3.4.24.16: neurolysin
This is an abbreviated version!
For detailed information about neurolysin, go to the full flat file.
Word Map on EC 3.4.24.16
-
3.4.24.16
-
bradykinin
-
metallopeptidase
-
metalloendopeptidase
-
dynorphins
-
pro-ile
-
neuropeptidase
-
pro10-tyr11
-
neuromedin
-
hemopressins
-
arg8-arg9
-
non-at2
-
neurotensin-degrading
-
molecular biology
-
pharmacology
-
medicine
- 3.4.24.16
- bradykinin
- metallopeptidase
- metalloendopeptidase
- dynorphins
- pro-ile
-
neuropeptidase
-
pro10-tyr11
-
neuromedin
- hemopressins
-
arg8-arg9
-
non-at2
-
neurotensin-degrading
- molecular biology
- pharmacology
- medicine
Reaction
Preferential cleavage in neurotensin: Pro10-/-Tyr =
Synonyms
endopeptidase 24.16, endopeptidase 24.16B, endopeptidase 3.4.24.16, EP 24.16, ep24.16, EP24.16c, EP24.16m, MEP, Microsomal endopeptidase, mitochondrial peptidase, MOP, More, NEL, neurolisin, neurolysin, neurotensin endopeptidase, neurotensin-cleaving enzyme, Nln, oligopeptidase M, peptidase, neurotensin endo, peptidase, neurotensin endo-, SABP, soluble angiotensin II-binding protein, Soluble angiotensin-binding protein, thimet oligopeptidase II, thimet peptidase II
ECTree
3.4.24.16 neurolysinAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.24.16 - neurolysin
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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
-
-
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-
?
additional information
?
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-
the enzyme is involved in the inactivation of numerous neuropeptides
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-
?
additional information
?
-
Mcc-Pro-Leu-Gly-Pro-D-Lys-Dnp and neurotensin compete for their hydrolysis by enzyme Nln
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-
?
additional information
?
-
-
the enzyme contributes to the catabolism of neurotensin in the dog intestine
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-
?
additional information
?
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-
the enzyme is active in inactivation of neuropeptides, biological relevance, overview
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-
?
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
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-
?
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
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-
?
additional information
?
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-
the enzyme is active in inactivation of neuropeptides, biological relevance, overview
-
-
?
additional information
?
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-
the enzyme is involved in angiogenesis and tumor growth, overview
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-
?
additional information
?
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-
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
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-
?
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
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-
?
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
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-
?
additional information
?
-
-
the enzyme can participate in the physiological inactivation of neurotensin
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-
?
additional information
?
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-
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
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-
?
additional information
?
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-
the enzyme is likely involved in the physiological termination of the neurotensinergic signal in the central nervous system and in the gastrointestinal tract
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-
?
additional information
?
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-
the enzyme cleaves several bioactive peptides at sites similar or different from thimet oligopeptidase, EC 3.4.24.15
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-
?
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
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-
?
additional information
?
-
-
cleavage sites of wild-type and mutant enzymes, overview
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-
?
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
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-
?
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
-
-
?
