8), Mus musculus (Q91YP2), Mus musculus C57BL6 (Q91YP2), Rattus norvegicus (P42676), Sus scrofa (Q02038)
brenda
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