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(7-methoxycoumarin-4-acetyl)-Pro-Leu-Gly-Pro-dLys-(2,4-dinitrophenyl) + H2O
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Pro-D-Lys(2,4-dinitrophenyl) + H2O
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl) + H2O
?
-
fluorogenic substrate
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH + H2O
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-OH
-
-
-
-
?
(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
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Gly-Gly-Phe-Leu-Arg-Arg-Ala-Lys-dinitrophenyl
(7-methoxycoumarin-4-yl)acetyl-Gly-Gly-Phe-Leu + Arg-Arg-Ala-Lys-dinitrophenyl
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH + H2O
?
-
in wild-type, clear preference for the 7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin substrate over 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol and 7-methoxycoumarin-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
-
?
(7-methoxycoumarin-4-yl)actayl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH + H2O
?
-
-
-
-
?
(Gly-Pro-Leu)n
Gly-Pro-Leu
-
n = 2, 3, 4 and 5, the peptides are cleaved only at Leu-Gly bonds, activity is most rapid with n = 3 and slowest with n = 5. The cleavage fitts a sequential first-order model
-
?
(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)-ENKPRRPYIQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(ortho-aminobenzoyl)-ENKPR + RPYIQ-(N-(2,4-dinitrophenyl)ethylenediamine) + (ortho-aminobenzoyl)-KPRRP + YIQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
84% cleavage at R-R bond, 16% cleavage at P-Y bond
-
?
(o-aminobenzoyl)-ENKPRRPYQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(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)-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)-GFSD + 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)-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)-GFSPFDQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GF + SPFDQ-(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)-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)-GF + SPFPQ-(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)
-
72% of the activity with (o-aminobenzoyl)-GFSPFRQ-(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)
-
14% 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)
-
8% of the activity with (o-aminobenzoyl)-GFSPFRQ-(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)-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)-GFSQFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSQ + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-GFSRFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-GFSR + 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)-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)-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) + (ortho-aminobenzoyl)-LYENKPRRPY + ILQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
68% cleavage at P-Y bond, 32% 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)-NKARRPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
?
-
-
-
-
?
(o-aminobenzoyl)-NKPARPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
?
-
-
-
-
?
(o-aminobenzoyl)-NKPRAPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
?
-
-
-
-
?
(o-aminobenzoyl)-NKPRRAPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
?
-
-
-
-
?
(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)-Phe-Arg-Lys-(dinitrophenyl-proline) + H2O
(o-aminobenzoyl)-Phe-Arg + Lys-(dinitrophenyl-proline)
-
-
-
?
(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)-RPPGFSPFR-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-RPPGF + SPFR-(N-(2,4-dinitrophenyl)ethylenediamine)
(o-aminobenzoyl)-RPPGFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-RPPGFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
(o-aminobenzoyl)-RPPGFSPFRSSRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-RPPGFSPFRS + SRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
23% of the activity with (o-aminobenzoyl)-GFSPFRQ-(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)
-
-
-
?
2,4-dinitrophenyl-Pro-Leu-Gly-Pro-Trp-D-Lys
?
2-aminobenzoyl-GFSHFRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-GFSH + FRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-GGFLRRDQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
2-aminobenzoyl-GGFL + RRDQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + 2-aminobenzoyl-GGFLR + RDQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
absence of Ca2+, 37% cleavage of R-R bond and 63% cleavage of L-R bond. Presence of 50 mM Ca2+, 74% cleavage of R-R bond and 26% of L-R bond
-
-
?
2-aminobenzoyl-GGFLRRVQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
2-aminobenzoyl-GGFL + RRVQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + 2-aminobenzoyl-GGFLR + RVQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
absence of Ca2+, 64% cleavage of R-R bond and 36% cleavage of L-R bond. Presence of 50 mM Ca2+, 79% cleavage of R-R bond and 21% of L-R bond
-
?
4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-Arg
4-phenylazobenzyloxycarbonyl-Pro-Leu + Gly-Pro-Arg
4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg
4-phenylazobenzyloxycarbonyl-Pro + Leu-Gly-Pro-D-Arg
-
-
-
?
4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg + H2O
?
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-(2,4-ditritrophenyl)Lys
?
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-(N6-(2,4-dinitrophenyl))Lys + H2O
?
-
-
-
-
?
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-Lys(2,4-dinitrophenyl) + H2O
?
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
7-methoxycoumarin-3-carboxylyl-Pro-Leu + Gly-Pro-D-Lys-dinitrophenyl
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin + H2O
?
-
-
-
?
7-methoxycoumarin-4-acetyl-PLGPdK-(2,4-dinitrophenyl) + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl) + H2O
?
-
-
-
?
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-2,4-dinitrophenyl + H2O
?
-
fluorogenic substrate
-
-
?
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-(2,4-dinitrophenyl) + H2O
?
-
-
-
?
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol + H2O
?
-
in wild-type, clear preference for the 7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin substrate over 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol and 7-methoxycoumarin-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
-
?
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenyl + H2O
?
-
-
?
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin + H2O
?
-
in wild-type, clear preference for the 7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin substrate over 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol and 7-methoxycoumarin-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
-
?
7-methoxycoumaryl-4-acetyl-Pro-Leu-Gly-D-Lys-(2,4-dinitrophenyl) + H2O
?
-
-
-
?
7-methoxycoumaryl-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl) + H2O
?
-
-
-
?
7-methoxycoumatin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl) + H2O
?
-
-
-
?
Abz-GFDPFRQ-EDDnp + H2O
?
Abz-GFSAFRQ-EDDnp + H2O
Abz-GFSA + FRQ-EDDnp
Abz-GFSDFRQ-EDDnp + H2O
Abz-GFSD + FRQ-EDDnp
-
-
-
-
?
Abz-GFSEFRQ-EDDnp + H2O
Abz-GFSE + FRQ-EDDnp
Abz-GFSFFRQ-EDDnp + H2O
Abz-GFSF + FRQ-EDDnp
Abz-GFSHFRQ-EDDnp + H2O
Abz-GFSH + FRQ-EDDnp
Abz-GFSIFR-EDDnp + H2O
Abz-GFSI + FR-EDDnp
-
-
-
-
?
Abz-GFSIFRQ-EDDnp + H2O
Abz-GFSI + FRQ-EDDnp
Abz-GFSLFRQ-EDDnp + H2O
Abz-GFSL + FRQ-EDDnp
-
-
-
-
?
Abz-GFSPARQ-EDDnp + H2O
Abz-GFSP + Ala-Arg-Gln-EDDnp
-
-
-
-
?
Abz-GFSPDRQ-EDDnp + 2 H2O
Abz-Gly-Phe + Ser-Pro + Asp-Arg-Gln-EDDnp
-
-
-
-
?
Abz-GFSPERQ-EDDnp + 2 H2O
Abz-Gly-Phe + Ser-Pro + Glu-Arg-Gln-EDDnp
-
-
-
-
?
Abz-GFSPFR-EDDnp + H2O
Abz-GFS + PFR-EDDnp
-
-
-
-
?
Abz-GFSPFRQ-EDDnp + H2O
?
Abz-GFSPFRQ-EDDnp + H2O
Abz-GFSP + FRQ-EDDnp
Abz-GFSPHRQ-EDDnp + H2O
Abz-GFSP + His-Arg-Gln-EDDnp
-
-
-
-
?
Abz-GFSPIRQ-EDDnp + 2 H2O
Abz-Gly-Phe + Ser-Pro + Ile-Arg-Gln-EDDnp
-
-
-
-
?
Abz-GFSPLRQ-EDDnp + 2 H2O
Abz-Gly-Phe + Ser-Pro + Leu-Arg-Gln-EDDnp
-
-
-
-
?
Abz-GFSPQRQ-EDDnp + H2O
Abz-GFSP + Gln-Arg-Gln-EDDnp
-
-
-
-
?
Abz-GFSPRRQ-EDDnp + H2O
Abz-GFSP + Arg-Arg-Gln-EDDnp
-
-
-
-
?
Abz-GFSPSRQ-EDDnp + H2O
Abz-GFSP + Ser-Arg-Gln-EDDnp
-
-
-
-
?
Abz-GFSQFRQ-EDDnp + H2O
Abz-GFSQ + FRQ-EDDnp
Abz-GFSRFRQ-EDDnp + H2O
Abz-GFSR + FRQ-EDDnp
Abz-GFSSFRQ-EDDnp + H2O
Abz-GFSS + FRQ-EDDnp
Abz-GFSWFRQ-EDDnp + H2O
Abz-GFSW + FRQ-EDDnp
Abz-GFSYFRQ-EDDnp + H2O
Abz-GFSY + FRQ-EDDnp
-
-
-
-
?
Abz-NKPRRPQ-EDDnp + H2O
Abz-NKPR + RPQ-EDDnp
-
-
-
-
?
Abz-RPPGFSPFRQ-EDDnp + H2O
Abz-RPPGFS + PFRQ-EDDnp
-
-
-
-
?
adrenorphin
peptide fragments
Ala-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-Thr-Phe-Thr-Ser-Cys + H2O
?
alpha-neoendorphin + H2O
?
aminobenzyl-Ala-Gly-Leu-Ala-nitrobenzylamide
aminobenzyl-Ala-Gly + Leu-Ala-nitrobenzylamide
-
weak
-
?
amyloid precursor protein + H2O
?
-
-
-
-
?
amyloid precursor protein-derived substrate
peptide fragments
-
spanning the beta-secretase site Ile-Ser-Glu-Val-Lys-Met-Asp-Ala-Glu-Phe-Arg-His-Asp-Ser, cleavage occurs predominantly at Lys-Met and Glu-Phe bonds
-
?
angiotensin I + H2O
angiotensin-(1-7) + ?
angiotensin II + H2O
?
-
7% of the activity with bradykinin
-
?
angiotensin-I + H2O
?
-
-
-
-
?
angiotensin-II + H2O
?
-
-
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met + H2O
peptide fragments
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe + Ser-Pro-Phe-Arg
ASNENMETM + H2O
?
-
-
-
?
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
benzoyl-Arg-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Arg + Ala-Ala-Phe-p-aminobenzoate
-
-
-
?
benzoyl-Asp-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Asp + Ala-Ala-Phe-p-aminobenzoate
-
-
-
?
benzoyl-Gly-Ala-Ala-Gly + H2O
benzoyl-Gly + Ala-Ala-Gly
-
-
-
-
?
benzoyl-Gly-Ala-Ala-Gly-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Gly-p-aminobenzoate
benzoyl-Gly-Ala-Ala-Leu-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Leu-p-aminobenzoate
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly-Arg-Ala-Ala-Phe-4-aminobenzoate + H2O
?
-
-
-
-
?
benzoyl-Gly-Arg-Ala-Ala-Phe-4-aminobenzoate + H2O
benzoyl-Gly-Arg + Ala-Ala-Phe-4-aminobenzoate
-
-
-
-
?
benzoyl-Gly-Asp-Ala-Ala-Phe-4-aminobenzoate + H2O
?
-
-
-
-
?
benzoyl-Gly-Asp-Ala-Ala-Phe-4-aminobenzoate + H2O
benzoyl-Gly-Asp + Ala-Ala-Phe-4-aminobenzoate
-
-
-
-
?
benzoyl-Gly-Gly-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Gly-Ala-Phe-p-aminobenzoate
benzoyl-Gly-Lys-Arg-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly-Lys-Arg + Ala-Ala-Phe-p-aminobenzoate
-
-
-
?
benzoyl-Gly-Phe-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly-Phe + Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly-Phe-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Phe-Ala-Phe-p-aminobenzoate
benzoyl-Gly-Phe-Phe-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly-Phe-Phe + Ala-Ala-Phe-p-aminobenzoate
-
-
-
?
beta-neoendorphin + H2O
?
cholecystokinin-8
peptide fragments
corticotropin-like intermediate lobe peptide
peptide fragments
CPI-0004Na + H2O
?
-
tetrapeptidic prodrug of doxorubicin
-
-
?
dinitrophenyl-Pro-Leu-Gly-Pro-Trp-D-Lys
dinitrophenyl-Pro-Leu + Gly-Pro-Trp-D-Lys
dynorphin A1-8 + H2O
?
-
-
-
-
?
ELFADKVPKTAENFR + 2 H2O
ELFADKVPKTA + Glu-Asn + Phe-Arg
-
intracellular peptide identified as a substrate by incubation of HEK-293 cell extract with recombinant enzyme. Peptide is derived from peptidylprolyl isomerase A
-
-
?
ELFSYLIEKVKR + H2O
ELFSYLIEK + VKR
-
purified TOP efficiently cleaves the nardilysin-dependent 12- and 13-residue precursors PRA(190-201) (ELFSYLIEKVKR) and PRA(190-202) (ELFSYLIEKVKRK) directly after the epitope's C-terminal Lys198
-
-
?
ELFSYLIEKVKRK + H2O
ELFSYLIEK + VKRK
-
purified TOP efficiently cleaves the nardilysin-dependent 12- and 13-residue precursors PRA(190-201) (ELFSYLIEKVKR) and PRA(190-202) (ELFSYLIEKVKRK) directly after the epitopes C-terminal Lys198
-
-
?
FAPGNYPAL + H2O
?
-
-
-
?
GFGDLKSPAGLQV + H2O
GFGDLK + SPAGLQV
-
intracellular peptide identified as a substrate by incubation of HEK-293 cell extract with recombinant enzyme. Peptide is derived from eukaryotic translation elongation factor 1beta2
-
-
?
Gly-Pro-Leu-Gly-Pro-Leu + H2O
?
-
-
-
-
?
Gly-Pro-Leu-Gly-Pro-Leu-Gly-Pro-Leu + H2O
?
-
-
-
-
?
Gly-Pro-Leu-Gly-Pro-Leu-Gly-Pro-Leu-Gly-Pro-Leu + H2O
?
-
-
-
-
?
Gly-Pro-Leu-Gly-Pro-Leu-Gly-Pro-Leu-Gly-Pro-Leu-Gly-Pro-Leu + H2O
?
-
-
-
-
?
gonadotrophin-releasing hormone + H2O
?
gonadotropin releasing hormone + H2O
?
-
-
-
-
?
gonadotropin-releasing hormone + H2O
?
-
-
-
?
gonadotropin-releasing hormone + H2O
peptide fragments
-
-
-
?
gondotropin-releasing hormone + H2O
?
IHSLPPEGKLG
IHSLPPE + GKLG
-
intracellular peptide identified as a substrate by incubation of HEK-293 cell extract with recombinant enzyme. Peptide is derived from cytochrome c oxidase subunit VIII
-
-
?
KDIEDVFYKY
KDIEDVF + YKY
-
intracellular peptide identified as a substrate by incubation of HEK-293 cell extract with recombinant enzyme. Peptide is derived from arginine/serine-rich splicing factor 1
-
-
?
LTLRTKL + H2O
LTLR + Thr + Lys-Leu
-
at 91% of the rate with RPPGF-SP-FR
-
-
?
luliberin
peptide fragments
-
-
-
-
?
LVVYPWTQRY + H2O
?
-
0.72% of the activity with bradykinin, cleavage sites: LVVYP-/-W-/-T-/-Q-/-RY
-
?
major histocompatibility complex class I-presented antigenic peptides + H2O
?
-
by destroying major histocompatibility complex class I-presented antigenic peptides the enzyme limits antigen presentation in vivo
-
?
Mca-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys (Dnp)-OH + H2O
?
-
-
-
?
Met-enkephalin-Arg6-Gly7-Leu8
?
-
-
-
-
?
N-acetyl-Ala-Ala-Ala
?
-
-
-
-
?
N-acetyl-Ala-Ala-Ala-Ala
N-acetyl-Ala + Ala-Ala-Ala
-
-
-
?
N-succinyl-Gly-Pro-4-methylcoumaryl-7-amide + H2O
?
-
-
-
?
o-aminobenzoyl-Gly-Gly-Phe-Leu-Arg-Arg-N-(2,4-dinitrophenyl)ethylenediamine
?
-
-
-
-
?
o-aminobenzoyl-Gly-Gly-Phe-Leu-Arg-Val-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
peptides of 9-17 residues generated by proteasomal degradation of casein + H2O
peptides of 6-9 residues
pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2 + H2O
pGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly-NH2
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
phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg
?
propionyl-Gly-Ser-Pro-(farnesyl-Cys)-Val-Leu-Met
propionyl-Gly-Ser-Pro-(farnesyl-Cys) + Val-Leu-Met
-
-
-
?
pTLRTKL + H2O
phospho-Thr-Leu-Arg + L-tyrosine + Lys-Leu
-
at 10% of the rate with RPPGF-SP-FR
-
-
?
PVNFKFLSH + H2O
?
-
140% of the activity with bradykinin, cleavage sites: PVNF-/-K-/-F-/-LSH
-
?
pyroGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly + H2O
pyroGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly
pyroGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly + H2O
pyroGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly + ?
-
i.e. luteinizing hormone-releasing hormone or LHRH-I, EP24.15 can convert the decapeptide LHRH-I to the active pentapeptide LHRH-(15). EP24.15 has a biomodulating action, forming a peptide product that opposes the action of its parent peptide
i.e. luteinizing hormone-releasing hormone(1-5) or LHRH-(1-5), the fragment does not bind to LHRH-receptor instead it has antagonistic properties at the N-methyl-D-aspartic acid receptor
-
?
RGPGRAFVTI + H2O
?
-
-
-
?
RPPGFSPFR + H2O
RPPGF + Ser-Pro + Phe-Arg
-
-
-
-
?
SAMTEEAAVAIKAMAK + H2O
SAMTEEAAVAIK + AMAK
-
intracellular peptide identified as a substrate by incubation of HEK-293 cell extract with recombinant enzyme. Peptide is derived from eukaryotic translation initiation factor 5A
-
-
?
succinyl-Ala-Ala-Ala-4-nitroanilide
succinyl-Ala-Ala + Ala-4-nitroanilide
-
weak
-
?
succinyl-Ala-Ala-Phe-4-nitroanilide
succinyl-Ala-Ala + Phe-4-nitroanilide
-
weak
-
?
succinyl-Ala-Ala-Val-4-nitroanilide
succinyl-Ala-Ala + Val-4-nitroanilide
-
weak
-
?
tert-butoxycarbonyl-Phe-Ala-Ala-Phe-p-aminobenzoate
tert-butoxycarbonyl-Phe + Ala-Ala-Phe-p-aminobenzoate
TPHPARIGL + H2O
?
-
-
-
?
TYQRTRALV + H2O
?
-
-
-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile + H2O
Tyr-Gly-Gly-Phe-Leu + Arg-Arg-Ile
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln + H2O
?
Tyr-Gly-Gly-Phe-Leu-Arg-Lys-Tyr-Pro
Tyr-Gly-Gly-Phe-Leu + Arg-Lys-Tyr-Pro
-
beta-neoendorphin
-
?
Val-Tyr-Ile-His-Pro-Phe-His-Leu + H2O
?
-
i.e. angiotensin I
-
-
?
vasoactive intestinal peptide
peptide fragments
VVYPW-TQ-RY-KL + H2O
VVYPW + Thr-Gln + Arg-Tyr + Lys-Leu
-
at 9% of the rate with RPPGF-SP-FR
-
-
?
VVYPWTQRY + H2O
?
-
10.6% of the activity with bradykinin, cleavage sites: VVYPW-/-T-/-Q-/-RY
-
?
additional information
?
-
(7-methoxycoumarin-4-acetyl)-Pro-Leu-Gly-Pro-dLys-(2,4-dinitrophenyl) + H2O
?
a fluorescent-quenched substrate
-
-
?
(7-methoxycoumarin-4-acetyl)-Pro-Leu-Gly-Pro-dLys-(2,4-dinitrophenyl) + H2O
?
a fluorescent-quenched substrate
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Pro-D-Lys(2,4-dinitrophenyl) + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Pro-D-Lys(2,4-dinitrophenyl) + H2O
?
-
-
-
-
?
(o-aminobenzoyl)-RPPGFSPFR-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-RPPGF + SPFR-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-RPPGFSPFR-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-RPPGF + SPFR-(N-(2,4-dinitrophenyl)ethylenediamine)
-
33% of the activity with (o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
?
(o-aminobenzoyl)-RPPGFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-RPPGFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
(o-aminobenzoyl)-RPPGFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
(o-aminobenzoyl)-RPPGFSP + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
85% of the activity with (o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
?
2,4-dinitrophenyl-Pro-Leu-Gly-Pro-Trp-D-Lys
?
-
-
-
-
?
2,4-dinitrophenyl-Pro-Leu-Gly-Pro-Trp-D-Lys
?
-
-
-
-
?
4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-Arg
4-phenylazobenzyloxycarbonyl-Pro-Leu + Gly-Pro-Arg
-
i.e. Pz-peptide
-
-
?
4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-Arg
4-phenylazobenzyloxycarbonyl-Pro-Leu + Gly-Pro-Arg
-
i.e. Pz-peptide
-
-
?
4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-Arg
4-phenylazobenzyloxycarbonyl-Pro-Leu + Gly-Pro-Arg
-
-
-
?
4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-Arg
4-phenylazobenzyloxycarbonyl-Pro-Leu + Gly-Pro-Arg
-
-
-
?
4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg + H2O
?
-
-
-
-
?
4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg + H2O
?
-
-
-
-
?
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-(2,4-ditritrophenyl)Lys
?
-
-
-
-
?
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-(2,4-ditritrophenyl)Lys
?
-
-
-
-
?
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-Lys(2,4-dinitrophenyl) + H2O
?
-
-
-
?
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-Lys(2,4-dinitrophenyl) + H2O
?
-
-
-
?
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
7-methoxycoumarin-3-carboxylyl-Pro-Leu + Gly-Pro-D-Lys-dinitrophenyl
-
-
-
?
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
7-methoxycoumarin-3-carboxylyl-Pro-Leu + Gly-Pro-D-Lys-dinitrophenyl
-
-
-
?
Abz-GFDPFRQ-EDDnp + H2O
?
-
-
-
?
Abz-GFDPFRQ-EDDnp + H2O
?
-
-
-
?
Abz-GFSAFRQ-EDDnp + H2O
Abz-GFSA + FRQ-EDDnp
-
-
-
-
?
Abz-GFSAFRQ-EDDnp + H2O
Abz-GFSA + FRQ-EDDnp
-
-
-
-
?
Abz-GFSEFRQ-EDDnp + H2O
Abz-GFSE + FRQ-EDDnp
-
-
-
-
?
Abz-GFSEFRQ-EDDnp + H2O
Abz-GFSE + FRQ-EDDnp
-
-
-
-
?
Abz-GFSFFRQ-EDDnp + H2O
Abz-GFSF + FRQ-EDDnp
-
-
-
-
?
Abz-GFSFFRQ-EDDnp + H2O
Abz-GFSF + FRQ-EDDnp
-
-
-
-
?
Abz-GFSHFRQ-EDDnp + H2O
Abz-GFSH + FRQ-EDDnp
-
-
-
-
?
Abz-GFSHFRQ-EDDnp + H2O
Abz-GFSH + FRQ-EDDnp
-
-
-
-
?
Abz-GFSIFRQ-EDDnp + H2O
Abz-GFSI + FRQ-EDDnp
-
-
-
-
?
Abz-GFSIFRQ-EDDnp + H2O
Abz-GFSI + FRQ-EDDnp
-
-
-
-
?
Abz-GFSPFRQ-EDDnp + H2O
?
-
-
-
?
Abz-GFSPFRQ-EDDnp + H2O
?
-
-
-
?
Abz-GFSPFRQ-EDDnp + H2O
Abz-GFSP + FRQ-EDDnp
-
-
-
-
?
Abz-GFSPFRQ-EDDnp + H2O
Abz-GFSP + FRQ-EDDnp
-
-
-
-
?
Abz-GFSPFRQ-EDDnp + H2O
Abz-GFSP + FRQ-EDDnp
-
-
-
-
?
Abz-GFSQFRQ-EDDnp + H2O
Abz-GFSQ + FRQ-EDDnp
-
-
-
-
?
Abz-GFSQFRQ-EDDnp + H2O
Abz-GFSQ + FRQ-EDDnp
-
-
-
-
?
Abz-GFSRFRQ-EDDnp + H2O
Abz-GFSR + FRQ-EDDnp
-
-
-
-
?
Abz-GFSRFRQ-EDDnp + H2O
Abz-GFSR + FRQ-EDDnp
-
-
-
-
?
Abz-GFSSFRQ-EDDnp + H2O
Abz-GFSS + FRQ-EDDnp
-
-
-
-
?
Abz-GFSSFRQ-EDDnp + H2O
Abz-GFSS + FRQ-EDDnp
-
-
-
-
?
Abz-GFSWFRQ-EDDnp + H2O
Abz-GFSW + FRQ-EDDnp
-
-
-
-
?
Abz-GFSWFRQ-EDDnp + H2O
Abz-GFSW + FRQ-EDDnp
-
-
-
-
?
adrenorphin
peptide fragments
-
-
-
-
?
adrenorphin
peptide fragments
-
-
-
?
Ala-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-Thr-Phe-Thr-Ser-Cys + H2O
?
-
i.e. somatostatin, cleavage sites: Asn5-Phe6, Phe6-Phe7 and Thr10-Phe11
-
-
?
Ala-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-Thr-Phe-Thr-Ser-Cys + H2O
?
-
i.e. somatostatin, cleavage sites: Asn5-Phe6, Phe6-Phe7 and Thr10-Phe11
-
-
?
alpha-neoendorphin + H2O
?
-
-
-
?
alpha-neoendorphin + H2O
?
-
-
-
?
angiotensin I + H2O
?
-
-
-
?
angiotensin I + H2O
?
-
33.5% of the activity with bradykinin
-
?
angiotensin I + H2O
angiotensin-(1-7) + ?
-
-
-
?
angiotensin I + H2O
angiotensin-(1-7) + ?
-
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met + H2O
peptide fragments
-
cleavage sites: Pro4-Gln5, Phe8-Gly9 and Phe7-Phe8
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met + H2O
peptide fragments
-
i.e. substance P, cleavage sites: Gln5-Gln6, Phe7-Phe8, Phe8-Gly9
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met + H2O
peptide fragments
-
i.e. substance P, cleavage sites: Gln5-Gln6, Phe7-Phe8, 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
-
?
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
-
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
-
i.e. bradykinin, cleavage site: Phe5-Ser6
-
-
?
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
-
-
?
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
i.e. angiotensin II, cleavage site: Tyr4-Ile5
-
?
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
i.e. angiotensin II, cleavage site: Tyr4-Ile5
-
?
benzoyl-Gly-Ala-Ala-Gly-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Gly-p-aminobenzoate
-
-
-
?
benzoyl-Gly-Ala-Ala-Gly-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Gly-p-aminobenzoate
-
-
-
?
benzoyl-Gly-Ala-Ala-Leu-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Leu-p-aminobenzoate
-
-
-
?
benzoyl-Gly-Ala-Ala-Leu-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Leu-p-aminobenzoate
-
-
-
-
?
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Phe-p-aminobenzoate
-
-
-
-
?
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Phe-p-aminobenzoate
-
-
-
-
?
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Phe-p-aminobenzoate
-
-
-
-
?
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Phe-p-aminobenzoate
-
-
-
?
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Phe-p-aminobenzoate
-
-
-
?
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Ala-Ala-Phe-p-aminobenzoate
-
-
-
?
benzoyl-Gly-Gly-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Gly-Ala-Phe-p-aminobenzoate
-
-
-
?
benzoyl-Gly-Gly-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Gly-Ala-Phe-p-aminobenzoate
-
-
-
?
benzoyl-Gly-Phe-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly-Phe + Ala-Ala-Phe-p-aminobenzoate
-
-
-
?
benzoyl-Gly-Phe-Ala-Ala-Phe-p-aminobenzoate
benzoyl-Gly-Phe + Ala-Ala-Phe-p-aminobenzoate
-
inactive with benzoyl-Gly-D-Phe-Ala-Ala-Phe-p-aminobenzoate
-
?
benzoyl-Gly-Phe-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Phe-Ala-Phe-p-aminobenzoate
-
-
-
?
benzoyl-Gly-Phe-Ala-Phe-p-aminobenzoate
benzoyl-Gly + Phe-Ala-Phe-p-aminobenzoate
-
-
-
?
beta-neoendorphin + H2O
?
-
-
-
?
beta-neoendorphin + H2O
?
-
-
-
?
bradykinin + H2O
?
-
-
-
?
bradykinin + H2O
?
-
degradation
-
-
?
bradykinin + H2O
?
-
participation of EP24.15 in the metabolism of bradykinin, bradykinin is internalized via the kinin B2 receptor, EP24.15 attenuates maximal kinin2 receptor responsiveness without influencing the potency of bradykinin to stimulate phosphoinositide hydrolysis and intracellular Ca2+ mobilization, overview
-
-
?
bradykinin + H2O
?
-
-
-
-
?
bradykinin + H2O
?
-
-
-
-
?
bradykinin + H2O
?
-
-
-
?
cholecystokinin-8
peptide fragments
-
sulfated
-
-
?
cholecystokinin-8
peptide fragments
-
sulfated
-
-
?
Collagen + H2O
?
-
degradation
-
-
?
Collagen + H2O
?
-
degradation by Pz peptidase A
-
-
?
Collagen + H2O
?
-
Pz peptidase A recognizes collagen-specific tripeptide units, Gly-Pro-Xaa, Pz peptidase A shares common reactions with mammalian thimet oligopeptidase and neurolysin, but has extremely low primary sequence identity to these enzymes
-
-
?
Collagen + H2O
?
-
the enzyme recognizes the specific sequence Gly-Pro-Xaa of in collagen
-
-
?
Collagen + H2O
?
-
degradation by Pz peptidase A
-
-
?
Collagen + H2O
?
-
Pz peptidase A recognizes collagen-specific tripeptide units, Gly-Pro-Xaa, Pz peptidase A shares common reactions with mammalian thimet oligopeptidase and neurolysin, but has extremely low primary sequence identity to these enzymes
-
-
?
Collagen + H2O
?
-
degradation
-
-
?
Collagen + H2O
?
-
the enzyme recognizes the specific sequence Gly-Pro-Xaa of in collagen
-
-
?
corticotropin-like intermediate lobe peptide
peptide fragments
-
-
-
-
?
corticotropin-like intermediate lobe peptide
peptide fragments
-
-
-
-
?
dinitrophenyl-Pro-Leu-Gly-Pro-Trp-D-Lys
dinitrophenyl-Pro-Leu + Gly-Pro-Trp-D-Lys
-
-
-
?
dinitrophenyl-Pro-Leu-Gly-Pro-Trp-D-Lys
dinitrophenyl-Pro-Leu + Gly-Pro-Trp-D-Lys
-
-
-
?
dynorphin 1-8 + H2O
?
-
-
-
?
dynorphin 1-8 + H2O
?
-
-
-
?
gonadotrophin-releasing hormone + H2O
?
-
-
-
-
?
gonadotrophin-releasing hormone + H2O
?
-
-
-
?
gonadotrophin-releasing hormone + H2O
?
-
-
-
-
?
gonadotrophin-releasing hormone + H2O
?
-
-
-
?
gondotropin-releasing hormone + H2O
?
-
-
-
?
gondotropin-releasing hormone + H2O
?
-
-
-
?
neuromedin N + H2O
?
-
degradation
-
-
?
neuromedin N + H2O
?
-
i.e. H-Lys-Ile-Pro-Tyr-Ile-Leu-OH
-
-
?
neuromedin N + H2O
?
-
degradation
-
-
?
neuromedin N + H2O
?
-
i.e. H-Lys-Ile-Pro-Tyr-Ile-Leu-OH
-
-
?
neuromedin N + H2O
?
-
degradation
-
-
?
neuromedin N + H2O
?
-
i.e. H-Lys-Ile-Pro-Tyr-Ile-Leu-OH
-
-
?
neurotensin + H2O
?
-
degradation
-
-
?
neurotensin + H2O
?
-
cleavage of the Arg8-Arg9 bond
-
-
?
neurotensin + H2O
?
-
-
-
-
?
neurotensin + H2O
?
-
-
-
?
neurotensin + H2O
?
-
degradation
-
-
?
neurotensin + H2O
?
-
cleavage of the Arg8-Arg9 bond
-
-
?
neurotensin + H2O
?
-
determination of specific cleavage sites, overview
-
-
?
neurotensin + H2O
?
-
-
-
-
?
neurotensin + H2O
?
-
degradation
-
-
?
neurotensin + H2O
?
-
cleavage of Arg-Arg bonds
-
-
?
neurotensin + H2O
?
-
cleavage of the Arg8-Arg9 bond
-
-
?
neurotensin + H2O
?
-
-
-
-
?
neurotensin + H2O
?
-
cleavage of Arg-Arg bonds
-
-
?
peptides of 9-17 residues generated by proteasomal degradation of casein + H2O
peptides of 6-9 residues
-
-
-
-
?
peptides of 9-17 residues generated by proteasomal degradation of casein + H2O
peptides of 6-9 residues
-
-
-
-
?
pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2 + H2O
pGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly-NH2
-
i.e. luteinizing hormone-releasing hormone
-
-
?
pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2 + H2O
pGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly-NH2
-
i.e. luteinizing hormone-releasing hormone
-
?
pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2 + H2O
pGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly-NH2
-
-
-
?
pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2 + H2O
pGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly-NH2
-
i.e. luteinizing hormone-releasing hormone
-
-
?
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
-
i.e. neurotensin
-
-
?
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
-
-
-
-
?
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
-
i.e. neurotensin
-
-
?
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
-
i.e. neurotensin
-
?
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
-
i.e. neurotensin
-
?
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
-
-
-
-
?
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
-
i.e. neurotensin
-
-
?
phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg
?
-
-
-
-
?
phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg
?
-
-
-
-
?
pyroGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly + H2O
pyroGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly
-
i.e. luteinizing hormone-releasing hormone or LHRH
i.e. luteinizing hormone-releasing hormone(1-5) or LHRH-(1-5)
-
?
pyroGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly + H2O
pyroGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly
-
gonadotropin-releasing hormone, the enzyme degrades gonadotropin-releasing hormone, GnRH, by cleaving the central Tyr5-Gly6 bond
-
-
?
pyroGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly + H2O
pyroGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly
-
i.e. luteinizing hormone-releasing hormone or LHRH-I, EP24.15 that cleaves the hormone at the fifth and sixth bond of the decapeptide (Tyr5-Gly6) to form LHRH-(15)
i.e. luteinizing hormone-releasing hormone(1-5) or LHRH-(1-5)
-
?
somatostatin + H2O
?
-
-
-
?
somatostatin + H2O
?
-
-
-
-
?
tert-butoxycarbonyl-Phe-Ala-Ala-Phe-p-aminobenzoate
tert-butoxycarbonyl-Phe + Ala-Ala-Phe-p-aminobenzoate
-
-
-
?
tert-butoxycarbonyl-Phe-Ala-Ala-Phe-p-aminobenzoate
tert-butoxycarbonyl-Phe + Ala-Ala-Phe-p-aminobenzoate
-
-
-
?
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 A(1-8)
-
-
?
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 A(1-8)
-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln + H2O
?
-
dynorphin 1-17
-
-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln + H2O
?
-
dynorphin 1-17
-
-
?
vasoactive intestinal peptide
peptide fragments
-
-
-
-
?
vasoactive intestinal peptide
peptide fragments
-
-
-
-
?
additional information
?
-
-
cleaves oligopeptides at the Xaa-Gly site in Xaa-Gly-Pro
-
-
?
additional information
?
-
-
no cleavage of denatured collagen, hemoglobin and casein
-
-
?
additional information
?
-
-
cleaves oligopeptides at the Xaa-Gly site in Xaa-Gly-Pro
-
-
?
additional information
?
-
-
no cleavage of denatured collagen, hemoglobin and casein
-
-
?
additional information
?
-
-
the enzyme is active in inactivation of neuropeptides, biological relevance, overview
-
-
?
additional information
?
-
-
no hydrolysis of proteins
-
-
?
additional information
?
-
-
no activity with Gly-Phe-Leu-Gly-Phe-Ile-Gly-Phe-Leu
-
-
?
additional information
?
-
-
proposed role in formation of enkephalins
-
-
?
additional information
?
-
-
enzyme is involved in degradation of proteasomal products of 9-17 residues
-
-
?
additional information
?
-
-
enzyme is involved in degradation of proteasomal products of 9-17 residues. No substrates: proteasomal degradation peptides of 18-24 residues
-
-
?
additional information
?
-
-
the enzyme cleaves several bioactive peptides at sites similar or different from neurolysin, EC 3.4.24.16
-
-
?
additional information
?
-
-
the enzyme is active in inactivation of neuropeptides, biological relevance, overview
-
-
?
additional information
?
-
-
residues E469, M490, H495, and R498 determine the substrate specificity of thimet oligopeptidase different from closely related neurolysin, EC 3.4.24.16
-
-
?
additional information
?
-
-
substrate specificity, no activity with Abz-GFSLFRQ-EDDnp, Abz-GFSPPRQ-EDDnp, and Abz-GFSPWRQ-EDDnp, overview. Importance of His600 for both substrate binding and/or product release from active site, participation of His600 in TOP catalysis, transferring a proton to the newly generated NH2-terminus or helping Tyr605 and/or Tyr612 in the intermediate oxyanion stabilization
-
-
?
additional information
?
-
the enzyme is able to act as a reducing agent in the peroxidase cycle of myoglobin and horseradish peroxidase. The enzyme also prevents the formation of tryptophanyl radical in myoglobin challenged by H2O2
-
-
?
additional information
?
-
-
activity in cytosol may be significant for regulation of major histocompatibility complex class I expression. The enzyme form in the extracellular space is significant for neuropeptide processing
-
?
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
?
-
-
the enzyme is involved in angiogenesis and tumor growth, overview
-
-
?
additional information
?
-
-
substrate and cleavage site specificity, overview, no activity with GFPPFRQ
-
-
?
additional information
?
-
-
degradation of the gonadotropin-releasing hormone by the tissue of the hypothalamo-pituitary axis occurs in a two-step mechanism involving both post-proline cleaving enzyme and the metalloendopeptidase 3.4.24.15
-
-
?
additional information
?
-
-
the enzyme is involved in the dipeptide transport system, transcriptional Pseudomonas dipeptide regulator PA4499, psdR, negatively regulated the peptidase, PA4498, proteomic profiling of wild-type PAO1 and a PA4499 mutant strains, overview
-
-
?
additional information
?
-
-
cleaves preferentially bonds on the carboxyl side of hydrophobic amino acids
-
-
?
additional information
?
-
-
no hydrolysis of Met-enkephalin
-
-
?
additional information
?
-
-
no activity with (o-aminobenzoyl)-LGMISLMKRPPGFSPFRSSRI-NH2
-
?
additional information
?
-
-
no activity with (ortho-aminobenzoyl)-PRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine), (ortho-aminobenzoyl)-KPRRPYILQ-(N-(2,4-dinitrophenyl)ethylenediamine) or (ortho-aminobenzoyl)-ENKPRRPYILQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
?
additional information
?
-
-
proposed role in formation of enkephalins
-
-
?
additional information
?
-
-
enzyme is involved in degradation of proteasomal products of 9-17 residues
-
-
?
additional information
?
-
-
enzyme modulates intracellular, peptidergic signaling cascades through type 2 bradykinin receptor
-
-
?
additional information
?
-
conformational changes due to chemical denaturation are directly correlated with a change in substrate specificity
-
-
?
additional information
?
-
-
enzyme is involved in degradation of proteasomal products of 9-17 residues. No substrates: proteasomal degradation peptides of 18-24 residues
-
-
?
additional information
?
-
-
enzyme oligomerization, induced by S-glutathionylation, has a regulatory function, overview
-
-
?
additional information
?
-
-
cleavage sites of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
identification of intracellular substrates by incubation of HEK-293 cell extract with recombinant enzyme or by overexpression of enzyme in HEK-293 cells. A majority of the potential substrate peptides are 9-11 amino acids in length
-
-
?
additional information
?
-
-
substrate specificity of EP24.15, overview
-
-
?
additional information
?
-
-
phosphorylation of substrates reduces catalytic activity, phosphorylation of competitive inhibitors only alters their Ki-values
-
-
?
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0.014 - 0.037
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH
0.0025
(7-methoxycoumarin-4-yl)acetyl-Gly-Gly-Phe-Ile-Arg-Arg-Ala-Lys-dinitrophenyl
-
recombinant enzyme from E. coli
0.0014
(7-methoxycoumarin-4-yl)acetyl-Gly-Gly-Phe-Leu-Arg-Arg-Ala-Lys-dinitrophenyl
-
recombinant enzyme from E. coli
0.0012 - 0.0057
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
0.0045
(o-aminobenzoyl)-AFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0102
(o-aminobenzoyl)-AKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.003
(o-aminobenzoyl)-DFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0012
(o-aminobenzoyl)-EFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.001
(o-aminobenzoyl)-FFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0042
(o-aminobenzoyl)-GASPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0166
(o-aminobenzoyl)-GDSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0225
(o-aminobenzoyl)-GESPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00071
(o-aminobenzoyl)-GFAPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0068
(o-aminobenzoyl)-GFDPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0052
(o-aminobenzoyl)-GFEPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0014
(o-aminobenzoyl)-GFFPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00072
(o-aminobenzoyl)-GFHPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00099
(o-aminobenzoyl)-GFIPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00038
(o-aminobenzoyl)-GFLPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00027
(o-aminobenzoyl)-GFNPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.006
(o-aminobenzoyl)-GFPPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0149
(o-aminobenzoyl)-GFQPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0053
(o-aminobenzoyl)-GFRPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0012
(o-aminobenzoyl)-GFSAFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0076
(o-aminobenzoyl)-GFSDFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0038
(o-aminobenzoyl)-GFSEFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00069
(o-aminobenzoyl)-GFSFFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0011
(o-aminobenzoyl)-GFSHFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0016
(o-aminobenzoyl)-GFSLFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0016
(o-aminobenzoyl)-GFSNFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.004
(o-aminobenzoyl)-GFSPARQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.037
(o-aminobenzoyl)-GFSPDRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.018
(o-aminobenzoyl)-GFSPERQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.002
(o-aminobenzoyl)-GFSPFAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0139
(o-aminobenzoyl)-GFSPFDQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.119
(o-aminobenzoyl)-GFSPFEQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0019
(o-aminobenzoyl)-GFSPFFQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0126
(o-aminobenzoyl)-GFSPFHQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0017
(o-aminobenzoyl)-GFSPFIQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0044
(o-aminobenzoyl)-GFSPFLQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.131
(o-aminobenzoyl)-GFSPFNQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0203
(o-aminobenzoyl)-GFSPFPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0038
(o-aminobenzoyl)-GFSPFQQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0048
(o-aminobenzoyl)-GFSPFRA-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0012
(o-aminobenzoyl)-GFSPFRE-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00069
(o-aminobenzoyl)-GFSPFRF-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0005
(o-aminobenzoyl)-GFSPFRI-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00057
(o-aminobenzoyl)-GFSPFRL-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0018
(o-aminobenzoyl)-GFSPFRN-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0059
(o-aminobenzoyl)-GFSPFRP-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
0.0022
(o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00019
(o-aminobenzoyl)-GFSPFRR-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0043
(o-aminobenzoyl)-GFSPFRS-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.007
(o-aminobenzoyl)-GFSPFSQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0015
(o-aminobenzoyl)-GFSPHRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0085
(o-aminobenzoyl)-GFSPIRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0045
(o-aminobenzoyl)-GFSPLRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.005
(o-aminobenzoyl)-GFSPNRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0043
(o-aminobenzoyl)-GFSPQRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0018
(o-aminobenzoyl)-GFSPRRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0073
(o-aminobenzoyl)-GFSPSRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0075
(o-aminobenzoyl)-GFSQFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0022
(o-aminobenzoyl)-GFSRFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0037
(o-aminobenzoyl)-GFSSFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0012
(o-aminobenzoyl)-GFSXFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
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
0.0048
(o-aminobenzoyl)-GHSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0028
(o-aminobenzoyl)-GISPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0037
(o-aminobenzoyl)-GLSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0045
(o-aminobenzoyl)-GNSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0037
(o-aminobenzoyl)-GPSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0099
(o-aminobenzoyl)-GQSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0036
(o-aminobenzoyl)-GRSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.006
(o-aminobenzoyl)-GSSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0017
(o-aminobenzoyl)-HFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00016
(o-aminobenzoyl)-IFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.00082
(o-aminobenzoyl)-LFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0071
(o-aminobenzoyl)-NAPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.00078
(o-aminobenzoyl)-NFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.064
(o-aminobenzoyl)-NKARRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.036
(o-aminobenzoyl)-NKPARPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.015
(o-aminobenzoyl)-NKPRAPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.0124
(o-aminobenzoyl)-NKPRRAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.0015
(o-aminobenzoyl)-QFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0015
(o-aminobenzoyl)-RFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.0014
(o-aminobenzoyl)-SFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.021
(ortho-aminobenzoyl)-ENKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.0028
(ortho-aminobenzoyl)-GGFLPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.114
(ortho-aminobenzoyl)-KPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.007
(ortho-aminobenzoyl)-LYENKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.0121
(ortho-aminobenzoyl)-NKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.0137
2,4-dinitrophenyl-Pro-Leu-Gly-Pro-Trp-D-Lys
-
-
0.0015 - 0.0043
2-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
0.0123
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-(N6-(2,4-dinitrophenyl))Lys
-
-
0.0082
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-Lys(2,4-dinitrophenyl)
pH and temperature not specified in the publication
0.009 - 0.0343
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
0.000057 - 0.00127
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin
0.004 - 0.01
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-(2,4-dinitrophenyl)
-
0.00401 - 0.009
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
0.000041 - 0.0021
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
0.0143
Abz-GFSAFRQ-EDDnp
-
pH 7.4, 37°C
0.0012 - 0.0098
Abz-GFSAFRQEDDnp
0.0009
Abz-GFSDFRQ-EDDnp
-
pH 7.4, 37°C
0.0011
Abz-GFSEFRQ-EDDnp
-
pH 7.4, 37°C
0.0021 - 0.0075
Abz-GFSEFRQEDDnp
0.0105
Abz-GFSFFRQ-EDDnp
-
pH 7.4, 37°C
0.0007 - 0.016
Abz-GFSFFRQEDDnp
0.0321
Abz-GFSHFRQ-EDDnp
-
pH 7.4, 37°C
0.0076 - 0.0096
Abz-GFSHFRQEDDnp
0.112
Abz-GFSIFRQ-EDDnp
-
pH 7.4, 37°C
0.0004 - 0.005
Abz-GFSIFRQEDDnp
0.0016 - 0.0102
Abz-GFSLFRQEDDnp
0.0218
Abz-GFSPARQ-EDDnp
-
pH 7.4, 37°C
0.0075
Abz-GFSPDRQ-EDDnp
-
pH 7.4, 37°C
0.0192
Abz-GFSPERQ-EDDnp
-
pH 7.4, 37°C
0.0093
Abz-GFSPFRQ-EDDnp
-
pH 7.4, 37°C
0.0131
Abz-GFSPHRQ-EDDnp
-
pH 7.4, 37°C
0.0062
Abz-GFSPIRQ-EDDnp
-
pH 7.4, 37°C
0.0122
Abz-GFSPLRQ-EDDnp
-
pH 7.4, 37°C
0.0148
Abz-GFSPQRQ-EDDnp
-
pH 7.4, 37°C
0.0213
Abz-GFSPRRQ-EDDnp
-
pH 7.4, 37°C
0.0135
Abz-GFSPSRQ-EDDnp
-
pH 7.4, 37°C
0.0091
Abz-GFSQFRQ-EDDnp
-
pH 7.4, 37°C
0.0012 - 0.0058
Abz-GFSQFRQEDDnp
0.0109
Abz-GFSRFRQ-EDDnp
-
pH 7.4, 37°C
0.0011 - 0.01
Abz-GFSRFRQEDDnp
0.0127
Abz-GFSSFRQ-EDDnp
-
pH 7.4, 37°C
0.0037 - 0.02
Abz-GFSSFRQEDDnp
0.0208
Abz-GFSWFRQ-EDDnp
-
pH 7.4, 37°C
0.0008 - 0.0074
Abz-GFSWFRQEDDnp
0.0009 - 0.011
Abz-GFSyFRQEDDnp
0.067
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
3.1 - 3.45
benzoyl-Gly-Ala-Ala-Gly-p-aminobenzoate
1.54 - 2.5
benzoyl-Gly-Ala-Ala-Leu-p-aminobenzoate
0.058 - 0.83
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
0.37
benzoyl-Gly-Arg-Ala-Ala-Phe-4-aminobenzoate
-
-
-
0.72
benzoyl-Gly-Asp-Ala-Ala-Phe-4-aminobenzoate
-
-
-
1.36 - 2
benzoyl-Gly-Gly-Ala-Phe-p-aminobenzoate
0.24
benzoyl-Gly-Lys-Arg-Ala-Ala-Phe-p-aminobenzoate
-
-
0.16
benzoyl-Gly-Phe-Ala-Ala-Phe-p-aminobenzoate
-
-
0.39 - 0.51
benzoyl-Gly-Phe-Ala-Phe-p-aminobenzoate
0.031
benzoyl-Gly-Phe-Phe-Ala-Ala-Phe-p-aminobenzoate
-
-
0.012 - 0.0161
dinitrophenyl-Pro-Leu-Gly-Pro-Trp-D-Lys
0.048
Gly-Pro-Leu-Gly-Pro-Leu
-
-
0.0149
Gly-Pro-Leu-Gly-Pro-Leu-Gly-Pro-Leu
-
-
0.0135
Gly-Pro-Leu-Gly-Pro-Leu-Gly-Pro-Leu-Gly-Pro-Leu
-
-
0.0154
Gly-Pro-Leu-Gly-Pro-Leu-Gly-Pro-Leu-Gly-Pro-Leu-Gly-Pro-Leu
-
-
0.0026 - 1.64
neurotensin
0.095
pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2
-
-
0.037
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu
-
-
32.5
propionyl-Gly-Ser-Pro-(farnesyl-Cys)-Val-Leu-Met
-
-
0.1 - 0.22
tert-butoxycarbonyl-Phe-Ala-Ala-Phe-p-aminobenzoate
0.06
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile
-
-
0.038
Tyr-Gly-Gly-Phe-Leu-Arg-Lys-Tyr-Pro
-
-
additional information
additional information
-
kinetics of wild-type and mutant TOP
-
0.014
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH
-
mutant Y605FY612F, 23°C, pH 7.8
0.024
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH
-
wild-type, 23°C, pH 7.8
0.034
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH
-
mutant Y612F, 23°C, pH 7.8
0.037
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH
-
mutant Y605F, 23°C, pH 7.8
0.0012
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
wild-type, 23°C, pH 7.8
0.0025
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G599A, 23°C, pH 7.8
0.0026
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G604A, 23°C, pH 7.8
0.0026
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant Y612F, 23°C, pH 7.8
0.0029
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G603A, 23°C, pH 7.8
0.0029
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G603P, 23°C, pH 7.8
0.0031
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant Y605FY612F, 23°C, pH 7.8
0.0042
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant Y605F, 23°C, pH 7.8
0.005
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G611A, 23°C, pH 7.8
0.0057
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G603A/G604A, 23°C, pH 7.8
0.0015
2-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605F
0.0022
2-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.0043
2-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605A
0.009
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
-
-
0.023
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
-
-
0.0343
7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl
-
recombinant enzyme from E. coli
0.000057
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin
pH 7.8, 23°C
0.00013
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin
pH 7.8, 23°C, presence of 1.5 M urea
0.00048
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin
pH 7.8, 23°C, presence of 2.5 M urea
0.00127
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin
pH 7.8, 23°C, presence of 3.5 M urea
0.004
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-(2,4-dinitrophenyl)
pH 7.0, with Ca2+
-
0.0046
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-(2,4-dinitrophenyl)
pH 7.8, wild-type enzyme
-
0.0051
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-(2,4-dinitrophenyl)
pH 7.8, mutant enzyme Y612F
-
0.01
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-(2,4-dinitrophenyl)
pH 7.0, without Ca2+ or at pH 5.8 with or without Ca2+
-
0.00401
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G603A, 23°C, pH 7.8
0.00408
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G599A, 23°C, pH 7.8
0.00543
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G603A/G604A, 23°C, pH 7.8
0.00643
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G603P, 23°C, pH 7.8
0.0067
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G611A, 23°C, pH 7.8
0.00788
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
wild-type, 23°C, pH 7.8
0.0081
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant Y605FY612F, 23°C, pH 7.8
0.0082
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant Y605F, 23°C, pH 7.8
0.00825
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G604A, 23°C, pH 7.8
0.009
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant Y612F, 23°C, pH 7.8
0.000041
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant G603A/G604A, 23°C, pH 7.8
0.000054
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant G603A, 23°C, pH 7.8
0.000057
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
wild-type, 23°C, pH 7.8
0.00008
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant Y605F, 23°C, pH 7.8
0.00009
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant G604A, 23°C, pH 7.8
0.000129
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant G599A, 23°C, pH 7.8
0.000136
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant G611A, 23°C, pH 7.8
0.00051
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant Y605FY612F, 23°C, pH 7.8
0.00057
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant Y612F, 23°C, pH 7.8
0.0021
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant G603P, 23°C, pH 7.8
0.0012
Abz-GFSAFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.0047
Abz-GFSAFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605F
0.0098
Abz-GFSAFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605A
0.0021
Abz-GFSEFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605F
0.003
Abz-GFSEFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605A
0.0075
Abz-GFSEFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.0007
Abz-GFSFFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.0033
Abz-GFSFFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605F
0.016
Abz-GFSFFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605A
0.0076
Abz-GFSHFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.0086
Abz-GFSHFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605F
0.0096
Abz-GFSHFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605A
0.0004
Abz-GFSIFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.0014
Abz-GFSIFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605F
0.005
Abz-GFSIFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605A
0.0016
Abz-GFSLFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.0032
Abz-GFSLFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605F
0.0102
Abz-GFSLFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605A
0.0012
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 Y605F
0.0058
Abz-GFSQFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605A
0.0011
Abz-GFSRFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.0044
Abz-GFSRFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605F
0.01
Abz-GFSRFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605A
0.0037
Abz-GFSSFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.0047
Abz-GFSSFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605F
0.02
Abz-GFSSFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605A
0.0008
Abz-GFSWFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.0015
Abz-GFSWFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605F
0.0074
Abz-GFSWFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605A
0.0009
Abz-GFSyFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.0023
Abz-GFSyFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605F
0.011
Abz-GFSyFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605A
3.1
benzoyl-Gly-Ala-Ala-Gly-p-aminobenzoate
-
-
3.45
benzoyl-Gly-Ala-Ala-Gly-p-aminobenzoate
-
-
1.54
benzoyl-Gly-Ala-Ala-Leu-p-aminobenzoate
-
-
2.5
benzoyl-Gly-Ala-Ala-Leu-p-aminobenzoate
-
-
0.058
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
-
-
0.49
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
-
-
0.83
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
-
-
1.36
benzoyl-Gly-Gly-Ala-Phe-p-aminobenzoate
-
-
2
benzoyl-Gly-Gly-Ala-Phe-p-aminobenzoate
-
-
0.39
benzoyl-Gly-Phe-Ala-Phe-p-aminobenzoate
-
-
0.51
benzoyl-Gly-Phe-Ala-Phe-p-aminobenzoate
-
-
0.012
dinitrophenyl-Pro-Leu-Gly-Pro-Trp-D-Lys
-
-
0.0133
dinitrophenyl-Pro-Leu-Gly-Pro-Trp-D-Lys
-
-
0.0161
dinitrophenyl-Pro-Leu-Gly-Pro-Trp-D-Lys
-
recombinant enzyme from E. coli
0.0026
neurotensin
-
recombinant wild-type enzyme, pH 7.5, 37°C
0.0033
neurotensin
-
recombinant mutant E469R/R498T, pH 7.5, 37°C
0.1
tert-butoxycarbonyl-Phe-Ala-Ala-Phe-p-aminobenzoate
-
-
0.22
tert-butoxycarbonyl-Phe-Ala-Ala-Phe-p-aminobenzoate
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.025 - 11.2
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH
0.00052 - 1.26
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
2.6 - 9.8
(o-aminobenzoyl)-AFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
0.75
(o-aminobenzoyl)-AKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
1 - 4.7
(o-aminobenzoyl)-DFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
0.53 - 6.08
(o-aminobenzoyl)-EFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
1.6
(o-aminobenzoyl)-FFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
2.5
(o-aminobenzoyl)-GASPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
2.2
(o-aminobenzoyl)-GDSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
5.8
(o-aminobenzoyl)-GESPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
5.7
(o-aminobenzoyl)-GFAPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
3.4
(o-aminobenzoyl)-GFDPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
4
(o-aminobenzoyl)-GFEPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
5.3
(o-aminobenzoyl)-GFFPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.89 - 6.08
(o-aminobenzoyl)-GFHPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
4.9
(o-aminobenzoyl)-GFIPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
3
(o-aminobenzoyl)-GFLPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
2.5
(o-aminobenzoyl)-GFNPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
1.6
(o-aminobenzoyl)-GFPPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
1.8
(o-aminobenzoyl)-GFQPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
7.7
(o-aminobenzoyl)-GFRPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
10.2
(o-aminobenzoyl)-GFSAFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
24.7
(o-aminobenzoyl)-GFSDFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
0.7
(o-aminobenzoyl)-GFSEFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
6.7
(o-aminobenzoyl)-GFSFFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
7
(o-aminobenzoyl)-GFSHFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
3.4
(o-aminobenzoyl)-GFSLFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
8.9
(o-aminobenzoyl)-GFSNFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
18.5
(o-aminobenzoyl)-GFSPARQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
8.2 - 8.9
(o-aminobenzoyl)-GFSPDRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
1.5 - 1.8
(o-aminobenzoyl)-GFSPERQ-(N-(2,4-dinitrophenyl)ethylenediamine)
2.3
(o-aminobenzoyl)-GFSPFAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
4
(o-aminobenzoyl)-GFSPFDQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
1.6 - 11.8
(o-aminobenzoyl)-GFSPFEQ-(N-(2,4-dinitrophenyl)ethylenediamine)
1.1
(o-aminobenzoyl)-GFSPFFQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
1.8 - 3
(o-aminobenzoyl)-GFSPFHQ-(N-(2,4-dinitrophenyl)ethylenediamine)
11.1
(o-aminobenzoyl)-GFSPFIQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
3.1
(o-aminobenzoyl)-GFSPFLQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
4.2 - 7.9
(o-aminobenzoyl)-GFSPFNQ-(N-(2,4-dinitrophenyl)ethylenediamine)
7
(o-aminobenzoyl)-GFSPFPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
0.82 - 6.08
(o-aminobenzoyl)-GFSPFQQ-(N-(2,4-dinitrophenyl)ethylenediamine)
17.5
(o-aminobenzoyl)-GFSPFRA-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
3.1
(o-aminobenzoyl)-GFSPFRE-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
7.1
(o-aminobenzoyl)-GFSPFRF-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
3
(o-aminobenzoyl)-GFSPFRI-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
4.8
(o-aminobenzoyl)-GFSPFRL-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
12.3
(o-aminobenzoyl)-GFSPFRN-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
2.6
(o-aminobenzoyl)-GFSPFRP-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
6.3
(o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
0.77 - 6.08
(o-aminobenzoyl)-GFSPFRR-(N-(2,4-dinitrophenyl)ethylenediamine)
4.3
(o-aminobenzoyl)-GFSPFRS-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
1.2 - 1.4
(o-aminobenzoyl)-GFSPFSQ-(N-(2,4-dinitrophenyl)ethylenediamine)
5.3
(o-aminobenzoyl)-GFSPHRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
3.8 - 5.9
(o-aminobenzoyl)-GFSPIRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
0.74 - 6.08
(o-aminobenzoyl)-GFSPLRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
10.1
(o-aminobenzoyl)-GFSPNRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
12.3
(o-aminobenzoyl)-GFSPQRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
2.7
(o-aminobenzoyl)-GFSPRRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
21.5
(o-aminobenzoyl)-GFSPSRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
1.5
(o-aminobenzoyl)-GFSQFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
6.3
(o-aminobenzoyl)-GFSRFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
8.8
(o-aminobenzoyl)-GFSSFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
6.3
(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
0.2 - 0.3
(o-aminobenzoyl)-GGFLRRFQ-(N-(2,4-dinitrophenyl)ethylenediamine)
0.6 - 1.6
(o-aminobenzoyl)-GGFLRRHQ-(N-(2,4-dinitrophenyl)ethylenediamine)
0.1 - 0.7
(o-aminobenzoyl)-GGFLRRIQ-(N-(2,4-dinitrophenyl)ethylenediamine)
0.2 - 0.5
(o-aminobenzoyl)-GGFLRRLQ-(N-(2,4-dinitrophenyl)ethylenediamine)
0.3 - 0.6
(o-aminobenzoyl)-GGFLRRNQ-(N-(2,4-dinitrophenyl)ethylenediamine)
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
0.2 - 0.3
(o-aminobenzoyl)-GGFLRRYQ-(N-(2,4-dinitrophenyl)ethylenediamine)
14.5
(o-aminobenzoyl)-GHSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
8.4
(o-aminobenzoyl)-GISPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
11.5
(o-aminobenzoyl)-GLSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
5.2
(o-aminobenzoyl)-GNSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
11.5
(o-aminobenzoyl)-GPSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
2.9
(o-aminobenzoyl)-GQSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
13.3
(o-aminobenzoyl)-GRSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
3.2
(o-aminobenzoyl)-GSSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
6
(o-aminobenzoyl)-HFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
0.94 - 6.08
(o-aminobenzoyl)-IFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
2.2 - 3.8
(o-aminobenzoyl)-LFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
3.6
(o-aminobenzoyl)-NAPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.75 - 3
(o-aminobenzoyl)-NFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
8
(o-aminobenzoyl)-NKARRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
4.2
(o-aminobenzoyl)-NKPARPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
8.7
(o-aminobenzoyl)-NKPRAPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
5.7
(o-aminobenzoyl)-NKPRRAPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
-
1.1 - 4.7
(o-aminobenzoyl)-QFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
4.3
(o-aminobenzoyl)-RFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
0.67 - 6.08
(o-aminobenzoyl)-SFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
3.2
(ortho-aminobenzoyl)-ENKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
3.7
(ortho-aminobenzoyl)-GGFLPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
3.7
(ortho-aminobenzoyl)-KPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.3
(ortho-aminobenzoyl)-LYENKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
0.7
(ortho-aminobenzoyl)-NKPRRPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C, hydrolysis of R-R bond
1.4 - 6.3
2-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
0.3 - 1.07
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin
0.00037 - 2.44
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
0.027 - 9.9
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenyl
0.1 - 1.34
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
11.1
Abz-GFSAFRQ-EDDnp
-
pH 7.4, 37°C
2.6 - 10.4
Abz-GFSAFRQEDDnp
0.3
Abz-GFSDFRQ-EDDnp
-
pH 7.4, 37°C
1.6
Abz-GFSEFRQ-EDDnp
-
pH 7.4, 37°C
1.5 - 5.3
Abz-GFSEFRQEDDnp
5.9
Abz-GFSFFRQ-EDDnp
-
pH 7.4, 37°C
6.7 - 27.3
Abz-GFSFFRQEDDnp
13.3
Abz-GFSHFRQ-EDDnp
-
pH 7.4, 37°C
1.8 - 24.7
Abz-GFSHFRQEDDnp
0.19
Abz-GFSIFRQ-EDDnp
-
pH 7.4, 37°C
0.001 - 13.6
Abz-GFSIFRQEDDnp
3.4 - 13.6
Abz-GFSLFRQEDDnp
1.7
Abz-GFSPARQ-EDDnp
-
pH 7.4, 37°C
0.03
Abz-GFSPDRQ-EDDnp
-
pH 7.4, 37°C
0.01
Abz-GFSPERQ-EDDnp
-
pH 7.4, 37°C
2.9
Abz-GFSPFRQ-EDDnp
-
pH 7.4, 37°C
0.3
Abz-GFSPHRQ-EDDnp
-
pH 7.4, 37°C
0.04
Abz-GFSPIRQ-EDDnp
-
pH 7.4, 37°C
0.02
Abz-GFSPLRQ-EDDnp
-
pH 7.4, 37°C
0.7
Abz-GFSPQRQ-EDDnp
-
pH 7.4, 37°C
4.5
Abz-GFSPRRQ-EDDnp
-
pH 7.4, 37°C
0.4
Abz-GFSPSRQ-EDDnp
-
pH 7.4, 37°C
7
Abz-GFSQFRQ-EDDnp
-
pH 7.4, 37°C
5.8 - 12.1
Abz-GFSQFRQEDDnp
9.1
Abz-GFSRFRQ-EDDnp
-
pH 7.4, 37°C
9.2
Abz-GFSSFRQ-EDDnp
-
pH 7.4, 37°C
1.5 - 8.8
Abz-GFSSFRQEDDnp
6
Abz-GFSWFRQ-EDDnp
-
pH 7.4, 37°C
0.2 - 9.1
Abz-GFSWFRQEDDnp
6.2 - 20.4
Abz-GFSyFRQEDDnp
33.8
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
5.3
benzoyl-Gly-Ala-Ala-Gly
-
-
1.15
benzoyl-Gly-Ala-Ala-Gly-p-aminobenzoate
-
-
3.1 - 17
benzoyl-Gly-Ala-Ala-Leu-p-aminobenzoate
4.77 - 179
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
5.25
benzoyl-Gly-Arg-Ala-Ala-Phe-4-aminobenzoate
-
-
-
2.2
benzoyl-Gly-Asp-Ala-Ala-Phe-4-aminobenzoate
-
-
-
1.45 - 4.54
benzoyl-Gly-Gly-Ala-Phe-p-aminobenzoate
10.1
benzoyl-Gly-Lys-Arg-Ala-Ala-Phe-p-aminobenzoate
-
-
2.75 - 8.6
benzoyl-Gly-Phe-Ala-Ala-Phe-p-aminobenzoate
19.2
benzoyl-Gly-Phe-Ala-Phe-p-aminobenzoate
-
-
6.2
benzoyl-Gly-Phe-Phe-Ala-Ala-Phe-p-aminobenzoate
-
-
12
pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2
-
-
7.9
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu
-
-
21.5 - 94.1
tert-butoxycarbonyl-Phe-Ala-Ala-Phe-p-aminobenzoate
86.4
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile
-
-
37.9
Tyr-Gly-Gly-Phe-Leu-Arg-Lys-Tyr-Pro
-
-
0.025
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH
-
mutant Y605FY612F, 23°C, pH 7.8
0.061
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH
-
mutant Y612F, 23°C, pH 7.8
1.4
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH
-
mutant Y605F, 23°C, pH 7.8
11.2
(7-methoxycoumarin-4-yl)acetyl-Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-OH
-
wild-type, 23°C, pH 7.8
0.00052
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant Y612F, 23°C, pH 7.8
0.0015
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant Y605FY612F, 23°C, pH 7.8
0.00449
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G603P, 23°C, pH 7.8
0.012
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant Y605F, 23°C, pH 7.8
0.11
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G604A, 23°C, pH 7.8
0.18
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G599A, 23°C, pH 7.8
0.3
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G611A, 23°C, pH 7.8
0.33
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
wild-type, 23°C, pH 7.8
1.22
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G603A/G604A, 23°C, pH 7.8
1.26
(7-methoxycoumarin-4-yl)acetyl-Leu-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Lys(Dnp)-OH
-
mutant G603A, 23°C, pH 7.8
2.6
(o-aminobenzoyl)-AFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
9.8
(o-aminobenzoyl)-AFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
1
(o-aminobenzoyl)-DFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
4.7
(o-aminobenzoyl)-DFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
0.53
(o-aminobenzoyl)-EFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
1.4
(o-aminobenzoyl)-EFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
6.08
(o-aminobenzoyl)-EFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
0.89
(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
8.2
(o-aminobenzoyl)-GFSPDRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
8.9
(o-aminobenzoyl)-GFSPDRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
1.5
(o-aminobenzoyl)-GFSPERQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
1.8
(o-aminobenzoyl)-GFSPERQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
1.6
(o-aminobenzoyl)-GFSPFEQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
11.8
(o-aminobenzoyl)-GFSPFEQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
1.8
(o-aminobenzoyl)-GFSPFHQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
3
(o-aminobenzoyl)-GFSPFHQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
4.2
(o-aminobenzoyl)-GFSPFNQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
7.9
(o-aminobenzoyl)-GFSPFNQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
0.82
(o-aminobenzoyl)-GFSPFQQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
2.3
(o-aminobenzoyl)-GFSPFQQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
6.08
(o-aminobenzoyl)-GFSPFQQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
6.3
(o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
6.3
(o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
6.3
(o-aminobenzoyl)-GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
0.77
(o-aminobenzoyl)-GFSPFRR-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
6.08
(o-aminobenzoyl)-GFSPFRR-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C
1.2
(o-aminobenzoyl)-GFSPFSQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
1.4
(o-aminobenzoyl)-GFSPFSQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
3.8
(o-aminobenzoyl)-GFSPIRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
5.9
(o-aminobenzoyl)-GFSPIRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
0.74
(o-aminobenzoyl)-GFSPLRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X bond
4.2
(o-aminobenzoyl)-GFSPLRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
6.08
(o-aminobenzoyl)-GFSPLRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-X 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
0.94
(o-aminobenzoyl)-IFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
1.5
(o-aminobenzoyl)-IFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
6.08
(o-aminobenzoyl)-IFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
2.2
(o-aminobenzoyl)-LFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
3.8
(o-aminobenzoyl)-LFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
0.75
(o-aminobenzoyl)-NFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
3
(o-aminobenzoyl)-NFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
1.1
(o-aminobenzoyl)-QFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
4.7
(o-aminobenzoyl)-QFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of P-F bond
0.67
(o-aminobenzoyl)-SFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 7.4, 37°C, cleavage of F-S bond
4.1
(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 F-S bond
1.4
2-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605F
4.7
2-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605A
6.3
2-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.3
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin
pH 7.8, 23°C
0.72
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin
pH 7.8, 23°C, presence of 1.5 M urea
0.91
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin
pH 7.8, 23°C, presence of 2.5 M urea
1.07
7-methoxycoumarin-4-acetyl-(L-Ala-L-Lys(2,4-dinitrophenyl))-bradykinin
pH 7.8, 23°C, presence of 3.5 M urea
0.00037
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant Y612F, 23°C, pH 7.8
0.0023
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant Y605FY612F, 23°C, pH 7.8
0.0026
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G603P, 23°C, pH 7.8
0.0086
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant Y605F, 23°C, pH 7.8
0.03
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G599A, 23°C, pH 7.8
0.11
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G604A, 23°C, pH 7.8
0.193
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G611A, 23°C, pH 7.8
0.44
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
wild-type, 23°C, pH 7.8
2.32
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G603A, 23°C, pH 7.8
2.44
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenol
-
mutant G603A/G604A, 23°C, pH 7.8
0.027
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenyl
pH 7.8, mutant enzyme Y612F
9.9
7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitrophenyl
pH 7.8, wild-type enzyme
0.1
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant Y605FY612F, 23°C, pH 7.8
0.18
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant G603P, 23°C, pH 7.8
0.27
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant G603A/G604A, 23°C, pH 7.8
0.28
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant G603A, 23°C, pH 7.8
0.3
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
wild-type, 23°C, pH 7.8
0.34
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant Y605F, 23°C, pH 7.8
0.53
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant G604A, 23°C, pH 7.8
0.75
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant Y612F, 23°C, pH 7.8
0.86
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant G599A, 23°C, pH 7.8
1.34
7-methoxycoumarin-4-acetyl-[Ala7, Lys(dinitrophenol)9]-bradykinin
-
mutant G611A, 23°C, pH 7.8
2.6
Abz-GFSAFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605F
10.2
Abz-GFSAFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
10.4
Abz-GFSAFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605A
1.5
Abz-GFSEFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
3.2
Abz-GFSEFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605F
5.3
Abz-GFSEFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605A
6.7
Abz-GFSFFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
12.7
Abz-GFSFFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605A
27.3
Abz-GFSFFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605F
1.8
Abz-GFSHFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605A
15.1
Abz-GFSHFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605F
24.7
Abz-GFSHFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.001
Abz-GFSIFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
5
Abz-GFSIFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605A
13.6
Abz-GFSIFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605F
3.4
Abz-GFSLFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
7
Abz-GFSLFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605A
13.6
Abz-GFSLFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605F
5.8
Abz-GFSQFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605A
6.3
Abz-GFSQFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
12.1
Abz-GFSQFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605F
0.6
Abz-GFSRFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605A
1.5
Abz-GFSRFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605F
7
Abz-GFSRFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
1.5
Abz-GFSSFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605A
1.7
Abz-GFSSFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605F
8.8
Abz-GFSSFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
0.2
Abz-GFSWFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605A
2.7
Abz-GFSWFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
9.1
Abz-GFSWFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605F
6.2
Abz-GFSyFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme
6.4
Abz-GFSyFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605F
20.4
Abz-GFSyFRQEDDnp
-
pH 7.4, 37°C, recombinant GST-tagged mutant Y605A
3.1
benzoyl-Gly-Ala-Ala-Leu-p-aminobenzoate
-
-
17
benzoyl-Gly-Ala-Ala-Leu-p-aminobenzoate
-
-
4.77
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
-
-
48.3
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
-
-
179
benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate
-
-
1.45
benzoyl-Gly-Gly-Ala-Phe-p-aminobenzoate
-
-
4.54
benzoyl-Gly-Gly-Ala-Phe-p-aminobenzoate
-
-
2.75
benzoyl-Gly-Phe-Ala-Ala-Phe-p-aminobenzoate
-
-
8.6
benzoyl-Gly-Phe-Ala-Ala-Phe-p-aminobenzoate
-
-
2.3
neurotensin
-
recombinant wild-type enzyme, pH 7.5, 37°C
4.2
neurotensin
-
recombinant mutant E469R/R498T, pH 7.5, 37°C
21.5
tert-butoxycarbonyl-Phe-Ala-Ala-Phe-p-aminobenzoate
-
-
94.1
tert-butoxycarbonyl-Phe-Ala-Ala-Phe-p-aminobenzoate
-
-
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Dahms, P.; Mentlein, R.
Purification of the main somatostatin-degrading proteases from rat and pig brains, their action on other neuropeptides, and their identification as endopeptidases 24.15 and 24.16
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Rattus norvegicus, Sus scrofa
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Thompson, A.; Grueninger-Leitch, F.; Huber, G.; Malherbe, P.
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1997
Homo sapiens
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Chicken liver Pz-peptidase, a thiol-dependent metallo-endopeptidase
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McKie, N.; Dando, P.M.; Brown, M.A.; Barrett, A.J.
Rat thimet oligopeptidase: large-scale expression in Escherichia coli and characterization of the recombinant enzyme
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Rattus norvegicus
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Thiol-dependent metallo-endopeptidase characteristics of Pz-peptidase in rat and rabbit
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Thimet oligopeptidase specificity: evidence of preferential cleavage near the C-terminus and product inhibition from kinetic analysis of peptide hydrolysis
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Homo sapiens
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Orlowski, M.; Reznik, S.; Ayala, J.; Pierotti, A.R.
Endopeptidase 24.15 from rat testes. Isolation of the enzyme and its specificity toward synthetic and natural peptides, including enkephalin-containing peptides
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Rattus norvegicus
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Isolation and characterization of Pz-peptidase from Bacillus licheniformis N22
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Bacillus licheniformis, Bacillus licheniformis N22
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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
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Sus scrofa
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Proteolytic processing of farnesylated peptides: assay and partial purification from pig brain membranes of an endopeptidase which has the characteristics of E.C. 3.4.24.15
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1994
Sus scrofa
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Thimet oligopeptidase and oligopeptidase M or neurolysin
Methods Enzymol.
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Homo sapiens, Rattus norvegicus
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Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15 [published erratum appears in Biochemistry 1994 Jan 18;33(2):622]
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Rattus norvegicus
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Smith, A.; Tetaz, T.; Roberts, J.L.; Glucksman, M.; Clarke, I.J.; Lew, R.A.
The role of EC 3.4.24.15 in the post-secretory regulation of peptide signals
Biochimie
76
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1994
Ovis aries
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Lessley, B.A.; Garner, D.L.
Purification and characterization of Pz-peptidase B, a neutral metalloendopeptidase from bovine spermatozoa
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43
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1990
Bos taurus
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Orlowski, M.; Michaud, C.; Chu, T.G.
A soluble metalloendopeptidase from rat brain. Purification of the enzyme and determination of specificity with synthetic and natural peptides
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1983
Rattus norvegicus
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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)
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292
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Rattus norvegicus
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Molecular and immunochemical evidences demonstrate that endooligopeptidase a is the predominant cytosolic oligopeptidase of rabbit brain
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269
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2000
Oryctolagus cuniculus
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Development and characterization of novel potent and stable inhibitors of endopeptidase EC 3.4.24.15
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-
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Regulation of cell-surface major histocompatibility complex class I expression by the endopeptidase EC3.4.24.15 (thimet oligopeptidase)
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Mus musculus
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Substrate specificity characterization of recombinant metallo oligo-peptidases thimet oligopeptidase and neurolysin
Biochemistry
40
4417-4425
2001
Rattus norvegicus
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Steer, D.; Lew, R.; Perlmutter, P.; Smith, A.I.; Aguilar, M.I.
Inhibitors of metalloendopeptidase EC 3.4.24.15 and EC 3.4.24.16 stabilized against proteolysis by the incorporation of beta-amino acids
Biochemistry
41
10819-10826
2002
Rattus norvegicus
brenda
Portaro, F.C.; Hayashi, M.A.; Silva, C.L.; de Camargo, A.C.
Free ATP inhibits thimet oligopeptidase (EC 3.4.24.15) activity, induces autophosphorylation in vitro, and controls oligopeptide degradation in macrophage
Eur. J. Biochem.
268
887-894
2001
Rattus norvegicus
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Temperature and salts effects on the peptidase activities of the recombinant metallooligopeptidases neurolysin and thimet oligopeptidase
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269
4326-4334
2002
Sus scrofa
brenda
Lew, R.A.; Boulos, E.; Stewart, K.M.; Perlmutter, P.; Harte, M.F.; Bond, S.; Reeve, S.B.; Norman, M.U.; Lew, M.J.; Aguilar, M.I.; Smith, I.
Substrate analogues incorporating b-amino acids: potential application for peptidase inhibition
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2001
Rattus norvegicus
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Sigman, J.A.; Edwards, S.R.; Pabon, A.; Glucksman, M.J.; Wolfson, A.J.
pH dependence studies provide insight into the structure and mechanism of thimet oligopeptidase (EC 3.4.24.15)
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545
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2003
Rattus norvegicus (P24155)
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Saric, T.; Beninga, J.; Graef, C.I.; Akopian, T.N.; Rock, K.L.; Goldberg, A.L.
Major histocompatibility complex class I-presented antigenic peptides are degraded in cytosolic extracts primarily by thimet oligopeptidase
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276
36474-36481
2001
Homo sapiens
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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
Ray, K.; Hines, C.S.; Coll-Rodriguez, J.; Rodgers, D.W.
Crystal structure of human thimet oligopeptidase provides insight into substrate recognition, regulation, and localization
J. Biol. Chem.
279
20480-20489
2004
Homo sapiens
brenda
Molina, H.M.; Carmona, A.K.; Kouyoumdjian, M.; Borges, D.R.
Thimet oligopeptidase EC 3.4.24.15 is a major liver kininase
Life Sci.
67
509-520
2000
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
Sus scrofa
brenda
Sigman, J.A.; Patwa, T.H.; Tablante, A.V.; Joseph, C.D.; Glucksman, M.J.; Wolfson, A.J.
Flexibility in substrate recognition by thimet oligopeptidase as revealed by denaturation studies
Biochem. J.
388
255-261
2005
Rattus norvegicus (P24155)
brenda
Shivakumar, B.R.; Wang, Z.; Hammond, T.G.; Harris, R.C.
EP24.15 interacts with the angiotensin II type I receptor and bradykinin B2 receptor
Cell Biochem. Funct.
23
195-204
2005
Homo sapiens
brenda
Dubois, V.; Nieder, M.; Collot, F.; Negrouk, A.; Nguyen, T.T.; Gangwar, S.; Reitz, B.; Wattiez, R.; Dasnois, L.; Trouet, A.
Thimet oligopeptidase (EC 3.4.24.15) activates CPI-0004Na, an extracellularly tumour-activated prodrug of doxorubicin
Eur. J. Cancer
42
3049-3056
2006
Homo sapiens
brenda
Oliveira, V.; Garrido, P.A.; Rodrigues, C.C.; Colquhoun, A.; Castro, L.M.; Almeida, P.C.; Shida, C.S.; Juliano, M.A.; Juliano, L.; Camargo, A.C.; Hyslop, S.; Roberts, J.L.; Grum-Tokars, V.; Glucksman, M.J.; Ferro, E.S.
Calcium modulates endopeptidase 24.15 (EC 3.4.24.15) membrane association, secondary structure and substrate specificity
FEBS J.
272
2978-2992
2005
Rattus norvegicus
brenda
Saric, T.; Graef, C.I.; Goldberg, A.L.
Pathway for degradation of peptides generated by proteasomes: a key role for thimet oligopeptidase and other metallopeptidases
J. Biol. Chem.
279
46723-46732
2004
Homo sapiens, Rattus norvegicus
brenda
Jeske, N.A.; Glucksman, M.J.; Roberts, J.L.
Metalloendopeptidase EC3.4.24.15 is constitutively released from the exofacial leaflet of lipid rafts in GT1-7 cells
J. Neurochem.
90
819-828
2004
Mus musculus
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
Ahmed, M.M.; Arif, M.; Chikuma, T.; Kato, T.
Pentylenetetrazol-induced seizures affect the levels of prolyl oligopeptidase, thimet oligopeptidase and glial proteins in rat brain regions, and attenuation by MK-801 pretreatment
Neurochem. Int.
47
248-259
2005
Rattus norvegicus
brenda
Kawasaki, A.; Nakano, H.; Tsujimoto, Y.; Matsui, H.; Shimizu, T.; Nakatsu, T.; Kato, H.; Watanabe, K.
Crystallization and preliminary X-ray crystallographic studies of Pz peptidase A from Geobacillus collagenovorans MO-1
Acta Crystallogr. Sect. F
63
142-144
2007
Geobacillus sp., Geobacillus sp. MO-1
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
Sugihara, Y.; Kawasaki, A.; Tsujimoto, Y.; Matsui, H.; Watanabe, K.
Potencies of phosphine peptide inhibitors of mammalian thimet oligopeptidase and neurolysin on two bacterial pz peptidases
Biosci. Biotechnol. Biochem.
71
594-597
2007
Geobacillus sp., Geobacillus sp. MO-1
brenda
Demasi, M.; Piassa Filho, G.M.; Castro, L.M.; Ferreira, J.C.; Rioli, V.; Ferro, E.S.
Oligomerization of the cysteinyl-rich oligopeptidase EP24.15 is triggered by S-glutathionylation
Free Radic. Biol. Med.
44
1180-1190
2008
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
Homo sapiens
brenda
Sanden, C.; Enquist, J.; Bengtson, S.H.; Herwald, H.; Leeb-Lundberg, F.L.
Kinin B2 receptor-mediated bradykinin internalization and metalloendopeptidase EP24.15-dependent intracellular bradykinin degradation
J. Pharmacol. Exp. Ther.
326
24-32
2008
Homo sapiens
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
Kiely, P.D.; O'Callaghan, J.; Abbas, A.; O'Gara, F.
Genetic analysis of genes involved in dipeptide metabolism and cytotoxicity in Pseudomonas aeruginosa PAO1
Microbiology
154
2209-2218
2008
Pseudomonas aeruginosa
brenda
Bruce, L.A.; Sigman, J.A.; Randall, D.; Rodriguez, S.; Song, M.M.; Dai, Y.; Elmore, D.E.; Pabon, A.; Glucksman, M.J.; Wolfson, A.J.
Hydrogen bond residue positioning in the 599-611 loop of thimet oligopeptidase is required for substrate selection
FEBS J.
275
5607-5617
2008
Rattus norvegicus
brenda
Berti, D.A.; Morano, C.; Russo, L.C.; Castro, L.M.; Cunha, F.M.; Zhang, X.; Sironi, J.; Klitzke, C.F.; Ferro, E.S.; Fricker, L.D.
Analysis of intracellular substrates and products of thimet oligopeptidase (EC 3.4.24.15) in human embryonic kidney 293 cells
J. Biol. Chem.
284
14105-14116
2009
Rattus norvegicus
brenda
Pereira, F.M.; Elias, C.G.; dAvila-Levy, C.M.; Branquinha, M.H.; Santos, A.L.
Cysteine peptidases in Herpetomonas samuelpessoai are modulated by temperature and dimethylsulfoxide-triggered differentiation
Parasitology
136
45-54
2009
Herpetomonas pessoai
brenda
Machado, M.F.; Marcondes, M.F.; Rioli, V.; Ferro, E.S.; Juliano, M.A.; Juliano, L.; Oliveira, V.
Catalytic properties of thimet oligopeptidase H600A mutant
Biochem. Biophys. Res. Commun.
394
429-433
2010
Homo sapiens
brenda
Crack, P.J.; Wu, T.J.; Cummins, P.M.; Ferro, E.S.; Tullai, J.W.; Glucksman, M.J.; Roberts, J.L.
The association of metalloendopeptidase EC 3.4.24.15 at the extracellular surface of the AtT-20 cell plasma membrane
Brain Res.
835
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1999
Mus musculus
brenda
Wu, T.J.; Mani, S.K.; Glucksman, M.J.; Roberts, J.L.
Stimulation of luteinizing hormone-releasing hormone (LHRH) gene expression in GT1-7 cells by its metabolite, LHRH-(1-5)
Endocrinology
146
280-286
2005
Mus musculus
brenda
Russo, L.C.; Goni, C.N.; Castro, L.M.; Asega, A.F.; Camargo, A.C.; Trujillo, C.A.; Ulrich, H.; Glucksman, M.J.; Scavone, C.; Ferro, E.S.
Interaction with calmodulin is important for the secretion of thimet oligopeptidase following stimulation
FEBS J.
276
4358-4371
2009
Homo sapiens, Mus musculus
brenda
Cyr, N.E.; Kua, L.H.; Bruce, L.A.; Chadwick, J.G.; Tetel, M.J.; Wolfson, A.J.
Nuclear thimet oligopeptidase is coexpressed with oestrogen receptor alpha in hypothalamic cells and regulated by oestradiol in female mice
J. Neuroendocrinol.
22
936-943
2010
Mus musculus, Mus musculus C57/BL6J
brenda
Wu, T.J.; Pierotti, A.R.; Jakubowski, M.; Sheward, W.J.; Glucksman, M.J.; Smith, A.I.; King, J.C.; Fink, G.; Roberts, J.L.
Endopeptidase EC 3.4.24.15 presence in the rat median eminence and hypophysial portal blood and its modulation of the luteinizing hormone surge
J. Neuroendocrinol.
9
813-822
1997
Rattus norvegicus
brenda
Cleverly, K.; Wu, T.J.
Is the metalloendopeptidase EC 3.4.24.15 (EP24.15), the enzyme that cleaves luteinizing hormone-releasing hormone (LHRH), an activating enzyme?
Reproduction
139
319-330
2010
Rattus norvegicus
brenda
Kawasaki, A.; Nakano, H.; Hosokawa, A.; Nakatsu, T.; Kato, H.; Watanabe, K.
The exquisite structure and reaction mechanism of bacterial Pz-peptidase A toward collagenous peptides: X-ray crystallographic structure analysis of PZ-peptidase a reveals differences from mammalian thimet oligopeptidase
J. Biol. Chem.
285
34972-34980
2010
Geobacillus sp. (Q4W803), Geobacillus sp. MO-1 (Q4W803)
brenda
Kessler, J.H.; Khan, S.; Seifert, U.; Le Gall, S.; Chow, K.M.; Paschen, A.; Bres-Vloemans, S.A.; de Ru, A.; van Montfoort, N.; Franken, K.L.; Benckhuijsen, W.E.; Brooks, J.M.; van Hall, T.; Ray, K.; Mulder, A.; Doxiadis, I.I.; van Swieten, P.F.; Overkleeft, H.S.; Prat, A.; Tomkinson, B.; Neefjes, J.; Klo, K.l.o.e.
Antigen processing by nardilysin and thimet oligopeptidase generates cytotoxic T cell epitopes
Nat. Immunol.
12
45-53
2011
Homo sapiens
brenda
Nakano, H.; Hosokawa, A.; Tagawa, R.; Inaka, K.; Ohta, K.; Nakatsu, T.; Kato, H.; Watanabe, K.
Crystallization and preliminary X-ray crystallographic analysis of Pz peptidase B from Geobacillus collagenovorans MO-1
Acta Crystallogr. Sect. F
68
757-759
2012
Geobacillus sp. (Q4W802), Geobacillus sp. (Q4W803), Geobacillus sp. MO-1 (Q4W802), Geobacillus sp. MO-1 (Q4W803)
brenda
Dalio, F.M.; Visniauskas, B.; Bicocchi, E.S.; Perry, J.C.; Freua, R.; Gesteira, T.F.; Nader, H.B.; Machado, M.F.; Tufik, S.; Ferro, E.S.; Andersen, M.L.; Toledo, C.A.; Chagas, J.R.; Oliveira, V.
Acute cocaine treatment increases thimet oligopeptidase in the striatum of rat brain
Biochem. Biophys. Res. Commun.
419
724-727
2012
Rattus norvegicus (P24155), Rattus norvegicus Wistar (P24155)
brenda
Guinan, A.F.; Rochfort, K.D.; Fitzpatrick, P.A.; Walsh, T.G.; Pierotti, A.R.; Phelan, S.; Murphy, R.P.; Cummins, P.M.
Shear stress is a positive regulator of thimet oligopeptidase (EC3.4.24.15) in vascular endothelial cells: consequences for MHC1 levels
Cardiovasc. Res.
99
545-554
2013
Homo sapiens (P52888), Bos taurus (Q1JPJ8)
brenda
Simoes, P.S.; Visniauskas, B.; Perosa, S.R.; Yacubian, E.M.; Centeno, R.; Canzian, M.; Lopes-Cendes, I.; Maurer Morelli, C.V.; Carrete, H.; Cavalheiro, E.A.; Tufik, S.; Chagas, J.R.; Mazzacoratti, M.d.a..G.
Expression and activity of thimet oligopeptidase (TOP) are modified in the hippocampus of subjects with temporal lobe epilepsy (TLE)
Epilepsia
55
754-762
2014
Rattus norvegicus (P24155), Homo sapiens (P52888), Homo sapiens
brenda
Pereira, M.G.; Souza, L.L.; Becari, C.; Duarte, D.A.; Camacho, F.R.; Oliveira, J.A.; Gomes, M.D.; Oliveira, E.B.; Salgado, M.C.; Garcia-Cairasco, N.; Costa-Neto, C.M.
Angiotensin II-independent angiotensin-(1-7) formation in rat hippocampus: involvement of thimet oligopeptidase
Hypertension
62
879-885
2013
Rattus norvegicus (P24155), Rattus norvegicus Wistar (P24155)
brenda
Ferreira, J.C.; Icimoto, M.Y.; Marcondes, M.F.; Oliveira, V.; Nascimento, O.R.; Nantes, I.L.
Recycling of the high valence States of heme proteins by cysteine residues of THIMET-oligopeptidase
PLoS ONE
8
e79102
2013
Homo sapiens (P52888)
brenda
Santos, N.B.; Franco, R.D.; Camarini, R.; Munhoz, C.D.; Eichler, R.A.S.; Gewehr, M.C.F.; Reckziegel, P.; Llanos, R.P.; Dale, C.S.; Silva, V.R.O.D.; Borges, V.F.; Lima, B.H.F.; Cunha, F.Q.; Visniauskas, B.; Chagas, J.R.; Tufik, S.; Peres, F.F.; Abilio, V.C.; Florio, J.C.; Iwai, L.K.; Rioli, V.; Presoto, B.C.; Guimaraes, A.O.; Pesquero, J.B.; Bader, M.; Castro, L.M.; Ferro, E.S.
Thimet oligopeptidase (EC 3.4.24.15) key functions suggested by knockout mice phenotype characterization
Biomolecules
9
382
2019
Mus musculus (Q8C1A5), Mus musculus C57BL/6 (Q8C1A5)
brenda
Icimoto, M.Y.; Ferreira, J.C.; Yokomizo, C.H.; Bim, L.V.; Marem, A.; Gilio, J.M.; Oliveira, V.; Nantes, I.L.
Redox modulation of thimet oligopeptidase activity by hydrogen peroxide
FEBS Open Bio
7
1037-1050
2017
Rattus norvegicus (P24155), Homo sapiens (P52888), Homo sapiens
brenda
Westlake, T.J.; Ricci, W.A.; Popescu, G.V.; Popescu, S.C.
Dimerization and thiol sensitivity of the salicylic acid binding thimet oligopeptidases TOP1 and TOP2 define their functions in redox-sensitive cellular pathways
Front. Plant Sci.
6
327
2015
Arabidopsis thaliana, Arabidopsis thaliana (A0A1R7T3A4)
brenda