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2-aminobenzoic acid-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoic acid-Gly-Phe-Ser-Pro-Phe-Arg + Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-MISLMKRPPGFSPFRSSRI-NH2 + H2O
2-aminobenzoyl-MISLMK + RPPGFSPFRSSRI-NH2
-
-
-
-
?
Ac-AGLTR-4-nitroanilide + H2O
Ac-AGLTR + 4-nitroaniline
-
chromogenic substrate based on the C1s cleavage site in complement component C4
-
?
Ac-Phe-Arg-4-nitroanilide
Ac-Phe-Arg + 4-nitroaniline
-
synthetic fluorogenic substrate
-
?
acetyl-Phe-Arg-4-nitroanilide + H2O
?
-
-
-
-
?
apelin-17 + H2O
KFR + ?
-
the enzyme cleaves the first three N-terminal amino acids (KFR) of apelin-17
-
-
?
benzoyl-Pro-Phe-Arg-4-nitroanilide + H2O
benzoyl-Pro-Phe-Arg + 4-nitroaniline
-
-
-
ir
complement component C4 + H2O
?
-
substrate is only cleaved in vitro, not in vivo
-
?
D-butyl-cyclohexylalanine-arginine-4-nitroanilide + H2O
D-butyl-cyclohexylalanine-arginine + 4-nitroaniline
-
-
-
?
D-Phe-Phe-Arg-4-methylcoumarin 7-amide
D-Phe-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
D-Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
D-Pro-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
D-Pro-Phe-Arg-p-nitroanilide + H2O
D-Pro-Phe-Arg + p-nitroaniline
-
-
-
-
?
D-Val-Leu-Arg-4-nitroanilide + H2O
D-Val-Leu-Arg + 4-nitroaniline
-
-
-
-
?
factor B + H2O
factor Bb + ?
-
-
-
-
?
factor FXII + H2O
activated factor XII + ?
cleavage between Arg and Val
-
-
?
factor H + H2O
?
-
-
-
-
?
factor X + H2O
factor XIIa + ?
-
-
-
-
?
factor XI + H2O
activated factor XI + ?
factor XII + H2O
activated factor XII
factor XII + H2O
activated factor XII + ?
factor XII + H2O
factor XIIa + ?
-
-
-
-
?
factor XII-2 + H2O
activated factor XII-2 + H2O
-
-
-
?
Glu-Pro-Arg-4-nitroanilide + H2O
Glu-Pro-Arg + 4-nitroaniline
-
-
-
?
H-D-Pro-Phe-Arg-4-nitroanilide + H2O
?
-
i.e. S2302, a chromogenic substrate
-
-
?
high molecular weight kininogen + H2O
bradykinin + fragments of kininogen
high-molecular-weight kininogen + H2O
bradykinin + fragments of kininogen
high-molecular-weight kininogen + H2O
high-molecular-weight kinin + bradykinin
ISLMKRPPGFSPFRSSR + H2O
ISLMKR + RPPGFSPFR + SSR
-
RPPGFSPFR is bradykinin, synthetic peptide containing the internal kinin sequence, 2 cleavage sites, the C-terminal one being preferred
-
?
kininogen + H2O
bradykinin + ?
kininogen + H2O
bradykinin + fragment of kininogen
kininogen + H2O
bradykinin + fragments of kininogen
kininogen + H2O
heavy chain of kininogen + light chain of kininogen + bradykinin
-
high molecular weight substrate, serine protease
bradykinin is an inflammatory peptide
ir
kininogen + H2O
heavy chain of kininogen + modified light chain of kininogen + bradykinin
-
high molecular weight substrate, serine protease
MW of products: 63 kDa, 45 kDa, and 13 kDa, respectively
?
low-molecular-weight kininogen + H2O
low-molecular-weight kinin + kallidin
-
-
kallidin is Lys-bradykinin or Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
?
modified kininogen + H2O
bradykinin + fragments of kininogen
N-acetyl-Phe-Arg-4-nitroanilide + H2O
N-acetyl-Phe-Arg + 4-nitroaniline
-
-
-
-
?
N-benzoyl-Phe-Val-Arg-4-nitroanilide + H2O
N-benzoyl-Phe-Val-Arg + 4-nitroaniline
-
-
-
-
?
N-benzoyl-Pro-Phe-Arg-4-nitroanilide
N-benzoyl-Pro-Phe-Arg + 4-nitroaniline
-
-
-
-
?
N-benzyloxycarbonyl-Ala-Lys-Arg-4-methylcoumarin 7-amide
N-benzyloxycarbonyl-Ala-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-butyl-(R)-cyclohexylalanyl-L-Arg-p-nitroanilide + H2O
N-butyl-(R)-cyclohexylalanyl-L-Arg + p-nitroaniline
i.e. Pefachrome PK
-
-
?
Nalpha-Benzoyl-L-Arg ethyl ester + H2O
Nalpha-Benzoyl-L-Arg + ethanol
Nalpha-toluenesulfonyl-L-arginine methyl ester + H2O
Nalpha-toluenesulfonyl-L-arginine + methanol
neuropeptide Y3-36 + H2O
neuropeptide Y3-35 + L-tyrosine
-
optimal kallikrein concentration is 5 microg/ml, cleavage of around 70% of neuropeptide Y3-36. Higher concentrations of kallikrein conversely results in a decrease of NPY3-35 levels without an increase of neuropeptide Y3-36 levels, suggesting that high concentrations of kallikrein enable additional and nonspecific neuropeptide Y cleavages
-
-
?
o-aminobenzoyl-FSAPMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSAPMK + RLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
-
18% of product formed, identification by mass spectroscopy
?
o-aminobenzoyl-FSAPMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSAPMKR + LTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
-
82% of product formed, identification by mass spectroscopy
?
o-aminobenzoyl-FSQAMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQAMK + RLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
-
35% of product formed, identification by mass spectroscopy
?
o-aminobenzoyl-FSQAMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQAMKR + LTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
-
65% of product formed, identification by mass spectroscopy
?
o-aminobenzoyl-FSQFMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQFMK + RLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
-
71% of product formed, identification by mass spectroscopy
?
o-aminobenzoyl-FSQFMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQFMKR + LTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
-
29% of product formed, identification by mass spectroscopy
?
o-aminobenzoyl-FSQGMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQGMK + RLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
-
52% of product formed, identification by mass spectroscopy
?
o-aminobenzoyl-FSQGMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQGMKR + LTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
-
48% of product formed, identification by mass spectroscopy
?
o-aminobenzoyl-FSQPAKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQPAK + RLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
-
28% of product formed, identification by mass spectroscopy
?
o-aminobenzoyl-FSQPAKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQPAKR + LTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
-
72% of product formed, identification by mass spectroscopy
?
o-aminobenzoyl-FSQPMARLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQPMAR + LTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
-
identification by mass spectroscopy
?
o-aminobenzoyl-FSQPMKALTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQPMK + ALTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
-
identification by mass spectroscopy
?
o-aminobenzoyl-FSQPMKRATLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQPMK + RATLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
-
13% of product formed, identification by mass spectroscopy
?
o-aminobenzoyl-FSQPMKRATLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQPMKR + ATLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
-
87% of product formed, identification by mass spectroscopy
?
o-aminobenzoyl-FSQPMKRLALGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQPMK + RLALGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
-
30% of product formed, identification by mass spectroscopy
?
o-aminobenzoyl-FSQPMKRLALGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQPMKR + LALGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
-
70% of product formed, identification by mass spectroscopy
?
o-aminobenzoyl-FSQPMKRLTAGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQPMKR + LTAGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
-
identification by mass spectroscopy
?
o-aminobenzoyl-FSQPMKRLTLANTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQPMK + RLTLANTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
-
20% of product formed, identification by mass spectroscopy
?
o-aminobenzoyl-FSQPMKRLTLANTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQPMKR + LTLANTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
-
80% of product formed, identification by mass spectroscopy
?
o-aminobenzoyl-FSQPMKRLTLGATTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQPMK + RLTLGATTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
-
19% of product formed, identification by mass spectroscopy
?
o-aminobenzoyl-FSQPMKRLTLGATTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQPMKR + LTLGATTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
-
81% of product formed, identification by mass spectroscopy
?
o-aminobenzoyl-FSQPMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQPMKR + LTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
synthetic fluorogenic substrate derived from the amino acid sequence of human prorenin cleavage site
identification by mass spectroscopy
?
o-aminobenzoyl-GEFIKKSSFQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-GEFIK + KSSFQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
synthetic fluorogenic substrate
67% of product formation, identification by mass spectroscopy
?
o-aminobenzoyl-GEFIKKSSFQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-GEFIKK + SSFQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
synthetic fluorogenic substrate
33% of product formation, identification by mass spectroscopy
?
o-aminobenzoyl-GEFIKKSSFTNVTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-GEFIK + KSSFTNVTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
synthetic fluorogenic substrate
62% of product formation, identification by mass spectroscopy
?
o-aminobenzoyl-GEFIKKSSFTNVTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-GEFIKK + SSFTNVTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
synthetic fluorogenic substrate
38% of product formation, identification by mass spectroscopy
?
o-aminobenzoyl-IKKSSF-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-IKK + SSF-N-(2,4-dinitrophenyl)-ethylene diamine
-
synthetic fluorogenic substrate
identification by mass spectroscopy
?
o-aminobenzoyl-LGMISLMKRPPGFSPFRSSRI-NH2 + H2O
bradykinin + ?
-
-
-
?
o-aminobenzoyl-VMIAALPRTMFIQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
?
-
low activity, substrate sequence is based on the Bauhinia ungulata inhibitor protein reactive site sequence
-
?
o-aminobenzoyl-VVISALPRTMFIQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
?
-
substrate sequence is based on the Bauhinia variegata inhibitor protein reactive site sequence
-
?
plasminogen + H2O
plasmin + ?
pro-hepatocyte growth factor + H2O
hepatocyte growth factor beta-chain + hepatocyte growth factor alpha-chain + 10 kDa fragment of the alpha-chain
-
i.e. HGF, two independent cleavage sites: Arg494-Val495, kinetically preferred, and Arg424-His425, recombinant mutant HGF R424A/R494E is no substrate
activation of hepatocyte growth factor
?
Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
pro-urokinase + H2O
urokinase + ?
pro-urokinase type plasminogen activator + H2O
urokinase type plasminogen activator + ?
-
-
-
-
?
RPGLPVRFESPLRINIIKE + H2O
RPGLPVR + FESPLRINIIKE
-
peptide based on the reactive site of the Bauhinia bauhinioides inhibitor protein, similar to the kinin moiety in human kininogen
-
?
RPGLPVRFESPLRINIIKE + H2O
RPGLPVRFESPLR + INIIKE
-
peptide based on the reactive site of the Bauhinia bauhinioides inhibitor protein, similar to the kinin moiety in human kininogen
main products
ir
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
additional information
?
-
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
-
-
-
-
?
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
-
-
-
ir
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
-
-
-
ir
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
-
-
-
ir
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
-
-
-
ir
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
-
-
-
ir
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
-
-
-
ir
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
-
-
-
ir
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
-
-
-
?
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
-
synthetic fluorogenic substrate
-
?
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
-
plasma kallikrein-selective substrate
-
-
?
factor XI + H2O
activated factor XI + ?
-
proteolytic activation
-
-
?
factor XI + H2O
activated factor XI + ?
-
proteolytic activation, part of the coagulation cascade
-
-
?
factor XII + H2O
?
-
activation of factor XII
-
?
factor XII + H2O
?
-
activation of factor XII
-
?
factor XII + H2O
?
activation of the factor XII, bound to negatively charged surfaces
-
?, ir
factor XII + H2O
?
activation of the factor XII, bound to negatively charged surfaces
-
?, ir
factor XII + H2O
?
activation of the factor XII, bound to negatively charged surfaces
-
?, ir
factor XII + H2O
activated factor XII
-
-
-
-
?
factor XII + H2O
activated factor XII
-
-
-
?
factor XII + H2O
activated factor XII
-
-
-
-
?
factor XII + H2O
activated factor XII + ?
-
-
-
-
?
factor XII + H2O
activated factor XII + ?
-
proteolytic activation
-
-
?
factor XII + H2O
activated factor XII + ?
-
-
-
-
?
high molecular weight kininogen + H2O
bradykinin + fragments of kininogen
-
-
-
-
?
high molecular weight kininogen + H2O
bradykinin + fragments of kininogen
-
-
-
-
?
high-molecular-weight kininogen + H2O
bradykinin + fragments of kininogen
-
-
-
-
?
high-molecular-weight kininogen + H2O
bradykinin + fragments of kininogen
cleavage between Lys and Arg as wekk as Arg and Ser
-
-
?
high-molecular-weight kininogen + H2O
bradykinin + fragments of kininogen
-
-
-
-
?
high-molecular-weight kininogen + H2O
high-molecular-weight kinin + bradykinin
-
-
bradykinin is Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
?
high-molecular-weight kininogen + H2O
high-molecular-weight kinin + bradykinin
-
pathways involving high-molecular-weight kininogen/high-molecular-weight kinin, overview
bradykinin is Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
?
kininogen + H2O
?
-
cleaves Lys-Arg and Arg-Ser bonds in kininogen to produce bradykinin, participates in early phase of intrinsic blood coagulation
-
-
?
kininogen + H2O
?
-
cleaves Lys-Arg and Arg-Ser bonds in kininogen to produce bradykinin, participates in early phase of intrinsic blood coagulation
-
-
?
kininogen + H2O
bradykinin + ?
-
-
-
?
kininogen + H2O
bradykinin + ?
-
-
-
-
?
kininogen + H2O
bradykinin + ?
-
cleaves Lys-Arg and Arg-Ser bonds in kininogen to produce bradykinin
-
?
kininogen + H2O
bradykinin + ?
-
the presence of S at P1' position for bradykinin release by human plasma kallikrein appears to be essential
-
-
?
kininogen + H2O
bradykinin + ?
-
-
-
?
kininogen + H2O
bradykinin + ?
-
-
-
?
kininogen + H2O
bradykinin + ?
-
-
-
-
?
kininogen + H2O
bradykinin + fragment of kininogen
-
-
-
?
kininogen + H2O
bradykinin + fragment of kininogen
-
-
-
?
kininogen + H2O
bradykinin + fragment of kininogen
-
-
-
?
kininogen + H2O
bradykinin + fragment of kininogen
-
-
-
?
kininogen + H2O
bradykinin + fragment of kininogen
-
-
-
?
kininogen + H2O
bradykinin + fragment of kininogen
-
-
-
?
kininogen + H2O
bradykinin + fragment of kininogen
-
-
-
ir
kininogen + H2O
bradykinin + fragment of kininogen
-
-
-
ir
kininogen + H2O
bradykinin + fragment of kininogen
-
-
-
ir
kininogen + H2O
bradykinin + fragment of kininogen
-
-
-
ir
kininogen + H2O
bradykinin + fragment of kininogen
-
high-molecular weight substrate, serine protease
-
?
kininogen + H2O
bradykinin + fragment of kininogen
-
enzyme is a cofactor in blood coagulation and modulates inflammation through release of bradykinin
-
ir
kininogen + H2O
bradykinin + fragment of kininogen
-
part of kallikrein-kininsystem
bradykinin is a potent mediator of inflammatory response
ir
kininogen + H2O
bradykinin + fragments of kininogen
-
-
-
-
?
kininogen + H2O
bradykinin + fragments of kininogen
-
-
-
?
kininogen + H2O
bradykinin + fragments of kininogen
-
-
-
-
?
kininogen + H2O
bradykinin + fragments of kininogen
high-molecular weight kininogen
-
?, ir
kininogen + H2O
bradykinin + fragments of kininogen
-
high-molecular weight kininogen, preferred substrate
-
?
kininogen + H2O
bradykinin + fragments of kininogen
-
low-molecular weight kininogen, low activity
-
?
kininogen + H2O
bradykinin + fragments of kininogen
-
high-molecular weight kininogen, involved in inflammatory reaction
-
ir
kininogen + H2O
bradykinin + fragments of kininogen
-
-
-
-
?
kininogen + H2O
bradykinin + fragments of kininogen
-
-
-
-
?
kininogen + H2O
bradykinin + fragments of kininogen
-
-
-
?
kininogen + H2O
bradykinin + fragments of kininogen
high-molecular weight kininogen
-
ir
kininogen + H2O
bradykinin + fragments of kininogen
human high-molecular weight kininogen
-
?
kininogen + H2O
bradykinin + fragments of kininogen
-
-
-
-
?
kininogen + H2O
bradykinin + fragments of kininogen
high-molecular weight kininogen
-
?, ir
modified kininogen + H2O
bradykinin + fragments of kininogen
-
high-molecular weight kininogen digested by human neutrophil elastase
-
?, ir
modified kininogen + H2O
bradykinin + fragments of kininogen
-
low-molecular weight kininogen digested by human neutrophil elastase, 26 amino acids cleaved off, is a better substrate than native low-molecular weight kininogen
-
?
Nalpha-Benzoyl-L-Arg ethyl ester + H2O
Nalpha-Benzoyl-L-Arg + ethanol
-
-
-
-
?
Nalpha-Benzoyl-L-Arg ethyl ester + H2O
Nalpha-Benzoyl-L-Arg + ethanol
-
-
-
-
?
Nalpha-toluenesulfonyl-L-arginine methyl ester + H2O
Nalpha-toluenesulfonyl-L-arginine + methanol
-
-
-
-
?
Nalpha-toluenesulfonyl-L-arginine methyl ester + H2O
Nalpha-toluenesulfonyl-L-arginine + methanol
-
-
-
-
?
plasminogen + H2O
plasmin + ?
-
activation of plasminogen
-
ir
plasminogen + H2O
plasmin + ?
-
activation of plasminogen
-
ir
plasminogen + H2O
plasmin + ?
-
proteolytic activation
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
-
?
pro-urokinase + H2O
urokinase + ?
-
activation of pro-urokinase
-
?
pro-urokinase + H2O
urokinase + ?
-
activation of pro-urokinase
-
?
Prorenin + H2O
Renin + ?
-
-
-
-
?
Prorenin + H2O
Renin + ?
-
activation of human prorenin
-
ir
Prorenin + H2O
Renin + ?
-
activation of prorenin
-
ir
Prorenin + H2O
Renin + ?
activation of prorenin
-
ir
Prorenin + H2O
Renin + ?
activation of prorenin, involved in the renin-angiotensin system
-
ir
Prorenin + H2O
Renin + ?
-
-
-
-
?
Prorenin + H2O
Renin + ?
activation of prorenin
-
ir
Prorenin + H2O
Renin + ?
activation of prorenin, involved in the renin-angiotensin system
-
ir
Prorenin + H2O
Renin + ?
activation of prorenin
-
ir
Prorenin + H2O
Renin + ?
-
rat prorenin, very low activity
-
ir
Prorenin + H2O
Renin + ?
activation of prorenin, involved in the renin-angiotensin system
-
ir
additional information
?
-
-
overexpression of prolylcarboxypeptidase in CHO cells enhances plasma prekallikrein activation
-
-
?
additional information
?
-
-
based on the reactive site sequence of Bauhinia ungulata Xa inhibitor peptides
-
-
?
additional information
?
-
belongs to the peptidase family S1, plasma kallikrein subfamily
-
?
additional information
?
-
-
no activity with o-aminobenzoyl-RPGLPVRFESPL-N-(2,4-dinitrophenyl)-ethylene diamine and o-aminobenzoyl-FESPLRINIIKE-N-(2,4-dinitrophenyl)-ethylene diamine, which are based on the Bauhinia bauhinioides inhibitor protein reactive site sequence
-
?
additional information
?
-
-
substrate specificity requirements
-
?
additional information
?
-
defects in gene KLKB1 cause Fletcher factor deficiency, a blood coagulation defect
-
?
additional information
?
-
-
enzyme activity is enhanced in orthotopic liver transplant recipients
-
?
additional information
?
-
-
involved in inflammatory processes via hydrolysis of complement
-
?
additional information
?
-
-
involved in plasma and vascular fibrinolytic activity
-
?
additional information
?
-
-
cathepsin may control the activity of plasma prekallikrein/kallikrein system proteins associated with either the cell surface or the extracellular matrix in (patho)physiological processes
-
-
?
additional information
?
-
-
the review indicates how the plasma kallikrein/kinin system and the plasma renin-angiotensin system are activated and interact in endotoxin or related forms of induced sepsis. Activation of both the plasma kallikrein/kinin system and the plasma renin-angiotensin system can lead to increased nitric oxide and prostaglandin formation
-
-
?
additional information
?
-
kallikrein participates in the surface-dependent activation of blood coagulation, fibrinolysis, kinin generation and inflammation, it has different specific cellular functions dependent on the tissue, overview
-
-
?
additional information
?
-
-
kallikrein participates in the surface-dependent activation of blood coagulation, fibrinolysis, kinin generation and inflammation, it has different specific cellular functions dependent on the tissue, overview
-
-
?
additional information
?
-
-
plasma kallikrein activates neutrophil aggregation and degranulation, the enzyme is part of the kallikrein-kininogen-kinin system, KKS, kininogen plays a role in signaling pathways via the kininogen receptors, mechanism of inflammation related to KKS, overview
-
-
?
additional information
?
-
-
the enzyme involved in intrinsic blood clotting, the kallikrein-kinin system and fibrinolysis
-
-
?
additional information
?
-
-
the enzyme is part of the kallikrein-kininogen-kinin system, KKS, overview
-
-
?
additional information
?
-
-
the enzyme is part of the plasma kallikrein-kininogen-kinin system, PKKS, which is involved in cardiovascular disease and artherothrombosis, e.g. coronary heart disease and stroke in middle-aged men, overview
-
-
?
additional information
?
-
-
the enzyme is part of the plasma kallikrein/kinin system that consists of the protein factor XII, prekallikrein, and high-molecular-weight kininogen, intravascular assembly of the plasma kallikrein/kinin system, overview, it acts as a surface-activated coagulation system arising when blood or plasma interacts with artificial surfaces, kallikrein is involved in development of arterial thrombosis, mechanisms, overview
-
-
?
additional information
?
-
-
kininogen domain structure, overview
-
-
?
additional information
?
-
peptides with Pro at P2 are poor substrates
-
-
?
additional information
?
-
belongs to the peptidase family S1, plasma kallikrein subfamily
-
?
additional information
?
-
-
active plasma kallikrein localizes to mast cells and regulates epithelial cell apoptosis, adipocyte differentiation and stromal remodeling during mammary gland involution
-
-
?
additional information
?
-
belongs to the peptidase family S1, plasma kallikrein subfamily
-
?
additional information
?
-
-
substrate specificity requirements, very low activity with the equivalent of rat prorenin to the cleavage site and with the peptide o-aminobenzoyl-NVTSPVQ-N-(2,4-dinitrophenyl)-ethylene diamine, activation of rat prorenin requires a different enzyme and/or mechanism
-
?
additional information
?
-
may play a role in invasion of the host immune response
-
?
additional information
?
-
-
based on the reactive site sequence of Bauhinia ungulata Xa inhibitor peptides
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
factor B + H2O
factor Bb + ?
-
-
-
-
?
factor FXII + H2O
activated factor XII + ?
cleavage between Arg and Val
-
-
?
factor H + H2O
?
-
-
-
-
?
factor X + H2O
factor XIIa + ?
-
-
-
-
?
factor XI + H2O
activated factor XI + ?
factor XII + H2O
activated factor XII
factor XII + H2O
activated factor XII + ?
factor XII + H2O
factor XIIa + ?
-
-
-
-
?
high molecular weight kininogen + H2O
bradykinin + fragments of kininogen
high-molecular-weight kininogen + H2O
bradykinin + fragments of kininogen
high-molecular-weight kininogen + H2O
high-molecular-weight kinin + bradykinin
kininogen + H2O
bradykinin + ?
kininogen + H2O
bradykinin + fragment of kininogen
kininogen + H2O
bradykinin + fragments of kininogen
kininogen + H2O
heavy chain of kininogen + light chain of kininogen + bradykinin
-
high molecular weight substrate, serine protease
bradykinin is an inflammatory peptide
ir
low-molecular-weight kininogen + H2O
low-molecular-weight kinin + kallidin
-
-
kallidin is Lys-bradykinin or Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
?
modified kininogen + H2O
bradykinin + fragments of kininogen
-
high-molecular weight kininogen digested by human neutrophil elastase
-
ir
plasminogen + H2O
plasmin + ?
-
-
-
-
?
pro-urokinase type plasminogen activator + H2O
urokinase type plasminogen activator + ?
-
-
-
-
?
additional information
?
-
factor XI + H2O
activated factor XI + ?
-
proteolytic activation
-
-
?
factor XI + H2O
activated factor XI + ?
-
proteolytic activation, part of the coagulation cascade
-
-
?
factor XII + H2O
?
activation of the factor XII, bound to negatively charged surfaces
-
ir
factor XII + H2O
?
activation of the factor XII, bound to negatively charged surfaces
-
ir
factor XII + H2O
?
activation of the factor XII, bound to negatively charged surfaces
-
ir
factor XII + H2O
activated factor XII
-
-
-
-
?
factor XII + H2O
activated factor XII
-
-
-
?
factor XII + H2O
activated factor XII
-
-
-
-
?
factor XII + H2O
activated factor XII + ?
-
-
-
-
?
factor XII + H2O
activated factor XII + ?
-
proteolytic activation
-
-
?
factor XII + H2O
activated factor XII + ?
-
-
-
-
?
high molecular weight kininogen + H2O
bradykinin + fragments of kininogen
-
-
-
-
?
high molecular weight kininogen + H2O
bradykinin + fragments of kininogen
-
-
-
-
?
high-molecular-weight kininogen + H2O
bradykinin + fragments of kininogen
-
-
-
-
?
high-molecular-weight kininogen + H2O
bradykinin + fragments of kininogen
cleavage between Lys and Arg as wekk as Arg and Ser
-
-
?
high-molecular-weight kininogen + H2O
bradykinin + fragments of kininogen
-
-
-
-
?
high-molecular-weight kininogen + H2O
high-molecular-weight kinin + bradykinin
-
-
bradykinin is Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
?
high-molecular-weight kininogen + H2O
high-molecular-weight kinin + bradykinin
-
pathways involving high-molecular-weight kininogen/high-molecular-weight kinin, overview
bradykinin is Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
?
kininogen + H2O
?
-
cleaves Lys-Arg and Arg-Ser bonds in kininogen to produce bradykinin, participates in early phase of intrinsic blood coagulation
-
-
?
kininogen + H2O
?
-
cleaves Lys-Arg and Arg-Ser bonds in kininogen to produce bradykinin, participates in early phase of intrinsic blood coagulation
-
-
?
kininogen + H2O
bradykinin + ?
-
-
-
-
?
kininogen + H2O
bradykinin + ?
-
the presence of S at P1' position for bradykinin release by human plasma kallikrein appears to be essential
-
-
?
kininogen + H2O
bradykinin + ?
-
-
-
-
?
kininogen + H2O
bradykinin + fragment of kininogen
-
-
-
ir
kininogen + H2O
bradykinin + fragment of kininogen
-
-
-
ir
kininogen + H2O
bradykinin + fragment of kininogen
-
-
-
ir
kininogen + H2O
bradykinin + fragment of kininogen
-
-
-
ir
kininogen + H2O
bradykinin + fragment of kininogen
-
enzyme is a cofactor in blood coagulation and modulates inflammation through release of bradykinin
-
ir
kininogen + H2O
bradykinin + fragment of kininogen
-
part of kallikrein-kininsystem
bradykinin is a potent mediator of inflammatory response
ir
kininogen + H2O
bradykinin + fragments of kininogen
-
-
-
-
?
kininogen + H2O
bradykinin + fragments of kininogen
-
-
-
?
kininogen + H2O
bradykinin + fragments of kininogen
-
-
-
-
?
kininogen + H2O
bradykinin + fragments of kininogen
high-molecular weight kininogen
-
ir
kininogen + H2O
bradykinin + fragments of kininogen
-
high-molecular weight kininogen, involved in inflammatory reaction
-
ir
kininogen + H2O
bradykinin + fragments of kininogen
-
-
-
-
?
kininogen + H2O
bradykinin + fragments of kininogen
-
-
-
-
?
kininogen + H2O
bradykinin + fragments of kininogen
-
-
-
?
kininogen + H2O
bradykinin + fragments of kininogen
high-molecular weight kininogen
-
ir
kininogen + H2O
bradykinin + fragments of kininogen
-
-
-
-
?
kininogen + H2O
bradykinin + fragments of kininogen
high-molecular weight kininogen
-
ir
Prorenin + H2O
Renin + ?
-
-
-
-
?
Prorenin + H2O
Renin + ?
-
activation of prorenin
-
ir
Prorenin + H2O
Renin + ?
activation of prorenin, involved in the renin-angiotensin system
-
ir
Prorenin + H2O
Renin + ?
-
-
-
-
?
Prorenin + H2O
Renin + ?
activation of prorenin, involved in the renin-angiotensin system
-
ir
Prorenin + H2O
Renin + ?
activation of prorenin, involved in the renin-angiotensin system
-
ir
additional information
?
-
-
overexpression of prolylcarboxypeptidase in CHO cells enhances plasma prekallikrein activation
-
-
?
additional information
?
-
defects in gene KLKB1 cause Fletcher factor deficiency, a blood coagulation defect
-
?
additional information
?
-
-
enzyme activity is enhanced in orthotopic liver transplant recipients
-
?
additional information
?
-
-
involved in inflammatory processes via hydrolysis of complement
-
?
additional information
?
-
-
involved in plasma and vascular fibrinolytic activity
-
?
additional information
?
-
-
cathepsin may control the activity of plasma prekallikrein/kallikrein system proteins associated with either the cell surface or the extracellular matrix in (patho)physiological processes
-
-
?
additional information
?
-
-
the review indicates how the plasma kallikrein/kinin system and the plasma renin-angiotensin system are activated and interact in endotoxin or related forms of induced sepsis. Activation of both the plasma kallikrein/kinin system and the plasma renin-angiotensin system can lead to increased nitric oxide and prostaglandin formation
-
-
?
additional information
?
-
kallikrein participates in the surface-dependent activation of blood coagulation, fibrinolysis, kinin generation and inflammation, it has different specific cellular functions dependent on the tissue, overview
-
-
?
additional information
?
-
-
kallikrein participates in the surface-dependent activation of blood coagulation, fibrinolysis, kinin generation and inflammation, it has different specific cellular functions dependent on the tissue, overview
-
-
?
additional information
?
-
-
plasma kallikrein activates neutrophil aggregation and degranulation, the enzyme is part of the kallikrein-kininogen-kinin system, KKS, kininogen plays a role in signaling pathways via the kininogen receptors, mechanism of inflammation related to KKS, overview
-
-
?
additional information
?
-
-
the enzyme involved in intrinsic blood clotting, the kallikrein-kinin system and fibrinolysis
-
-
?
additional information
?
-
-
the enzyme is part of the kallikrein-kininogen-kinin system, KKS, overview
-
-
?
additional information
?
-
-
the enzyme is part of the plasma kallikrein-kininogen-kinin system, PKKS, which is involved in cardiovascular disease and artherothrombosis, e.g. coronary heart disease and stroke in middle-aged men, overview
-
-
?
additional information
?
-
-
the enzyme is part of the plasma kallikrein/kinin system that consists of the protein factor XII, prekallikrein, and high-molecular-weight kininogen, intravascular assembly of the plasma kallikrein/kinin system, overview, it acts as a surface-activated coagulation system arising when blood or plasma interacts with artificial surfaces, kallikrein is involved in development of arterial thrombosis, mechanisms, overview
-
-
?
additional information
?
-
-
active plasma kallikrein localizes to mast cells and regulates epithelial cell apoptosis, adipocyte differentiation and stromal remodeling during mammary gland involution
-
-
?
additional information
?
-
may play a role in invasion of the host immune response
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-benzyl-1H-pyrazole-4-carboxylic acid 4-carbamimidoyl-benzylamide
-
ASP-440, small molecule inhibitor of plasma kallikrein
2-mercaptoethanol
-
inhibition of prekallikrein activation
2-[3'-acetyl-5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxybiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-2',6-dihydroxybiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-2'-fluoro-6-hydroxybiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-3',6-dihydroxybiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-3'-carbamoyl-6-hydroxybiphenyl-3-yl]butanedioic acid
-
inhibitor with the best potency and selectivity profile for plasma kallikrein versus related serine proteases. This compound is highly stable in vivo and could be further developed for the treatment and inflammatory or coagulation disorders. Pharmacokinetic data
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-3'-chloro-6-hydroxybiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-3'-cyano-6-hydroxybiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-4'-chloro-6-hydroxybiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-2'-methoxybiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-2'-methylbiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-3'-methoxybiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-3'-methylbiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-4'-methoxybiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-4'-methylbiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxybiphenyl-3-yl]butanedioic acid
-
-
alpha 2 macroglobulin
-
-
-
alpha1-antiprotease
-
-
-
alpha1-proteinase inhibitor-Leu-Gly-Arg
-
mutant of serpin alpha1-proteinase inhibitor with exchange at P3, P2 and P1 position, fast complexing, inhibition kinetics
-
alpha1-proteinase inhibitor-Pro-Phe-Arg
-
mutant of serpin alpha1-proteinase inhibitor with exchange at P3, P2 and P1 position, inhibition kinetics
-
alpha2-Macroglobulin
-
-
-
Alzheimer's amyloid beta-protein precursor
-
weak inhibition
-
antithrombin
-
inhibition by antithrombin is 3.4fold improved by heparin, forming a ternary complex with antithrombin
-
Bauhinia unglata factor Xa inhibitor
-
-
-
Bauhinia ungulata factor Xa inhibitor protein
-
-
-
Bauhinia variegata trypsin inhibitor protein
-
-
-
BCX4161
low nanomolar inhibitory potency
bicyclic peptide Ac-CiS1F2[Aze]3Y4[HArg]5Cii[Ala(PsiCH2-NH)]6H7Q8D9L10Ciii
-
-
-
bicyclic peptide Ac-CiS1W2P3A4R5CiiL6H7Q8D9L10Ciii
-
-
-
bovine dermatan sulfate
-
68% inhibition at
-
C1 esterase inhibitor
-
-
-
C1 inhibitor
-
increased levels of kallikrein-C1 inhibitor complex are independently associated with increased risk for all-cause mortality and the combined endpoint of all-cause mortality or recurrent troponin T-positive events in patients with admission troponin T greater than/equal 0.05 ng/mL
-
cysteine
-
inhibition of prekallikrein activation
D-Arg-Hph-Arg-CH2OCH2CF3
-
-
D-Arg-Phe-Arg-CH2OCH2CF3
-
-
D-Arg-Phe-Arg-Ser-NH2
-
-
D-Phe-Phe-Arg-chloromethylketone
-
complete inhibition at 0.01 mM
D-Pro-Cha-ArgOH-CH2OCH2CF3
-
-
D-Pro-Phe-Arg-CH2OCH2CF3
-
-
diisopropylfluorophosphate
diphenylcarbamoylfluoride
-
-
dithiothreitol
-
inhibition of prekallikrein activation
DX-88
-
DX-88 has a strong neuroprotective effect in the early phases of brain ischemia preventing reperfusion injury and indicates that inhibition of plasma kallikrein may be useful tool in the strategy aimed at reducing the detrimental effects linked to reperfusion
-
ecotin
-
ecotin with mutation H53P in the 50s loop, mutations S82W/T83N/M84R/M85R/A86S in the 80s loop and mutations R108S/N110S in the 100s loop is a high-affinity and highly specific plasma kallikrein inhibitor. Specifically inhibits contact activation of human plasma at the level mediated by plasma kallikrein. Discriminates between enzyme and zymogen. Partial thromboplastin time inhibition can be rescued by addition of PKal
-
ecotin-plasma kallikrein
-
highly specific inhibitor of active plasma kallikrein
-
Elastase
-
of human neutrophils, degrades kininogen itself to kinin-containing fragments and therefore quenches the kininogen degeneration/bradykinin generation by plasma kallikrein
-
ferritin
-
high-molecular weight kininogen is a ferritin-binding protein, binding to the modified light chain of activated kininogen. Binding to kininogen retards the release of bradykinin by inhibition of kallikrein, no inhibition with substrates other than kininogen, binding mechanism, inhibition by holo- and apoferritin
-
glutathione
-
inhibition of prekallikrein activation
heparin
-
improves inhibition by other enzyme inhibitor 1.4-3.4fold, the enzyme binds to a heparin-matrix, but its secondary structure is not modified by heparin, circular dichroism, overview
hepatocyte growth factor activator inhibitor-1
-
i.e. HAI-1, Kunitz type inhibitor specific for serine proteases, relatively weak inhibition
-
hepatocyte growth factor activator inhibitor-1B
-
splicing variant of hepatocyte growth factor activator inhibitor-1, Kunitz type inhibitor specific for serine proteases, relatively weak inhibition
-
HgCl2
-
inhibition of prekallikrein activation
human C1 esterase inhibitor
-
63% inhibition at 0.04 mg/ml
-
human IgG1 monoclonal antibody DX-2930
-
N-alpha-tosyl-D,L-homophenylalanine-4-anilide hydrochloride
-
also known as Pefabloc PK, inhibits plasma kallikrein exclusively
N-[(6-amino-2,4-dimethylpyridin-3-yl)methyl]-1-[[4-(1H-pyrazol-1-ylmethyl)phenyl]methyl]-1H-pyrazole-4-carboxamide
low nanomolar inhibitory potency
o-aminobenzoyl-FESPLRINIIKE-N-(2,4-dinitrophenyl)-ethylene diamine
-
competitive inhibitors, based on the Bauhinia bauhinioides inhibitor protein reactive site sequence
o-aminobenzoyl-RPGLPVRFESPL-N-(2,4-dinitrophenyl)-ethylene diamine
-
competitive inhibitors, based on the Bauhinia bauhinioides inhibitor protein reactive site sequence
Oxyuranus microlepidotus inhibitor
-
-
-
p-Carboethoxyphenyl epsilon-guanidine caproate
-
-
plasma kallikrein serine protease inhibitor
-
highly specific
-
plasma kallikrein-specific Kunitz domain inhibitor
-
-
-
Protein C inhibitor
-
-
-
Soybean trypsin inhibitor
-
specific serine protease inhibitor protein from Bauhinia bauhinioides seeds
-
Swartzia pickellii trypsin inhibitor
-
purified from seeds, serine protease inhibitor, contains a glycosylation site at Asn38, Kunitz type, but contains only 1 disulfide bridge
-
taicatoxin serine protease inhibitor
-
broad spectrum inhibitor with most potent inhibitory activity observed against plasma kallikrein
-
trans-(4-aminomethylcyclohexanecarbonyl)-Tyr(O-2-Pyrim)-4-carboxyanilide
-
-
trans-(4-aminomethylcyclohexanecarbonyl)-Tyr(O-Pic)-octylamide
-
-
trans-4-aminomethylcyclohexanecarbonyl-D-phenylalanyl-PSI(CH2-NH)-4-aminophenyl acetic acid
-
PKSI-527 pseudo-peptide analogue, 5% inhibition at 1 mM
trans-4-aminomethylcyclohexanecarbonyl-L-phenylalanyl-4-aminophenyl acetic acid
-
i.e. PKSI-527, selective inhibitor, both carbonyl groups of the structure are required
trans-4-aminomethylcyclohexanecarbonyl-L-phenylalanyl-PSI(CH2-NH)-4-aminophenyl acetic acid
-
PKSI-527 pseudo-peptide analogue, 7% inhibition at 1 mM
trans-4-aminomethylcyclohexanecarbonyl-PSI(CH2-NH)-L-phenylalanyl-4-aminophenyl acetic acid
-
PKSI-527 pseudo-peptide analogue, 20% inhibition at 1 mM
triafestin-1
-
isolation and analysis of the enzyme inhibitor from salivary glands of instar nymphs of Triatoma infestans, SwissProt ID A7BJ45, recombinant production in insect or Escherichia coli cells, triafestin-1 specifically interacts with factor XII and high molecular weight kininogen in a Zn2+-dependent manner, and inhibit activation of the kallikrein-kinin system by interfering with the association of factor XII and high molecular weight kininogen with biological activating surfaces as well as inhibiting prekallikrein activation, overview
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triafestin-2
-
isolation and analysis of enzyme inhibitors from salivary glands of instar nymphs of Triatoma infestans, SwissProt ID A7BJ46, recombinant production in insect or Escherichia coli cells, triafestin-2 specifically interacts with factor XII and high molecular weight kininogen in a Zn2+-dependent manner, and inhibit activation of the kallikrein-kinin system by interfering with the association of factor XII and high molecular weight kininogen with biological activating surfaces as well as inhibiting prekallikrein activation, overview
-
tuna dermatan sulfate
-
80% inhibition at
-
Type IV collagen
-
0.02 mg/ml of collagen causes a slight loss of activity even after 5 hours, whereas with 0.1 mg/ml of collagen, there is an initial rapid decrease of activity to about 40%
-
Z-Phe-OH
-
inhibition of prekallikrein activation
Zn2+
-
inhibits the activation of prekallikrein at concentrations above 0.01 mM, regulatory role
antipain
-
inhibition of prekallikrein activation
benzamidine
-
-
C1-inhibitor
-
activation of plasma kallikrein and generation of bradykinin are responsible for the angioedema attacks observed with C-1 inhibitor deficiency. C1-inhibitor concentration of greater than 0.001 mM is needed to inhibit 3 nM kallikrein
-
C1-inhibitor
-
inhibition by C1-inhibitor is 1.4fold improved by heparin
-
diisopropylfluorophosphate
-
-
diisopropylfluorophosphate
-
-
diisopropylfluorophosphate
-
-
ecallantide
-
also called DX-88, C305H442N86O91S8, potent and specific inhibitor of plasma kallikrein
-
human IgG1 monoclonal antibody DX-2930
potently and specifically inhibits plasma kallikrein
-
human IgG1 monoclonal antibody DX-2930
-
potently and specifically inhibits plasma kallikrein
-
human IgG1 monoclonal antibody DX-2930
-
potently and specifically inhibits plasma kallikrein
-
human IgG1 monoclonal antibody DX-2930
-
potently and specifically inhibits plasma kallikrein
-
leupeptin
-
-
Soybean trypsin inhibitor
-
-
-
Soybean trypsin inhibitor
-
-
-
Soybean trypsin inhibitor
-
-
-
specific serine protease inhibitor protein from Bauhinia bauhinioides seeds
-
Kunitz type, purified 20 kDa protein
-
specific serine protease inhibitor protein from Bauhinia bauhinioides seeds
-
Kunitz type, purified 20 kDa protein, thermolabile inhibition, optimal at pH 8.0 for trypsin, characterization
-
additional information
-
inhibitory potential of diverse trans-(4-aminomethylcyclohexanecarbonyl)-derivatives, structure-activity relationship study, overview
-
additional information
-
no inhibition by hirudin, bdellin, and corn trypsin inhibitor
-
additional information
-
no inhibition by corn trypsin inhibitor
-
additional information
-
angiotensin II inhibits plasma prekallikrein activation by 11%. 2-Mercaptoethanol, EDTA, benzamidine, 2-aminoethyl benzenesulfonyl fluoride, antipain or leupeptin have little effect on activation, whereas cysteine inhibits activation by approximately 65% at 10 mM. Incubation with 500 mM des-arg9-bradykinin, bradykinin fragment 1-7 or bradykinin fragment 1-5 inhibit plasma prekallikrein activation on A-549 cells by 6%, 20% and 4%, respectively. Plasma prekallikrein activation on A-549 cells is not significantly inhibited by Plummers inhibitor, phosphoramidon, captropril, or apstatin
-
additional information
-
preplasma kallikrein activation on MeT-5A, NCI-H2052, NCI-H28 and primary murine mesothelial cells is strongly inhibited by 10 mM cysteine, 100 mM bradykinin, 100 mg/ml protamine sulfate and 5 mM novobiocin. Moderate inhibition is observed with 2-mercaptoethanol, 2-aminoethyl benzenesulfonyl fluoride, antipain and leupeptin on most cell lines. Angiotensin II, benzamidine and EDTA do not inhibit activation
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Sus scrofa
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Abdallah, R.T.; Keum, J.S.; El-Shewy, H.M.; Lee, M.H.; Wang, B.; Gooz, M.; Luttrell, D.K.; Luttrell, L.M.; Jaffa, A.A.
Plasma kallikrein promotes epidermal growth factor receptor transactivation and signaling in vascular smooth muscle through direct activation of protease-activated receptors
J. Biol. Chem.
285
35206-35215
2010
Homo sapiens
brenda
Liu, J.; Gao, B.B.; Clermont, A.C.; Blair, P.; Chilcote, T.J.; Sinha, S.; Flaumenhaft, R.; Feener, E.P.
Hyperglycemia-induced cerebral hematoma expansion is mediated by plasma kallikrein
Nat. Med.
17
206-210
2011
Rattus norvegicus
brenda
Renne, T.
The vascular side of plasma kallikrein
Blood
125
589-590
2015
Mus musculus
brenda
Baeriswyl, V.; Rapley, H.; Pollaro, L.; Stace, C.; Teufel, D.; Walker, E.; Chen, S.; Winter, G.; Tite, J.; Heinis, C.
Bicyclic peptides with optimized ring size inhibit human plasma kallikrein and its orthologues while sparing paralogous proteases
ChemMedChem
7
1173-1176
2012
Homo sapiens (P03952), Homo sapiens
brenda
Ravindran, S.; Schapira, M.; Patston, P.A.
Modulation of C1-inhibitor and plasma kallikrein activities by type IV collagen
Int. J. Biomater.
2012
212417
2012
Homo sapiens
brenda
Kenniston, J.; Faucette, R.; Martik, D.; Comeau, S.; Lindberg, A.; Kopacz, K.; Conley, G.; Chen, J.; Viswanathan, M.; Kastrapeli, N.; Cosic, J.; Mason, S.; DiLeo, M.; Abendroth, J.; Kuzmic, P.; Ladner, R.; Edwards, T.; TenHoor, C.; Adelman, B.; Nixon, A.;
Inhibition of plasma kallikrein by a highly specific active site blocking antibody
J. Biol. Chem.
289
23596-23608
2014
Macaca fascicularis, Mus musculus, Rattus norvegicus, Homo sapiens (P03952), Homo sapiens
brenda
Koumandou, V.L.; Scorilas, A.
Evolution of the plasma and tissue kallikreins, and their alternative splicing isoforms
PLoS ONE
8
e68074
2013
Homo sapiens
brenda
Veronez, C.L.; Nascimento, F.D.; Melo, K.R.; Nader, H.B.; Tersariol, I.L.; Motta, G.
The involvement of proteoglycans in the human plasma prekallikrein interaction with the cell surface
PLoS ONE
9
e91280
2014
Homo sapiens
brenda
Renne, T.; Gruber, A.
Plasma kallikrein: Novel functions for an old protease
Thromb. Haemost.
107
1012-1013
2012
Mus musculus
brenda
Bjoerkqvist, J.; Jaemsae, A.; Renne, T.
Plasma kallikrein: the bradykinin-producing enzyme
Thromb. Haemost.
110
399-407
2013
Homo sapiens
brenda
Pathak, M.; Wong, S.S.; Dreveny, I.; Emsley, J.
Structure of plasma and tissue kallikreins
Thromb. Haemost.
110
423-433
2013
Homo sapiens (P03952)
brenda
Feener, E.P.; Zhou, Q.; Fickweiler, W.
Role of plasma kallikrein in diabetes and metabolism
Thromb. Haemost.
110
434-441
2013
Mus musculus
brenda
Ottaiano, T.F.; Andrade, S.S.; de Oliveira, C.; Silva, M.C.C.; Buri, M.V.; Juliano, M.A.; Girao, M.J.B.C.; Sampaio, M.U.; Schmaier, A.H.; Wlodawer, A.; Maffei, F.H.A.; Oliva, M.L.V.
Plasma kallikrein enhances platelet aggregation response by subthreshold doses of ADP
Biochimie
135
72-81
2017
Homo sapiens
brenda
Lieb, W.; Chen, M.; Teumer, A.; De Boer, R.; Lin, H.; Fox, E.; Musani, S.; Wilson, J.; Wang, T.; Voelzke, H.; Petersen, A.; Meisinger, C.; Nauck, M.; Schlesinger, S.; Li, Y.; Menard, J.; Hercberg, S.; Wichmann, H.; Voelker, U.; Rawal, R.; Bidlingmaier, M.
Genome-wide meta-analyses of plasma renin activity and concentration reveal association with the kininogen 1 and prekallikrein genes
Circ. Cardiovasc. Genet.
8
131-140
2015
Homo sapiens
brenda
Fischer, C.; Lamer, T.; Wang, W.; McKinnie, S.M.K.; Iturrioz, X.; Llorens-Cortes, C.; Oudit, G.Y.; Vederas, J.C.
Plasma kallikrein cleaves and inactivates apelin-17 Palmitoyl- and PEG-extended apelin-17 analogs as metabolically stable blood pressure-lowering agents
Eur. J. Med. Chem.
166
119-124
2019
Homo sapiens
brenda
Xu, M.; Chen, Y.; Xu, P.; Andreasen, P.A.; Jiang, L.; Li, J.; Huang, M.
Crystal structure of plasma kallikrein reveals the unusual flexibility of the S1 pocket triggered by Glu217
FEBS Lett.
592
2658-2667
2018
Mus musculus (P26262), Mus musculus
brenda
Schmaier, A.H.
Plasma prekallikrein its role in hereditary angioedema and health and disease
Front. Med.
5
3-3
2018
Homo sapiens, Mus musculus
brenda
Motta, G.; Tersariol, I.L.S.
Modulation of the plasma kallikrein-kinin system proteins performed by heparan sulfate proteoglycans
Front. Physiol.
8
481
2017
Homo sapiens
brenda
Teufel, D.P.; Bennett, G.; Harrison, H.; van Rietschoten, K.; Pavan, S.; Stace, C.; Le Floch, F.; Van Bergen, T.; Vermassen, E.; Barbeaux, P.; Hu, T.T.; Feyen, J.H.M.; Vanhove, M.
Stable and long-lasting, novel bicyclic peptide plasma kallikrein inhibitors for the treatment of diabetic macular edema
J. Med. Chem.
61
2823-2836
2018
Rattus norvegicus
brenda
Partridge, J.R.; Choy, R.M.; Silva-Garcia, A.; Yu, C.; Li, Z.; Sham, H.; Metcalf, B.
Structures of full-length plasma kallikrein bound to highly specific inhibitors describe a new mode of targeted inhibition
J. Struct. Biol.
206
170-182
2019
Homo sapiens (P03952)
brenda
Li, C.; Voos, K.M.; Pathak, M.; Hall, G.; McCrae, K.R.; Dreveny, I.; Li, R.; Emsley, J.
Plasma kallikrein structure reveals apple domain disc rotated conformation compared to factor XI
J. Thromb. Haemost.
17
759-770
2019
Homo sapiens (P03952), Homo sapiens
brenda
Goebel, K.; Asaridou, C.M.; Merker, M.; Eichler, S.; Herrmann, A.M.; Geuss, E.; Ruck, T.; Schuengel, L.; Groeneweg, L.; Narayanan, V.; Schneider-Hohendorf, T.; Gross, C.C.; Wiendl, H.; Kehrel, B.E.; Kleinschnitz, C.; Meuth, S.G.
Plasma kallikrein modulates immune cell trafficking during neuroinflammation via PAR2 and bradykinin release
Proc. Natl. Acad. Sci. USA
116
271-276
2019
Homo sapiens, Mus musculus
brenda