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Information on EC 3.4.21.34 - plasma kallikrein
for references in articles please use BRENDA:EC3.4.21.34
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.21 Serine endopeptidases
3.4.21.34 plasma kallikrein
IUBMB Comments
Formed from plasma prokallikrein (Fletcher factor) by factor XIIa. Activates coagulation factors XII, VII and plasminogen. Selective for Arg > Lys in P1, in small molecule substrates.
The enzyme appears in viruses and cellular organisms
- 3.4.21.34
- kininogens
- coagulation
- hypertension
- plasmin
- thrombin
- urine
- renin
- aprotinin
- arterial
- prostate
- plasminogen
- angiotensin
- prostaglandin
- clot
-
fibrinolysis
- glandular
-
chromogenic
- thromboplastin
-
prostate-specific
- angioedema
- fibrinogen
- aldosterone
- antithrombin
- elastase
-
submandibular
-
hageman
-
kininase
- urokinase
-
normotensive
-
high-molecular-weight
-
amidolytic
- prothrombin
-
renin-angiotensin
-
hypotensive
- captopril
-
trypsin-like
- hk2
-
2-macroglobulin
- kaolin
-
c1-inh
-
natriuresis
-
renin-angiotensin-aldosterone
-
kunitz
- c1s
- c1-inhibitor
-
hypertensives
-
esterolytic
- medicine
- pharmacology
-
2-antiplasmin
-
euglobulins
-
antifibrinolytic
Reaction Schemes
showselective cleavage of some Arg-/- and Lys-/- bonds, including Lys-/-Arg and Arg-/-Ser in (human) kininogen to release bradykinin
Synonyms
kallikrein, prekallikrein, plasma kallikrein, urinary kallikrein, kininogenase, plasma prekallikrein, plasma pk, pancreatic kallikrein, klk13, klkb1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bradykininogenase
-
-
-
-
callicrein
-
-
-
-
depot-Padutin
-
-
-
-
dilminal D
-
-
-
-
EC 3.4.21.8
-
-
formerly
-
EC 3.4.4.21
-
-
formerly, part transferred
-
Fletcher factor
-
-
-
-
glumorin
-
-
-
-
kallidinogenase
-
-
-
-
kallikrein
kallikrein I
-
-
-
-
kallikrein II
-
-
-
-
kininogenase
-
-
-
-
kininogenin
-
-
-
-
KLKb1
onokrein P
-
-
-
-
padreatin
-
-
-
-
padutin
-
-
-
-
pancreatic kallikrein
-
-
-
-
PKA
PKal
plasma PK
Plasma prekallikrein
PPK
prekallikrein
serum kallikrein
urinary kallikrein
-
-
-
-
urokallikrein
-
-
-
-
kallikrein
-
-
-
-
Plasma prekallikrein
-
-
-
-
serum kallikrein
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
selective cleavage of some Arg-/- and Lys-/- bonds, including Lys-/-Arg and Arg-/-Ser in (human) kininogen to release bradykinin
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase
-
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CAS REGISTRY NUMBER
COMMENTARY
410538-33-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
Substrates: -
Products: -
Products: -
?
2-aminobenzoyl-MISLMKRPPGFSPFRSSRI-NH2 + H2O
2-aminobenzoyl-MISLMK + RPPGFSPFRSSRI-NH2
-
Substrates: -
Products: -
Products: -
?
Ac-AGLTR-4-nitroanilide + H2O
Ac-AGLTR + 4-nitroaniline
-
Substrates: chromogenic substrate based on the C1s cleavage site in complement component C4
Products: -
Products: -
?
Ac-Phe-Arg-4-nitroanilide
Ac-Phe-Arg + 4-nitroaniline
-
Substrates: synthetic fluorogenic substrate
Products: -
Products: -
?
apelin-17 + H2O
KFR + ?
-
Substrates: the enzyme cleaves the first three N-terminal amino acids (KFR) of apelin-17
Products: -
Products: -
?
benzoyl-Pro-Phe-Arg-4-nitroanilide + H2O
benzoyl-Pro-Phe-Arg + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
ir
complement component C4 + H2O
?
-
Substrates: substrate is only cleaved in vitro, not in vivo
Products: -
Products: -
?
D-butyl-cyclohexylalanine-arginine-4-nitroanilide + H2O
D-butyl-cyclohexylalanine-arginine + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
D-Phe-Phe-Arg-4-methylcoumarin 7-amide
D-Phe-Phe-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
D-Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
D-Pro-Phe-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
D-Pro-Phe-Arg-p-nitroanilide + H2O
D-Pro-Phe-Arg + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
D-Val-Leu-Arg-4-nitroanilide + H2O
D-Val-Leu-Arg + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
factor FXII + H2O
activated factor XII + ?
Substrates: cleavage between Arg and Val
Products: -
Products: -
?
Glu-Pro-Arg-4-nitroanilide + H2O
Glu-Pro-Arg + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
H-D-Pro-Phe-Arg-4-nitroanilide + H2O
?
-
Substrates: i.e. S2302, a chromogenic substrate
Products: -
Products: -
?
ISLMKRPPGFSPFRSSR + H2O
ISLMKR + RPPGFSPFR + SSR
-
Substrates: RPPGFSPFR is bradykinin, synthetic peptide containing the internal kinin sequence, 2 cleavage sites, the C-terminal one being preferred
Products: -
Products: -
?
kininogen + H2O
heavy chain of kininogen + light chain of kininogen + bradykinin
-
Substrates: high molecular weight substrate, serine protease
Products: bradykinin is an inflammatory peptide
Products: bradykinin is an inflammatory peptide
ir
kininogen + H2O
heavy chain of kininogen + modified light chain of kininogen + bradykinin
-
Substrates: high molecular weight substrate, serine protease
Products: MW of products: 63 kDa, 45 kDa, and 13 kDa, respectively
Products: MW of products: 63 kDa, 45 kDa, and 13 kDa, respectively
?
low-molecular-weight kininogen + H2O
low-molecular-weight kinin + kallidin
-
Substrates: -
Products: kallidin is Lys-bradykinin or Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
Products: kallidin is Lys-bradykinin or Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
?
N-acetyl-Phe-Arg-4-nitroanilide + H2O
N-acetyl-Phe-Arg + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
N-benzoyl-Phe-Val-Arg-4-nitroanilide + H2O
N-benzoyl-Phe-Val-Arg + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
N-benzoyl-Pro-Phe-Arg-4-nitroanilide
N-benzoyl-Pro-Phe-Arg + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
N-benzyloxycarbonyl-Ala-Lys-Arg-4-methylcoumarin 7-amide
N-benzyloxycarbonyl-Ala-Lys-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
N-butyl-(R)-cyclohexylalanyl-L-Arg-p-nitroanilide + H2O
N-butyl-(R)-cyclohexylalanyl-L-Arg + p-nitroaniline
Substrates: i.e. Pefachrome PK
Products: -
Products: -
?
Nalpha-toluenesulfonyl-L-arginine methyl ester + H2O
Nalpha-toluenesulfonyl-L-arginine + methanol
neuropeptide Y3-36 + H2O
neuropeptide Y3-35 + L-tyrosine
-
Substrates: 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
Products: -
Products: -
?
o-aminobenzoyl-FSAPMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSAPMK + RLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
Substrates: -
Products: 18% of product formed, identification by mass spectroscopy
Products: 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
-
Substrates: -
Products: 82% of product formed, identification by mass spectroscopy
Products: 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
-
Substrates: -
Products: 35% of product formed, identification by mass spectroscopy
Products: 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
-
Substrates: -
Products: 65% of product formed, identification by mass spectroscopy
Products: 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
-
Substrates: -
Products: 71% of product formed, identification by mass spectroscopy
Products: 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
-
Substrates: -
Products: 29% of product formed, identification by mass spectroscopy
Products: 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
-
Substrates: -
Products: 52% of product formed, identification by mass spectroscopy
Products: 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
-
Substrates: -
Products: 48% of product formed, identification by mass spectroscopy
Products: 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
-
Substrates: -
Products: 28% of product formed, identification by mass spectroscopy
Products: 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
-
Substrates: -
Products: 72% of product formed, identification by mass spectroscopy
Products: 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
-
Substrates: -
Products: identification by mass spectroscopy
Products: identification by mass spectroscopy
?
o-aminobenzoyl-FSQPMKALTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQPMK + ALTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
Substrates: -
Products: identification by mass spectroscopy
Products: identification by mass spectroscopy
?
o-aminobenzoyl-FSQPMKRATLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQPMK + RATLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
Substrates: -
Products: 13% of product formed, identification by mass spectroscopy
Products: 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
-
Substrates: -
Products: 87% of product formed, identification by mass spectroscopy
Products: 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
-
Substrates: -
Products: 30% of product formed, identification by mass spectroscopy
Products: 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
-
Substrates: -
Products: 70% of product formed, identification by mass spectroscopy
Products: 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
-
Substrates: -
Products: identification by mass spectroscopy
Products: identification by mass spectroscopy
?
o-aminobenzoyl-FSQPMKRLTLANTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQPMK + RLTLANTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
Substrates: -
Products: 20% of product formed, identification by mass spectroscopy
Products: 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
-
Substrates: -
Products: 80% of product formed, identification by mass spectroscopy
Products: 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
-
Substrates: -
Products: 19% of product formed, identification by mass spectroscopy
Products: 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
-
Substrates: -
Products: 81% of product formed, identification by mass spectroscopy
Products: 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
-
Substrates: synthetic fluorogenic substrate derived from the amino acid sequence of human prorenin cleavage site
Products: identification by mass spectroscopy
Products: identification by mass spectroscopy
?
o-aminobenzoyl-GEFIKKSSFQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-GEFIK + KSSFQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
Substrates: synthetic fluorogenic substrate
Products: 67% of product formation, identification by mass spectroscopy
Products: 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
-
Substrates: synthetic fluorogenic substrate
Products: 33% of product formation, identification by mass spectroscopy
Products: 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
-
Substrates: synthetic fluorogenic substrate
Products: 62% of product formation, identification by mass spectroscopy
Products: 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
-
Substrates: synthetic fluorogenic substrate
Products: 38% of product formation, identification by mass spectroscopy
Products: 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
-
Substrates: synthetic fluorogenic substrate
Products: identification by mass spectroscopy
Products: identification by mass spectroscopy
?
o-aminobenzoyl-LGMISLMKRPPGFSPFRSSRI-NH2 + H2O
bradykinin + ?
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-VMIAALPRTMFIQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
?
-
Substrates: low activity, substrate sequence is based on the Bauhinia ungulata inhibitor protein reactive site sequence
Products: -
Products: -
?
o-aminobenzoyl-VVISALPRTMFIQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
?
-
Substrates: substrate sequence is based on the Bauhinia variegata inhibitor protein reactive site sequence
Products: -
Products: -
?
pro-hepatocyte growth factor + H2O
hepatocyte growth factor beta-chain + hepatocyte growth factor alpha-chain + 10 kDa fragment of the alpha-chain
-
Substrates: i.e. HGF, two independent cleavage sites: Arg494-Val495, kinetically preferred, and Arg424-His425, recombinant mutant HGF R424A/R494E is no substrate
Products: activation of hepatocyte growth factor
Products: activation of hepatocyte growth factor
?
pro-urokinase + H2O
urokinase + ?
-
Substrates: activation of pro-urokinase
Products: -
Products: -
?
pro-urokinase type plasminogen activator + H2O
urokinase type plasminogen activator + ?
-
Substrates: -
Products: -
Products: -
?
RPGLPVRFESPLRINIIKE + H2O
RPGLPVR + FESPLRINIIKE
-
Substrates: peptide based on the reactive site of the Bauhinia bauhinioides inhibitor protein, similar to the kinin moiety in human kininogen
Products: -
Products: -
?
RPGLPVRFESPLRINIIKE + H2O
RPGLPVRFESPLR + INIIKE
-
Substrates: peptide based on the reactive site of the Bauhinia bauhinioides inhibitor protein, similar to the kinin moiety in human kininogen
Products: main products
Products: main products
ir
Suc-AAPF-7-amido-4-methylcoumarin + H2O
Suc-AAPF + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
Transforming growth factor + H2O
?
Substrates: (TGF)-beta 1
Products: -
Products: -
?
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
ir
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
-
Substrates: synthetic fluorogenic substrate
Products: -
Products: -
?
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
-
Substrates: plasma kallikrein-selective substrate
Products: -
Products: -
?
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
factor XI + H2O
activated factor XI + ?
-
Substrates: proteolytic activation, part of the coagulation cascade
Products: -
Products: -
?
factor XI + H2O
activated factor XI + ?
-
Substrates: proteolytic activation
Products: -
Products: -
?
factor XII + H2O
?
Substrates: activation of the factor XII, bound to negatively charged surfaces
Products: -
Products: -
?, ir
factor XII + H2O
?
Substrates: activation of the factor XII, bound to negatively charged surfaces
Products: -
Products: -
?, ir
factor XII + H2O
?
Substrates: activation of the factor XII, bound to negatively charged surfaces
Products: -
Products: -
?, ir
factor XII + H2O
activated factor XII + ?
-
Substrates: proteolytic activation
Products: -
Products: -
?
high molecular weight kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: -
Products: -
Products: -
?
high molecular weight kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: -
Products: -
Products: -
?
high-molecular weight kininogen + H2O
bradykinin + ?
Substrates: -
Products: -
Products: -
?
high-molecular weight kininogen + H2O
bradykinin + ?
Substrates: -
Products: -
Products: -
?
high-molecular-weight kininogen + H2O
bradykinin + fragments of kininogen
Substrates: cleavage between Lys and Arg as wekk as Arg and Ser
Products: -
Products: -
?
high-molecular-weight kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: -
Products: -
Products: -
?
high-molecular-weight kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: -
Products: -
Products: -
?
high-molecular-weight kininogen + H2O
high-molecular-weight kinin + bradykinin
-
Substrates: pathways involving high-molecular-weight kininogen/high-molecular-weight kinin, overview
Products: bradykinin is Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
Products: bradykinin is Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
?
high-molecular-weight kininogen + H2O
high-molecular-weight kinin + bradykinin
-
Substrates: -
Products: bradykinin is Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
Products: bradykinin is Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
?
kininogen + H2O
?
-
Substrates: cleaves Lys-Arg and Arg-Ser bonds in kininogen to produce bradykinin, participates in early phase of intrinsic blood coagulation
Products: -
Products: -
?
kininogen + H2O
?
-
Substrates: cleaves Lys-Arg and Arg-Ser bonds in kininogen to produce bradykinin, participates in early phase of intrinsic blood coagulation
Products: -
Products: -
?
kininogen + H2O
bradykinin + ?
-
Substrates: cleaves Lys-Arg and Arg-Ser bonds in kininogen to produce bradykinin
Products: -
Products: -
?
kininogen + H2O
bradykinin + ?
-
Substrates: the presence of S at P1' position for bradykinin release by human plasma kallikrein appears to be essential
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragment of kininogen
-
Substrates: -
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragment of kininogen
-
Substrates: high-molecular weight substrate, serine protease
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragment of kininogen
-
Substrates: -
Products: -
Products: -
ir
kininogen + H2O
bradykinin + fragment of kininogen
-
Substrates: enzyme is a cofactor in blood coagulation and modulates inflammation through release of bradykinin
Products: -
Products: -
ir
kininogen + H2O
bradykinin + fragment of kininogen
-
Substrates: part of kallikrein-kininsystem
Products: bradykinin is a potent mediator of inflammatory response
Products: bradykinin is a potent mediator of inflammatory response
ir
kininogen + H2O
bradykinin + fragments of kininogen
Substrates: high-molecular weight kininogen
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: high-molecular weight kininogen, preferred substrate
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: low-molecular weight kininogen, low activity
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragments of kininogen
Substrates: high-molecular weight kininogen
Products: -
Products: -
ir
kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: high-molecular weight kininogen, involved in inflammatory reaction
Products: -
Products: -
ir
kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: -
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragments of kininogen
Substrates: -
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: -
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragments of kininogen
Substrates: -
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: -
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragments of kininogen
Substrates: -
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: -
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragments of kininogen
Substrates: human high-molecular weight kininogen
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragments of kininogen
Substrates: high-molecular weight kininogen
Products: -
Products: -
ir
kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: -
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragments of kininogen
Substrates: -
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragments of kininogen
Substrates: high-molecular weight kininogen
Products: -
Products: -
?, ir
kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: -
Products: -
Products: -
?
modified kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: high-molecular weight kininogen digested by human neutrophil elastase
Products: -
Products: -
?
modified kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: low-molecular weight kininogen digested by human neutrophil elastase, 26 amino acids cleaved off, is a better substrate than native low-molecular weight kininogen
Products: -
Products: -
?
modified kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: high-molecular weight kininogen digested by human neutrophil elastase
Products: -
Products: -
ir
Nalpha-Benzoyl-L-Arg ethyl ester + H2O
Nalpha-Benzoyl-L-Arg + ethanol
-
Substrates: -
Products: -
Products: -
?
Nalpha-Benzoyl-L-Arg ethyl ester + H2O
Nalpha-Benzoyl-L-Arg + ethanol
-
Substrates: -
Products: -
Products: -
?
Nalpha-toluenesulfonyl-L-arginine methyl ester + H2O
Nalpha-toluenesulfonyl-L-arginine + methanol
-
Substrates: -
Products: -
Products: -
?
Nalpha-toluenesulfonyl-L-arginine methyl ester + H2O
Nalpha-toluenesulfonyl-L-arginine + methanol
-
Substrates: -
Products: -
Products: -
?
plasminogen + H2O
plasmin + ?
-
Substrates: activation of plasminogen
Products: -
Products: -
ir
plasminogen + H2O
plasmin + ?
-
Substrates: proteolytic activation
Products: -
Products: -
?
Prorenin + H2O
Renin + ?
-
Substrates: activation of human prorenin
Products: -
Products: -
ir
Prorenin + H2O
Renin + ?
Substrates: activation of prorenin
Products: -
Products: -
ir
Prorenin + H2O
Renin + ?
Substrates: activation of prorenin, involved in the renin-angiotensin system
Products: -
Products: -
ir
Prorenin + H2O
Renin + ?
Substrates: activation of prorenin
Products: -
Products: -
ir
Prorenin + H2O
Renin + ?
Substrates: activation of prorenin, involved in the renin-angiotensin system
Products: -
Products: -
ir
Prorenin + H2O
Renin + ?
Substrates: activation of prorenin
Products: -
Products: -
ir
Prorenin + H2O
Renin + ?
-
Substrates: rat prorenin, very low activity
Products: -
Products: -
ir
Prorenin + H2O
Renin + ?
Substrates: activation of prorenin, involved in the renin-angiotensin system
Products: -
Products: -
ir
additional information
?
-
-
Substrates: overexpression of prolylcarboxypeptidase in CHO cells enhances plasma prekallikrein activation
Products: -
Products: -
?
additional information
?
-
Substrates: belongs to the peptidase family S1, plasma kallikrein subfamily
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity requirements
Products: -
Products: -
?
additional information
?
-
-
Substrates: based on the reactive site sequence of Bauhinia ungulata Xa inhibitor peptides
Products: -
Products: -
?
additional information
?
-
Substrates: defects in gene KLKB1 cause Fletcher factor deficiency, a blood coagulation defect
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme activity is enhanced in orthotopic liver transplant recipients
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in inflammatory processes via hydrolysis of complement
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in plasma and vascular fibrinolytic activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is part of the kallikrein-kininogen-kinin system, KKS, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme involved in intrinsic blood clotting, the kallikrein-kinin system and fibrinolysis
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: kininogen domain structure, overview
Products: -
Products: -
?
additional information
?
-
Substrates: peptides with Pro at P2 are poor substrates
Products: -
Products: -
?
additional information
?
-
Substrates: belongs to the peptidase family S1, plasma kallikrein subfamily
Products: -
Products: -
?
additional information
?
-
-
Substrates: active plasma kallikrein localizes to mast cells and regulates epithelial cell apoptosis, adipocyte differentiation and stromal remodeling during mammary gland involution
Products: -
Products: -
?
additional information
?
-
Substrates: plasma prekallikrein conversion of the commercial chromogenic substrate S-2302 is monitored in the chromogenic enzyme assay
Products: -
Products: -
-
additional information
?
-
Substrates: plasma prekallikrein conversion of the commercial chromogenic substrate S-2302 is monitored in the chromogenic enzyme assay
Products: -
Products: -
-
additional information
?
-
Substrates: belongs to the peptidase family S1, plasma kallikrein subfamily
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: may play a role in invasion of the host immune response
Products: -
Products: -
?
additional information
?
-
-
Substrates: based on the reactive site sequence of Bauhinia ungulata Xa inhibitor peptides
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
factor FXII + H2O
activated factor XII + ?
Substrates: cleavage between Arg and Val
Products: -
Products: -
?
kininogen + H2O
heavy chain of kininogen + light chain of kininogen + bradykinin
-
Substrates: high molecular weight substrate, serine protease
Products: bradykinin is an inflammatory peptide
Products: bradykinin is an inflammatory peptide
ir
low-molecular-weight kininogen + H2O
low-molecular-weight kinin + kallidin
-
Substrates: -
Products: kallidin is Lys-bradykinin or Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
Products: kallidin is Lys-bradykinin or Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
?
modified kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: high-molecular weight kininogen digested by human neutrophil elastase
Products: -
Products: -
ir
pro-urokinase type plasminogen activator + H2O
urokinase type plasminogen activator + ?
-
Substrates: -
Products: -
Products: -
?
Transforming growth factor + H2O
?
Substrates: (TGF)-beta 1
Products: -
Products: -
?
factor XI + H2O
activated factor XI + ?
-
Substrates: proteolytic activation, part of the coagulation cascade
Products: -
Products: -
?
factor XI + H2O
activated factor XI + ?
-
Substrates: proteolytic activation
Products: -
Products: -
?
factor XII + H2O
?
Substrates: activation of the factor XII, bound to negatively charged surfaces
Products: -
Products: -
ir
factor XII + H2O
?
Substrates: activation of the factor XII, bound to negatively charged surfaces
Products: -
Products: -
ir
factor XII + H2O
?
Substrates: activation of the factor XII, bound to negatively charged surfaces
Products: -
Products: -
ir
factor XII + H2O
activated factor XII + ?
-
Substrates: proteolytic activation
Products: -
Products: -
?
high molecular weight kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: -
Products: -
Products: -
?
high molecular weight kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: -
Products: -
Products: -
?
high-molecular weight kininogen + H2O
bradykinin + ?
Substrates: -
Products: -
Products: -
?
high-molecular weight kininogen + H2O
bradykinin + ?
Substrates: -
Products: -
Products: -
?
high-molecular-weight kininogen + H2O
bradykinin + fragments of kininogen
Substrates: cleavage between Lys and Arg as wekk as Arg and Ser
Products: -
Products: -
?
high-molecular-weight kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: -
Products: -
Products: -
?
high-molecular-weight kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: -
Products: -
Products: -
?
high-molecular-weight kininogen + H2O
high-molecular-weight kinin + bradykinin
-
Substrates: pathways involving high-molecular-weight kininogen/high-molecular-weight kinin, overview
Products: bradykinin is Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
Products: bradykinin is Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
?
high-molecular-weight kininogen + H2O
high-molecular-weight kinin + bradykinin
-
Substrates: -
Products: bradykinin is Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
Products: bradykinin is Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
?
kininogen + H2O
?
-
Substrates: cleaves Lys-Arg and Arg-Ser bonds in kininogen to produce bradykinin, participates in early phase of intrinsic blood coagulation
Products: -
Products: -
?
kininogen + H2O
?
-
Substrates: cleaves Lys-Arg and Arg-Ser bonds in kininogen to produce bradykinin, participates in early phase of intrinsic blood coagulation
Products: -
Products: -
?
kininogen + H2O
bradykinin + ?
-
Substrates: the presence of S at P1' position for bradykinin release by human plasma kallikrein appears to be essential
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragment of kininogen
-
Substrates: -
Products: -
Products: -
ir
kininogen + H2O
bradykinin + fragment of kininogen
-
Substrates: enzyme is a cofactor in blood coagulation and modulates inflammation through release of bradykinin
Products: -
Products: -
ir
kininogen + H2O
bradykinin + fragment of kininogen
-
Substrates: part of kallikrein-kininsystem
Products: bradykinin is a potent mediator of inflammatory response
Products: bradykinin is a potent mediator of inflammatory response
ir
kininogen + H2O
bradykinin + fragments of kininogen
Substrates: high-molecular weight kininogen
Products: -
Products: -
ir
kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: high-molecular weight kininogen, involved in inflammatory reaction
Products: -
Products: -
ir
kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: -
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragments of kininogen
Substrates: -
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: -
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragments of kininogen
Substrates: -
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: -
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragments of kininogen
Substrates: -
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: -
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragments of kininogen
Substrates: high-molecular weight kininogen
Products: -
Products: -
ir
kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: -
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragments of kininogen
Substrates: -
Products: -
Products: -
?
kininogen + H2O
bradykinin + fragments of kininogen
Substrates: high-molecular weight kininogen
Products: -
Products: -
ir
kininogen + H2O
bradykinin + fragments of kininogen
-
Substrates: -
Products: -
Products: -
?
Prorenin + H2O
Renin + ?
Substrates: activation of prorenin, involved in the renin-angiotensin system
Products: -
Products: -
ir
Prorenin + H2O
Renin + ?
Substrates: activation of prorenin, involved in the renin-angiotensin system
Products: -
Products: -
ir
Prorenin + H2O
Renin + ?
Substrates: activation of prorenin, involved in the renin-angiotensin system
Products: -
Products: -
ir
additional information
?
-
-
Substrates: overexpression of prolylcarboxypeptidase in CHO cells enhances plasma prekallikrein activation
Products: -
Products: -
?
additional information
?
-
Substrates: defects in gene KLKB1 cause Fletcher factor deficiency, a blood coagulation defect
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme activity is enhanced in orthotopic liver transplant recipients
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in inflammatory processes via hydrolysis of complement
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in plasma and vascular fibrinolytic activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is part of the kallikrein-kininogen-kinin system, KKS, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme involved in intrinsic blood clotting, the kallikrein-kinin system and fibrinolysis
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: active plasma kallikrein localizes to mast cells and regulates epithelial cell apoptosis, adipocyte differentiation and stromal remodeling during mammary gland involution
Products: -
Products: -
?
additional information
?
-
Substrates: may play a role in invasion of the host immune response
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R)-N2-[5-[1-amino-3-cyclopropyl-1-(pyridin-2-yl)propyl]-2-fluorophenyl]-N1-(5-chloropyridin-2-yl)-4,4-difluoropyrrolidine-1,2-dicarboxamide
-
(2R,4R)-N2-[5-[1-amino-1-(4-cyanopyridin-2-yl)-3-cyclopropylpropyl]-2-fluorophenyl]-N1-(5-chloropyridin-2-yl)-4-methoxypyrrolidine-1,2-dicarboxamide
-
(2R,4R)-N2-[5-[1-amino-3-cyclopropyl-1-(pyridin-2-yl)propyl]-2-fluorophenyl]-N1-(4-chlorophenyl)-4-ethoxypyrrolidine-1,2-dicarboxamide
-
(2R,4R)-N2-[5-[1-amino-3-cyclopropyl-1-(pyridin-2-yl)propyl]-2-fluorophenyl]-N1-(4-chlorophenyl)-4-hydroxypyrrolidine-1,2-dicarboxamide
-
(2R,4R)-N2-[5-[1-amino-3-cyclopropyl-1-(pyridin-2-yl)propyl]-2-fluorophenyl]-N1-(4-chlorophenyl)-4-methoxypyrrolidine-1,2-dicarboxamide
-
(2R,4R)-N2-[5-[1-amino-3-cyclopropyl-1-(pyridin-2-yl)propyl]-2-fluorophenyl]-N1-(5-chloropyridin-2-yl)-4-methoxypyrrolidine-1,2-dicarboxamide
-
(2R,4S)-N2-[5-[1-amino-3-cyclopropyl-1-(pyridin-2-yl)propyl]-2-fluorophenyl]-N1-(4-chlorophenyl)-4-hydroxy-4-phenylpyrrolidine-1,2-dicarboxamide
-
1-(1-aminoisoquinolin-7-yl)-N-(5-[[(cyclopropylmethyl)amino](phenyl)methyl]-2-fluorophenyl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-(3-carbamimidoylphenyl)-N-(5-[[(cyclopropylmethyl)amino](phenyl)methyl]-2-fluorophenyl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-(3-cyanophenyl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxylic acid
-
1-benzyl-1H-pyrazole-4-carboxylic acid 4-carbamimidoyl-benzylamide
-
ASP-440, small molecule inhibitor of plasma kallikrein
1-[3-(aminomethyl)phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxylic acid
-
1-[3-(aminomethyl)phenyl]-N-(2-fluorophenyl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-(3-fluoro-4'-sulfamoyl[1,1'-biphenyl]-4-yl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-(3-fluoro[1,1'-biphenyl]-4-yl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-(4'-carbamoyl-3-fluoro[1,1'-biphenyl]-4-yl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-(4-cyclopropyl-2-fluorophenyl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-(5-[(3-cyanophenyl)[(cyclopropylmethyl)amino]methyl]-2-fluorophenyl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-(5-[(4-cyanophenyl)[(cyclopropylmethyl)amino]methyl]-2-fluorophenyl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-(5-[(S)-(3-cyanophenyl)[(cyclopropylmethyl)amino]methyl]-2-fluorophenyl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-(5-[[(cyclopropylmethyl)amino](phenyl)methyl]-2-fluorophenyl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
1-[3-(aminomethyl)phenyl]-N-(5-[[(cyclopropylmethyl)amino](pyridin-2-yl)methyl]-2-fluorophenyl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-(5-[[(cyclopropylmethyl)amino](pyridin-3-yl)methyl]-2-fluorophenyl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-(5-[[(cyclopropylmethyl)amino](pyridin-4-yl)methyl]-2-fluorophenyl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-([1,1'-biphenyl]-4-yl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-phenyl-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-[2-fluoro-3-[hydroxy(phenyl)methyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-[2-fluoro-4-(piperidin-1-yl)phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
7.5% inihibition at 0.005 mM
1-[3-(aminomethyl)phenyl]-N-[2-fluoro-4-[hydroxy(phenyl)methyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-[2-fluoro-5-[hydroxy(phenyl)methyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-[2-fluoro-5-[methoxy(phenyl)methyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-[3-fluoro-3'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-[3-[(cyclopropylmethoxy)(phenyl)methyl]-2-fluorophenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-[3-[(cyclopropylmethoxy)(phenyl)methyl]-4-fluorophenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-[3-[(cyclopropylmethoxy)(phenyl)methyl]-5-fluorophenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-[3-[(cyclopropylmethoxy)(phenyl)methyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
1-[3-(aminomethyl)phenyl]-N-[3-[hydroxy(phenyl)methyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-[3-[phenyl(propoxy)methyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-[4-[(cyclopropylmethoxy)(phenyl)methyl]-2-fluorophenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-[5-[(3-aminophenyl)(cyclopropylmethoxy)methyl]-2-fluorophenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-[5-[(cyclopropylmethoxy)(2-hydroxyphenyl)methyl]-2-fluorophenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-[5-[(cyclopropylmethoxy)(phenyl)methyl]-2-fluorophenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
1-[3-(aminomethyl)phenyl]-N-[5-[(R)-[(cyclopropylmethyl)amino](phenyl)methyl]-2-fluorophenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-[5-[(S)-[(cyclopropylmethyl)amino](phenyl)methyl]-2-fluorophenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-[5-[ethoxy(phenyl)methyl]-2-fluorophenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N5-(5-[[(cyclopropylmethyl)amino](phenyl)methyl]-2-fluorophenyl)-1H-pyrazole-3,5-dicarboxamide
-
2-methylpropyl 4-([N2-[4-(aminomethyl)cyclohexane-1-carbonyl]-L-arginyl]amino)benzoate
-
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
-
-
3-amino-1-methyl-15-[(1H-pyrazol-1-yl)methyl]-7,10,11,12,24,25-hexahydro-6H,18H,23H-19,22-(metheno)pyrido[4,3-j][1,9,13,17,18]benzodioxatriazacyclohenicosin-23-one
-
3-amino-N-[(3R)-1-(3-chlorophenyl)pyrrolidin-3-yl]-1-([4-[(5-fluoro-2-oxopyridin-1(2H)-yl)methyl]phenyl]methyl)-1H-pyrazole-4-carboxamide
-
3-amino-N-[(3S)-1-(3-chlorophenyl)pyrrolidin-3-yl]-1-([4-[(5-fluoro-2-oxopyridin-1(2H)-yl)methyl]phenyl]methyl)-1H-pyrazole-4-carboxamide
-
3-amino-N-[(6-amino-2,4-dimethylpyridin-3-yl)methyl]-1-([4-[(3,5-dimethyl-1H-pyrazol-1-yl)methyl]phenyl]methyl)-1H-pyrazole-4-carboxamide
-
3-amino-N-[2-(3-chlorophenoxy)ethyl]-1-([4-[(2-oxopyridin-1(2H)-yl)methyl]phenyl]methyl)-1H-pyrazole-4-carboxamide
-
3-amino-N-[2-(3-chlorophenoxy)ethyl]-1-([4-[(5-fluoro-2-oxopyridin-1(2H)-yl)methyl]phenyl]methyl)-1H-pyrazole-4-carboxamide
-
5-[[(1-[5-[(3-chloroquinolin-6-yl)methyl]pyridin-3-yl]ethenyl)amino]methyl]-4,6-dimethylpyridin-2-amine
-
ACiNTWNPWCiiPWDAPLCiiiA
cyclized on Ci, Cii, Ciii by 1,3,5 trismethylbenzene
-
ACiNTWNPWCiiPWDAPLCiiiA cyclized on Ci, Cii, Ciii by 1,3,5 trismethylbenzene
-
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
-
antithrombin
-
inhibition by antithrombin is 3.4fold improved by heparin, forming a ternary complex with antithrombin
-
Bauhinia bauhinioides Kunitz-type serine protease inhibitor
BbKI or BbTI-II, recombinant protein expressed in Escherichia coli Rosetta 2 (DE3) as His6-MBP-TEV-BbKI construct, the MBP tag is cleaved off. An 18 kDa protein originally isolated from the seeds of Bauhinia bauhinioides. The protein is a potent inhibitor of the trypsin-like plasma kallikrein, but also a potent inhibitor of human tissue kallikrein 4 (KLK4) and the chymotrypsin-like human tissue kallikrein 7 (KLK7). Modeling of structures of BbKI complexed with the catalytic domain of human plasma kallikrein, andn with KLK4 and KLK7, structure comparisons and interaction analysis, overview. Competitive inhibition
-
Bauhinia bauhinioides Kunitz-type serine protease inhibitor mutant L55R
recombinant protein expressed in Escherichia coli Rosetta 2 (DE3) as His6-MBP-TEV-BbKI construct, the MBP tag is cleaved off. Modeling of structures of BbKI mutant complexed with the catalytic domain of human plasma kallikrein, andn with KLK4 and KLK7, structure comparisons and interaction analysis, overview
-
berotralstat
BCX7353, a potent, selective, and oral plasma kallikrein inhibitor to prevent attacks of hereditary angioedema (HAE)
bicyclic peptide Ac-CiS1F2[Aze]3Y4[HArg]5Cii[Ala(PsiCH2-NH)]6H7Q8D9L10Ciii
-
-
-
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
-
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
-
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
-
N-alpha-tosyl-D,L-homophenylalanine-4-anilide hydrochloride
-
also known as Pefabloc PK, inhibits plasma kallikrein exclusively
N-benzoyl-3-cyclohexyl-D-alanyl-N-[[4-(aminomethyl)phenyl]methyl]-L-phenylalaninamide
-
N-benzoyl-O-ethyl-D-tyrosyl-(betaR)-N-[[4-(aminomethyl)phenyl]methyl]-beta-hydroxy-L-phenylalaninamide
-
N-[(1-amino-5-methylisoquinolin-6-yl)methyl]-3-(methoxymethyl)-1-([4-[(1H-pyrazol-1-yl)methyl]phenyl]methyl)-1H-pyrazole-4-carboxamide
-
N-[(2-fluoro-3,6-dimethoxyphenyl)methyl]-3-(methoxymethyl)-1-([4-[(2-oxopyridin-1(2H)-yl)methyl]phenyl]methyl)-1H-pyrazole-4-carboxamide
-
N-[(3-chloro-1H-pyrrolo[2,3-b]pyridin-5-yl)methyl]-3-(methoxymethyl)-1-([4-[(4-methyl-1H-pyrazol-1-yl)methyl]phenyl]methyl)-1H-pyrazole-4-carboxamide
-
N-[(3-chloro-1H-pyrrolo[2,3-b]pyridin-5-yl)methyl]-3-cyano-1-([4-[(4-methyl-1H-pyrazol-1-yl)methyl]phenyl]methyl)-1H-pyrazole-4-carboxamide
-
N-[(3-chloro-1H-pyrrolo[2,3-b]pyridin-5-yl)methyl]-5-([3-(methanesulfonyl)-4-[(2-oxopyridin-1(2H)-yl)methyl]phenyl]methyl)pyridine-3-carboxamide
-
N-[(3-chloro-4-fluoro-1H-indol-5-yl)methyl]-8-[(3-chloroquinolin-6-yl)methyl]-7H-purin-6-amine
-
N-[(3-chloro-6-fluoro-1H-indol-5-yl)methyl]-8-[(3-chloroquinolin-6-yl)methyl]-7H-purin-6-amine
-
N-[(3-chloro-6-fluoro-1H-indol-5-yl)methyl]-8-[[3-(trifluoromethyl)quinolin-6-yl]methyl]-7H-purin-6-amine
-
N-[(3-fluoro-4-methoxypyridin-2-yl)methyl]-1-([4-[(2-oxopyridin-1(2H)-yl)methyl]phenyl]methyl)-3-(trifluoromethyl)-1H-pyrazole-4-carboxamide
-
N-[(3-fluoro-4-methoxypyridin-2-yl)methyl]-1-([4-[(5-fluoro-2-oxopyridin-1(2H)-yl)methyl]phenyl]methyl)-3-(methoxymethyl)-1H-pyrazole-4-carboxamide
-
N-[(5-chloro-1H-indazol-3-yl)methyl]-8-[(3-chloroquinolin-6-yl)methyl]-7H-purin-6-amine
-
N-[(6-amino-2,4-dimethylpyridin-3-yl)methyl]-1-([4-[(1H-pyrazol-1-yl)methyl]phenyl]methyl)-1H-imidazole-4-carboxamide
-
N-[(6-amino-2,4-dimethylpyridin-3-yl)methyl]-1-([4-[(1H-pyrazol-1-yl)methyl]phenyl]methyl)-1H-pyrazole-4-carboxamide
-
N-[(6-amino-2,4-dimethylpyridin-3-yl)methyl]-1-[(4-phenoxyphenyl)methyl]-1H-imidazole-4-carboxamide
-
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
N-[(6-amino-2,4-dimethylpyridin-3-yl)methyl]-1-[[4-(benzyloxy)phenyl]methyl]-1H-pyrazole-4-carboxamide
-
N-[(6-amino-2,4-dimethylpyridin-3-yl)methyl]-5-([3-(methanesulfonyl)-4-[(2-oxopyridin-1(2H)-yl)methyl]phenyl]methyl)pyridine-3-carboxamide
-
N-[(6-amino-2,4-dimethylpyridin-3-yl)methyl]-8-[[3-(trifluoromethyl)quinolin-6-yl]methyl]-7H-purin-6-amine
-
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
O-ethyl-N-(3-methyl-1H-pyrrole-2-carbonyl)-D-tyrosyl-N-[[4-(aminomethyl)phenyl]methyl]-L-phenylalaninamide
-
O-ethyl-N-(3-methylthiophene-2-carbonyl)-D-tyrosyl-N-[[4-(aminomethyl)phenyl]methyl]-L-phenylalaninamide
-
O-ethyl-N-propanoyl-D-tyrosyl-N-[[4-(aminomethyl)phenyl]methyl]-L-phenylalaninamide
-
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(Tra)-Lys-4-methoxy-carbonylanilide
-
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
-
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
-
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%
-
Zn2+
-
inhibits the activation of prekallikrein at concentrations above 0.01 mM, regulatory role
1-[3-(aminomethyl)phenyl]-N-(5-[[(cyclopropylmethyl)amino](phenyl)methyl]-2-fluorophenyl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-(5-[[(cyclopropylmethyl)amino](phenyl)methyl]-2-fluorophenyl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-[3-[(cyclopropylmethoxy)(phenyl)methyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-[3-[(cyclopropylmethoxy)(phenyl)methyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-[5-[(cyclopropylmethoxy)(phenyl)methyl]-2-fluorophenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
1-[3-(aminomethyl)phenyl]-N-[5-[(cyclopropylmethoxy)(phenyl)methyl]-2-fluorophenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
Aprotinin
besides PKal, aprotinin inhibits glandular kallikrein, plasmin, trypsin and tissue kallikrein
Aprotinin
besides PKal, aprotinin inhibits glandular kallikrein, plasmin, trypsin and tissue kallikrein. No inhibition by N-[(6-amino-2,4-dimethylpyridin-3-yl)methyl]-1-([4-[(1H-pyrazol-1-yl)methyl]phenyl]methyl)-1H-pyrazole-4-carboxamide, 1-benzyl-N-[(4-carbamimidoylphenyl)methyl]-1H-pyrazole-4-carboxamide, 3-amino-N-[(6-amino-2,4-dimethylpyridin-3-yl)methyl]-1-([4-[(3,5-dimethyl-1H-pyrazol-1-yl)methyl]phenyl]methyl)-1H-pyrazole-4-carboxamide, N-[(3-fluoro-4-methoxypyridin-2-yl)methyl]-1-([4-[(2-oxopyridin-1(2H)-yl)methyl]phenyl]methyl)-3-(trifluoromethyl)-1H-pyrazole-4-carboxamide, N-[(3-fluoro-4-methoxypyridin-2-yl)methyl]-1-([4-[(5-fluoro-2-oxopyridin-1(2H)-yl)methyl]phenyl]methyl)-3-(methoxymethyl)-1H-pyrazole-4-carboxamide, 3-amino-1-methyl-15-[(1H-pyrazol-1-yl)methyl]-7,10,11,12,24,25-hexahydro-6H,18H,23H-19,22-(metheno)pyrido[4,3-j][1,9,13,17,18]benzodioxatriazacyclohenicosin-23-one, and 3-amino-1-methyl-15-[(1H-pyrazol-1-yl)methyl]-7,10,11,12,24,25-hexahydro-6H,18H,23H-19,22-(metheno)pyrido[4,3-j][1,9,13,17,18]benzodioxatriazacyclohenicosin-23-one
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
-
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
-
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
-
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
-
additional information
roles of PKal in various biological systems or pathways and the development of PKal inhibitors, structure-activity relationship (SAR) and selectivity, overview
-
additional information
structure-guided inhibitor design, overview. Structure-activity relationships: substitutions on the C ring
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dermatan sulfate
-
dermatan sulfate induces contact activation and activates plasma kallikrein-mediated cleavage of factor H
kininogen
-
dependent on in vivo, high molecular weight, in complex with prekallikrein
-
Zn2+
-
prekallikrein, required, optimal activation on cells at 0.008 mM, activation range 0.005-0.01 mM, higher concentration inhibit, regulatory role
Factor XII
role of Factor XII in activating the plasma kallikrein-kinin system (KKS), the mechanism of activity and control in the KKS, and the function of high-molecular weight kininogen (HK) on contact activation proteins on cell membranes, overview
-
factor XIIa
activation by cleavage into light- and heavy-chain, that are linked by one or more disulfide bridges after cleavage
-
factor XIIa
the activated factor XII cleaves the enzyme proform Pk to activated form Pka
-
factor XIIa
role of Factor XIIa (activated factor XII) in activating the plasma kallikrein-kinin system (KKS), the mechanism of activity and control in the KKS, and the function of high-molecular weight kininogen (HK) on contact activation proteins on cell membranes, overview
-
factor XIIa
activation by cleavage into light- and heavy-chain, that are linked by one or more disulfide bridges after cleavage
-
factor XIIa
the activated factor XII cleaves the enzyme proform Pk to activated form Pka
-
factor XIIa
activation by cleavage into light- and heavy-chain, that are linked by one or more disulfide bridges after cleavage
-
additional information
-
the proform plasma kallikrein (PK) is cleaved generating the active form PKa. The american alligator possesses a factor FXII and a high-molecular weight kininogen (BK), but no FXI
-
additional information
binding to negatively charged surfaces activates the enzyme
-
additional information
-
prekallikrein activation mechanism, in vitro activated when expose to artificial negatively charged surfaces, in vivo activated as prekallikrein/kininogen complex by an antipain sensitive protease
-
additional information
-
activation of prekallikrein to active kallikrein proceeds via hydrolysis of the bond Arg371-Ile372 leading to formation of 2 chains connected via 2 disulfide bonds
-
additional information
-
mesothelial cells activate the plasma kallikrein-kinin system during pleural inflammation
-
additional information
-
transformed lung epithelial cells express urokinase plasminogen activator receptor, cytokeratin 1 and gC1qR, and assembly of the kininogen-plasma prekallikrein complex on both transformed cell lines and primary human bronchial epithelial cells results in the formation of plasma kallikrein and liberation of bradykinin from kininogen
-
additional information
-
prekallikrein proteolysis/activation is influenced by H-kininogen/glycosaminoglycans assembly and controls plasma kallikrein activity
-
additional information
once adhered to negatively charged surfaces such as collagen fibers (plaque rupture) or platelet polyphosphates released from platelet storage granules upon activation or glass, a small amount of FXII is activated to form alpha-FXIIa which further converts plasma prekallikrein (PPK) to PKal. In addition, on the surface of endothelial cells, PPK is rapidly activated to PKal by prolylcarboxypeptidase (PRCP, an endothelial cell surface activator of PPK) or heat shock protein 90
-
additional information
the proform plasma kallikrein (PK) is cleaved generating the active form PKa. The catfish possesses a factor FXI, but no FXII or high-molecular weight kininogen (BK)
-
additional information
Latimeria sp.
-
the proform plasma kallikrein (PK) is cleaved generating the active form PKa. The Coelacanth possesses a factor high-molecular weight kininogen (BK), but no FXII or FXI
-
additional information
the proform plasma kallikrein (PK) is cleaved generating the active form PKa. The opossum possesses a factor FXI, a FXII, and a high-molecular weight kininogen (BK)
-
additional information
binding to negatively charged surfaces activates the enzyme
-
additional information
plasma pKal is activated by particulate matter (PM), PM2.5, and the activated Kal plays an important role in PM2.5-induced lung injury. Ambient PM2.5 is collected and concentrated using a versatile aerosol concentration enrichment system. A teflon filter (47mm diameter) is used to collect ambient PM2.5 at 10 l/min air flow rate. Collected PM mass concentrations are determined gravimetrically using a microbalance in a room with controlled temperature and humidity. PM2.5 induces Kal activation, HK cleavage and BK release in vitro
-
additional information
-
the proform plasma kallikrein (PK) is cleaved generating the active form PKa. The duck-billed platypus possesses a factor FXII and a high-molecular weight kininogen (BK), but no FXI
-
additional information
-
the proform plasma kallikrein (PK) is cleaved generating the active form PKa. The west african lung fish possesses a factor FXII and a high-molecular weight kininogen (BK), but no FXI
-
additional information
binding to negatively charged surfaces activates the enzyme
-
additional information
the proform plasma kallikrein (PK) is cleaved generating the active form PKa. The african clawed frog possesses a factor FXII and a high-molecular weight kininogen (BK), but no FXI
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0049
2-aminobenzoic acid-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C
0.0045
o-aminobenzoyl-FSAPMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
0.012
o-aminobenzoyl-FSQAMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
0.0033
o-aminobenzoyl-FSQFMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
0.005
o-aminobenzoyl-FSQGMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
0.0018
o-aminobenzoyl-FSQPAKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
0.008
o-aminobenzoyl-FSQPMARLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
0.0022
o-aminobenzoyl-FSQPMKRATLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
0.0007
o-aminobenzoyl-FSQPMKRLALGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
0.001
o-aminobenzoyl-FSQPMKRLTAGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
0.0013
o-aminobenzoyl-FSQPMKRLTLANTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
0.0027
o-aminobenzoyl-FSQPMKRLTLGATTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
0.0117
o-aminobenzoyl-FSQPMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
0.00043
o-aminobenzoyl-VMIAALPRTMFIQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
0.00142
o-aminobenzoyl-VVISALPRTMFIQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
0.091
D-butyl-cyclohexylalanine-arginine-4-nitroanilide
catalytic domain expressed after mutagenizing three asparagines to glutamate in a baculovirus/Sf9 system
-
0.108
D-butyl-cyclohexylalanine-arginine-4-nitroanilide
full-length kallikrein
-
0.117
D-butyl-cyclohexylalanine-arginine-4-nitroanilide
protease domain in Pichia pastoris as a heterologously glycosylated zymogen that is activated by limited trypsin digestion and treated with endoglycosidase H deglycosidase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
2-aminobenzoic acid-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C
46.2
o-aminobenzoyl-FSAPMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
192
o-aminobenzoyl-FSQAMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
90
o-aminobenzoyl-FSQFMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
480
o-aminobenzoyl-FSQGMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
18
o-aminobenzoyl-FSQPAKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
48
o-aminobenzoyl-FSQPMARLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
72
o-aminobenzoyl-FSQPMKRATLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
42
o-aminobenzoyl-FSQPMKRLALGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
18
o-aminobenzoyl-FSQPMKRLTAGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
3 - 6
o-aminobenzoyl-FSQPMKRLTLANTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
60
o-aminobenzoyl-FSQPMKRLTLGATTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
60
o-aminobenzoyl-FSQPMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
0.01
o-aminobenzoyl-VMIAALPRTMFIQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
3.13
o-aminobenzoyl-VVISALPRTMFIQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
3.66
o-aminobenzoyl-VVISALPRTMFIQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00005
(2R)-N2-[5-[1-amino-3-cyclopropyl-1-(pyridin-2-yl)propyl]-2-fluorophenyl]-N1-(5-chloropyridin-2-yl)-4,4-difluoropyrrolidine-1,2-dicarboxamide
above, pH and temperature not specified in the publication
0.00005
(2R,4R)-N2-[5-[1-amino-1-(4-cyanopyridin-2-yl)-3-cyclopropylpropyl]-2-fluorophenyl]-N1-(5-chloropyridin-2-yl)-4-methoxypyrrolidine-1,2-dicarboxamide
above, pH and temperature not specified in the publication
0.00005
(2R,4R)-N2-[5-[1-amino-3-cyclopropyl-1-(pyridin-2-yl)propyl]-2-fluorophenyl]-N1-(4-chlorophenyl)-4-ethoxypyrrolidine-1,2-dicarboxamide
above, pH and temperature not specified in the publication
0.00005
(2R,4R)-N2-[5-[1-amino-3-cyclopropyl-1-(pyridin-2-yl)propyl]-2-fluorophenyl]-N1-(4-chlorophenyl)-4-hydroxypyrrolidine-1,2-dicarboxamide
above, pH and temperature not specified in the publication
0.00005
(2R,4R)-N2-[5-[1-amino-3-cyclopropyl-1-(pyridin-2-yl)propyl]-2-fluorophenyl]-N1-(4-chlorophenyl)-4-methoxypyrrolidine-1,2-dicarboxamide
above, pH and temperature not specified in the publication
0.00005
(2R,4R)-N2-[5-[1-amino-3-cyclopropyl-1-(pyridin-2-yl)propyl]-2-fluorophenyl]-N1-(5-chloropyridin-2-yl)-4-methoxypyrrolidine-1,2-dicarboxamide
above, pH and temperature not specified in the publication
0.00005
(2R,4S)-N2-[5-[1-amino-3-cyclopropyl-1-(pyridin-2-yl)propyl]-2-fluorophenyl]-N1-(4-chlorophenyl)-4-hydroxy-4-phenylpyrrolidine-1,2-dicarboxamide
above, pH and temperature not specified in the publication
0.00005
1-[3-(aminomethyl)phenyl]-N-[3-[hydroxy(phenyl)methyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
above, pH and temperature not specified in the publication
0.00005
1-[3-(aminomethyl)phenyl]-N-[3-[phenyl(propoxy)methyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
above, pH and temperature not specified in the publication
0.000006
2-[3'-acetyl-5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxybiphenyl-3-yl]butanedioic acid
-
-
0.000013
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-2',6-dihydroxybiphenyl-3-yl]butanedioic acid
-
-
0.000012
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-2'-fluoro-6-hydroxybiphenyl-3-yl]butanedioic acid
-
-
0.000003
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-3',6-dihydroxybiphenyl-3-yl]butanedioic acid
-
-
0.0000005
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-3'-carbamoyl-6-hydroxybiphenyl-3-yl]butanedioic acid
-
-
0.000003 - 0.000065
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-3'-chloro-6-hydroxybiphenyl-3-yl]butanedioic acid
0.00001
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-3'-cyano-6-hydroxybiphenyl-3-yl]butanedioic acid
-
-
0.000037
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-4'-chloro-6-hydroxybiphenyl-3-yl]butanedioic acid
-
-
0.000006
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-2'-methoxybiphenyl-3-yl]butanedioic acid
-
-
0.000006
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-2'-methylbiphenyl-3-yl]butanedioic acid
-
-
0.000005
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-3'-methoxybiphenyl-3-yl]butanedioic acid
-
-
0.000004
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-3'-methylbiphenyl-3-yl]butanedioic acid
-
-
0.000027
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-4'-methoxybiphenyl-3-yl]butanedioic acid
-
-
0.000018
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-4'-methylbiphenyl-3-yl]butanedioic acid
-
-
0.0000008
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxybiphenyl-3-yl]butanedioic acid
-
-
1
Ac-CiSF[Aze]Y[HArg]CiiVYYPDICiiiA-Sar3-[d-Arg]2)
above, pH and temperature not specified in the publication
0.00000015
AcCiNTWNPWCiiPWDAPLCiiiA-Sar3-[D-Arg]2
pH and temperature not specified in the publication
0.00000007
ACiNTWNPWCiiPWDAPLCiiiA cyclized on Ci, Cii, Ciii by 1,3,5 trismethylbenzene
pH and temperature not specified in the publication
0.0000129
Bauhinia bauhinioides Kunitz-type serine protease inhibitor
pH 8.0, temperature not specified in the publication
-
0.0000144
Bauhinia bauhinioides Kunitz-type serine protease inhibitor mutant L55R
pH 8.0, temperature not specified in the publication
-
0.0000017
Oxyuranus microlepidotus inhibitor
-
in 0.1 M Tris-HCl, pH 7.4, 0.01% (v/v) Tween 80 at 25°C
-
0.00000035
specific serine protease inhibitor protein from Bauhinia bauhinoides seeds
-
pH 8.0, 37°C
-
0.000000057
taicatoxin serine protease inhibitor
-
in 0.1 MTris-HCl, pH 7.4, 0.01% (v/v) Tween 80 at 25°C
-
0.00483
textilinin-1
-
in 0.1 M Tris-HCl, pH 7.4, 0.01% (v/v) Tween 80 at 25°C
-
0.00081
trans-4-aminomethylcyclohexanecarbonyl-L-phenylalanyl-4-aminophenyl acetic acid
-
37°C
additional information
additional information
-
inhibition kinetics and secondorder rate constants
-
0.000003
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-3'-chloro-6-hydroxybiphenyl-3-yl]butanedioic acid
-
-
0.000065
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-3'-chloro-6-hydroxybiphenyl-3-yl]butanedioic acid
-
-
0.00000036
ACiSWPARCiiLHQDLCiiiA
pH and temperature not specified in the publication
0.00003
ACiSWPARCiiLHQDLCiiiA
pH and temperature not specified in the publication
0.000000011
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, at room temperature
-
0.000000014
ecotin
-
ecotin with mutation H53P in the 50s loop and mutations S82W/T83N/M84R/M85R/A86S in the 80s loop, at room temperature
-
0.000000025
ecotin
-
ecotin with mutations S82W/T83N/M84R/M85R/A86S in the 80s loop and mutations R108S/N110S in the 100s loop, at room temperature
-
0.000000037
ecotin
-
ecotin with mutations S82W/T83N/M84R/M85R/A86S in the 80s loop, at room temperature
-
0.000000097
ecotin
-
ecotin with mutation H53P in the 50s loop, at room temperature
-
0.000000118
ecotin
-
ecotin with mutations R108S/N110S in the 100s loop, at room temperature
-
0.000000186
ecotin
-
ecotin with mutation H53P in the 50s loop and mutations R108S/N110S in the 100s loop, at room temperature
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00009
1-benzyl-N-[(4-carbamimidoylphenyl)methyl]-1H-pyrazole-4-carboxamide
Homo sapiens
pH and temperature not specified in the publication
3.4
1-[3-(1H-pyrazol-1-yl)phenyl]methanamine
Rattus norvegicus
pH and temperature not specified in the publication
0.0154
1-[3-(aminomethyl)phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
pH and temperature not specified in the publication
0.0273
1-[3-(aminomethyl)phenyl]-N-(2-fluorophenyl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.000395
1-[3-(aminomethyl)phenyl]-N-(3-fluoro-4'-sulfamoyl[1,1'-biphenyl]-4-yl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.00102
1-[3-(aminomethyl)phenyl]-N-(3-fluoro[1,1'-biphenyl]-4-yl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.000395
1-[3-(aminomethyl)phenyl]-N-(4'-carbamoyl-3-fluoro[1,1'-biphenyl]-4-yl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.000577
1-[3-(aminomethyl)phenyl]-N-(4-cyclopropyl-2-fluorophenyl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.0000018
1-[3-(aminomethyl)phenyl]-N-(5-[(3-cyanophenyl)[(cyclopropylmethyl)amino]methyl]-2-fluorophenyl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.0000072
1-[3-(aminomethyl)phenyl]-N-(5-[(4-cyanophenyl)[(cyclopropylmethyl)amino]methyl]-2-fluorophenyl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.0000139
1-[3-(aminomethyl)phenyl]-N-(5-[(S)-(3-cyanophenyl)[(cyclopropylmethyl)amino]methyl]-2-fluorophenyl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.000009
1-[3-(aminomethyl)phenyl]-N-(5-[[(cyclopropylmethyl)amino](phenyl)methyl]-2-fluorophenyl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.0000104
1-[3-(aminomethyl)phenyl]-N-(5-[[(cyclopropylmethyl)amino](pyridin-2-yl)methyl]-2-fluorophenyl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.00001
1-[3-(aminomethyl)phenyl]-N-(5-[[(cyclopropylmethyl)amino](pyridin-3-yl)methyl]-2-fluorophenyl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.0000052
1-[3-(aminomethyl)phenyl]-N-(5-[[(cyclopropylmethyl)amino](pyridin-4-yl)methyl]-2-fluorophenyl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.0029
1-[3-(aminomethyl)phenyl]-N-([1,1'-biphenyl]-4-yl)-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.0226
1-[3-(aminomethyl)phenyl]-N-phenyl-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.000149
1-[3-(aminomethyl)phenyl]-N-[2-fluoro-3-[hydroxy(phenyl)methyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.001
1-[3-(aminomethyl)phenyl]-N-[2-fluoro-4-[hydroxy(phenyl)methyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.00071
1-[3-(aminomethyl)phenyl]-N-[2-fluoro-5-[hydroxy(phenyl)methyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.000231
1-[3-(aminomethyl)phenyl]-N-[2-fluoro-5-[methoxy(phenyl)methyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.001229
1-[3-(aminomethyl)phenyl]-N-[3-fluoro-3'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.0000374
1-[3-(aminomethyl)phenyl]-N-[3-[(cyclopropylmethoxy)(phenyl)methyl]-2-fluorophenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.000708
1-[3-(aminomethyl)phenyl]-N-[3-[(cyclopropylmethoxy)(phenyl)methyl]-4-fluorophenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.0001
1-[3-(aminomethyl)phenyl]-N-[3-[(cyclopropylmethoxy)(phenyl)methyl]-5-fluorophenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.0000376
1-[3-(aminomethyl)phenyl]-N-[3-[(cyclopropylmethoxy)(phenyl)methyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.000651
1-[3-(aminomethyl)phenyl]-N-[4-[(cyclopropylmethoxy)(phenyl)methyl]-2-fluorophenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.0000064
1-[3-(aminomethyl)phenyl]-N-[5-[(cyclopropylmethoxy)(phenyl)methyl]-2-fluorophenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.0000012
1-[3-(aminomethyl)phenyl]-N-[5-[(R)-[(cyclopropylmethyl)amino](phenyl)methyl]-2-fluorophenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.000024
1-[3-(aminomethyl)phenyl]-N-[5-[(S)-[(cyclopropylmethyl)amino](phenyl)methyl]-2-fluorophenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.000134
1-[3-(aminomethyl)phenyl]-N-[5-[ethoxy(phenyl)methyl]-2-fluorophenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
1
1-[3-[3-(trifluoromethyl)-1H-pyrazol-1-yl]phenyl]methanamine
Rattus norvegicus
pH and temperature not specified in the publication
0.015
2-methylpropyl 4-([N2-[4-(aminomethyl)cyclohexane-1-carbonyl]-L-arginyl]amino)benzoate
Homo sapiens
pH and temperature not specified in the publication
0.000002 - 0.000022
3-amino-1-methyl-15-[(1H-pyrazol-1-yl)methyl]-7,10,11,12,24,25-hexahydro-6H,18H,23H-19,22-(metheno)pyrido[4,3-j][1,9,13,17,18]benzodioxatriazacyclohenicosin-23-one
0.0000048
3-amino-N-[(3R)-1-(3-chlorophenyl)pyrrolidin-3-yl]-1-([4-[(5-fluoro-2-oxopyridin-1(2H)-yl)methyl]phenyl]methyl)-1H-pyrazole-4-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000684
3-amino-N-[(3S)-1-(3-chlorophenyl)pyrrolidin-3-yl]-1-([4-[(5-fluoro-2-oxopyridin-1(2H)-yl)methyl]phenyl]methyl)-1H-pyrazole-4-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.00000003
3-amino-N-[(6-amino-2,4-dimethylpyridin-3-yl)methyl]-1-([4-[(3,5-dimethyl-1H-pyrazol-1-yl)methyl]phenyl]methyl)-1H-pyrazole-4-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0000029
3-amino-N-[2-(3-chlorophenoxy)ethyl]-1-([4-[(2-oxopyridin-1(2H)-yl)methyl]phenyl]methyl)-1H-pyrazole-4-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0000062
3-amino-N-[2-(3-chlorophenoxy)ethyl]-1-([4-[(5-fluoro-2-oxopyridin-1(2H)-yl)methyl]phenyl]methyl)-1H-pyrazole-4-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0001
5-[[(1-[5-[(3-chloroquinolin-6-yl)methyl]pyridin-3-yl]ethenyl)amino]methyl]-4,6-dimethylpyridin-2-amine
Homo sapiens
below, pH and temperature not specified in the publication
0.00000026
avoralstat
Rattus norvegicus
pH and temperature not specified in the publication
0.000000888
berotralstat
Rattus norvegicus
pH and temperature not specified in the publication
0.004
N-benzoyl-3-cyclohexyl-D-alanyl-N-[[4-(aminomethyl)phenyl]methyl]-L-phenylalaninamide
Homo sapiens
pH and temperature not specified in the publication
0.00002
N-benzoyl-O-ethyl-D-tyrosyl-(betaR)-N-[[4-(aminomethyl)phenyl]methyl]-beta-hydroxy-L-phenylalaninamide
Homo sapiens
pH and temperature not specified in the publication
0.00000056
N-[(1-amino-5-methylisoquinolin-6-yl)methyl]-3-(methoxymethyl)-1-([4-[(1H-pyrazol-1-yl)methyl]phenyl]methyl)-1H-pyrazole-4-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0000021
N-[(2-fluoro-3,6-dimethoxyphenyl)methyl]-3-(methoxymethyl)-1-([4-[(2-oxopyridin-1(2H)-yl)methyl]phenyl]methyl)-1H-pyrazole-4-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0000087
N-[(3-chloro-1H-pyrrolo[2,3-b]pyridin-5-yl)methyl]-3-(methoxymethyl)-1-([4-[(4-methyl-1H-pyrazol-1-yl)methyl]phenyl]methyl)-1H-pyrazole-4-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000001
N-[(3-chloro-1H-pyrrolo[2,3-b]pyridin-5-yl)methyl]-3-cyano-1-([4-[(4-methyl-1H-pyrazol-1-yl)methyl]phenyl]methyl)-1H-pyrazole-4-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0001
N-[(3-chloro-1H-pyrrolo[2,3-b]pyridin-5-yl)methyl]-5-([3-(methanesulfonyl)-4-[(2-oxopyridin-1(2H)-yl)methyl]phenyl]methyl)pyridine-3-carboxamide
Homo sapiens
below, pH and temperature not specified in the publication
0.0001
N-[(3-chloro-4-fluoro-1H-indol-5-yl)methyl]-8-[(3-chloroquinolin-6-yl)methyl]-7H-purin-6-amine
Homo sapiens
below, pH and temperature not specified in the publication
0.0001
N-[(3-chloro-6-fluoro-1H-indol-5-yl)methyl]-8-[(3-chloroquinolin-6-yl)methyl]-7H-purin-6-amine
Homo sapiens
below, pH and temperature not specified in the publication
0.0001
N-[(3-chloro-6-fluoro-1H-indol-5-yl)methyl]-8-[[3-(trifluoromethyl)quinolin-6-yl]methyl]-7H-purin-6-amine
Homo sapiens
below, pH and temperature not specified in the publication
0.0000032
N-[(3-fluoro-4-methoxypyridin-2-yl)methyl]-1-([4-[(2-oxopyridin-1(2H)-yl)methyl]phenyl]methyl)-3-(trifluoromethyl)-1H-pyrazole-4-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0000067
N-[(3-fluoro-4-methoxypyridin-2-yl)methyl]-1-([4-[(5-fluoro-2-oxopyridin-1(2H)-yl)methyl]phenyl]methyl)-3-(methoxymethyl)-1H-pyrazole-4-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0001
N-[(5-chloro-1H-indazol-3-yl)methyl]-8-[(3-chloroquinolin-6-yl)methyl]-7H-purin-6-amine
Homo sapiens
below, pH and temperature not specified in the publication
0.0000002
N-[(6-amino-2,4-dimethylpyridin-3-yl)methyl]-1-([4-[(1H-pyrazol-1-yl)methyl]phenyl]methyl)-1H-imidazole-4-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0000024
N-[(6-amino-2,4-dimethylpyridin-3-yl)methyl]-1-([4-[(1H-pyrazol-1-yl)methyl]phenyl]methyl)-1H-pyrazole-4-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000009
N-[(6-amino-2,4-dimethylpyridin-3-yl)methyl]-1-[(4-phenoxyphenyl)methyl]-1H-imidazole-4-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0000082
N-[(6-amino-2,4-dimethylpyridin-3-yl)methyl]-1-[[4-(1H-pyrazol-1-ylmethyl)phenyl]methyl]-1H-pyrazole-4-carboxamide
Homo sapiens
at pH 7.4 and 23°C
0.0000021
N-[(6-amino-2,4-dimethylpyridin-3-yl)methyl]-1-[[4-(benzyloxy)phenyl]methyl]-1H-pyrazole-4-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0001
N-[(6-amino-2,4-dimethylpyridin-3-yl)methyl]-5-([3-(methanesulfonyl)-4-[(2-oxopyridin-1(2H)-yl)methyl]phenyl]methyl)pyridine-3-carboxamide
Homo sapiens
below, pH and temperature not specified in the publication
0.0001
N-[(6-amino-2,4-dimethylpyridin-3-yl)methyl]-8-[[3-(trifluoromethyl)quinolin-6-yl]methyl]-7H-purin-6-amine
Homo sapiens
below, pH and temperature not specified in the publication
0.00002
O-ethyl-N-(3-methyl-1H-pyrrole-2-carbonyl)-D-tyrosyl-N-[[4-(aminomethyl)phenyl]methyl]-L-phenylalaninamide
Homo sapiens
pH and temperature not specified in the publication
0.00001
O-ethyl-N-(3-methylthiophene-2-carbonyl)-D-tyrosyl-N-[[4-(aminomethyl)phenyl]methyl]-L-phenylalaninamide
Homo sapiens
pH and temperature not specified in the publication
0.000089
O-ethyl-N-propanoyl-D-tyrosyl-N-[[4-(aminomethyl)phenyl]methyl]-L-phenylalaninamide
Homo sapiens
pH and temperature not specified in the publication
0.014
Tra-hArg-4-carboxyanilide
Homo sapiens
pH and temperature not specified in the publication
0.018
Tra-hArg-4-methoxycarbonylanilide
Homo sapiens
pH and temperature not specified in the publication
0.00085
Tra-L-Phe-4-ACA
Homo sapiens
pH and temperature not specified in the publication
0.0013
Tra-L-Phe-4-carboxymethylanilide
Homo sapiens
pH and temperature not specified in the publication
0.05
trans-4-aminomethylcyclohexanecarbonyl(Tra)-Lys-4-methoxy-carbonylanilide
Homo sapiens
pH and temperature not specified in the publication
0.000002
3-amino-1-methyl-15-[(1H-pyrazol-1-yl)methyl]-7,10,11,12,24,25-hexahydro-6H,18H,23H-19,22-(metheno)pyrido[4,3-j][1,9,13,17,18]benzodioxatriazacyclohenicosin-23-one
Homo sapiens
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
37
-
assay at
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
from golden hamster liver or Biomphalaria glabrata
SwissProt
brenda
-
95366, 95367, 95369, 95372, 95373, 649590, 649734, 650313, 650449, 650481, 650493, 650841, 650844, 651467, 651518, 651519, 652338, 652456, 653115, 653796, 653878, 667855, 667859
-
-
brenda
-
683460, 683546, 683824, 684080, 695990, 696533, 697372, 697828, 707431, 707622, 709045, 709723, 710095, 717295, 717305, 717314, 717809
-
-
brenda
patients with pemphigus foliaceus (autoimmune blistering disease) and control
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
in sections of hypothalamus and spinalcord, prekallikrein expression
brenda
-
mouse plasma kallikrein is differentially expressed in the developing mammary gland
brenda
-
active plasma kallikrein is localized to connective tissue-type mast cells in the mammary gland
brenda
interstitial Leydig cells of the testes, synthesis of prekallikrein
brenda
-
the kallikrein-kininogen-kinin system is biologically active during establishment of pregnancy in the pig
brenda
additional information
-
activity in plasma of patients with pemphigus foliaceus is significantly increased compared with controls
brenda
PK is the 85 to 88 kDa precursor of the serine protease PKa and circulates in plasma
brenda
the plasma concentration of PPK in healthy individuals is about 580 nM, 75-90% are complexed with high-molecular weight kininogen (HK)
brenda
PK is the 85 to 88 kDa precursor of the serine protease PKa and circulates in plasma
brenda
single cells of the distal tubules, synthesis of prekallikrein
brenda
plasma prekallikrein is synthesised in hepatocytes and epithalial liver cells, and secreted into the blood
brenda
hepatocytes are the local center of the PK gene transcription. It also occurs at different levels in non-hepatic tissues, but circulating PK in plasma is obtained essentially from the liver
brenda
hepatocytes are the local center of the PK gene transcription. It also occurs at different levels in non-hepatic tissues, but circulating PK in plasma is obtained essentially from the liver
brenda
additional information
-
no expression of prekallikrein in the choroid plexus or the cerebellum
brenda
additional information
-
at least four promoter regions and diverse transcription start sites can be utilized. Tissue-dependent alternative use of promoters and transcription starts is evident from a comparison of the start sites in liver and kidney
brenda
additional information
-
intravascular assembly of the plasma kallikrein/kinin system
brenda
additional information
mRNA of PK is also found in nonhepatic cells, such as endothelial cells, fibroblasts, leukocytes, and in extrahepatic tissues. PK expressed in nonhepatic cells and tissues might contribute to local action
brenda
additional information
plasma prekallikrein (PPK), with MW of approx. 85-88 kDa, is a zymogen of trypsin-like serine protease and predominantly synthesized in the liver. Low levels of PPK also exist in several extrahepatic tissues
brenda
additional information
mRNA of PK is also found in nonhepatic cells, such as endothelial cells, fibroblasts, leukocytes, and in extrahepatic tissues. PK expressed in nonhepatic cells and tissues might contribute to local action
brenda
additional information
-
at least four promoter regions and diverse transcription start sites can be utilized. Tissue-dependent alternative use of promoters and transcription starts is evident from a comparison of the start sites in liver and kidney
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
plasma, in orthotopic liver transplant recipients in complex with alpha-2-macroglonulin
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
human PKa evolution among the vertebrate coagulation proteins, including the relations with Factor XI, overview. Duplication of the gene for PK occurred during mammalian evolution, resulting in FXI changing independently of the KKS in placental mammals
malfunction
metabolism
physiological function
additional information
malfunction
-
cerebral hematoma expansion triggered by intracerebral infusion of autologous blood is increased in diabetic rats, and this response is ameliorated by plasma kallikrein inhibition and deficiency, respectively
malfunction
-
C1-inhibitor deficiency can lead to uncontrolled enzyme activity, which is a clinically significant cause of hereditary angioedema
malfunction
-
enzyme deficiency has minor effect on the haemostatic capacity of gene-deficient mice
malfunction
-
prekallikrein-deficient mice are protected from increased BK-driven vascular leakage in retinal vessels, ferric chloride-triggered arterial thrombosis, and hypotension in anaphylaxis models. Prekallikrein-deficient mice have defective ex vivo plasma clotting that leads to a prolonged activated partial thromboplastin time. Chronic plasma kallikrein deficiency induces vascular alterations that cannot be reverted by short-term normalizing plasma kallikrein levels and provides a thromboprotective activity in addition to reduced contact activation
malfunction
-
enzyme deficiency leads to decreased immune cell trafficking in the course of neuroinflammation
malfunction
-
enzyme deficiency leads to decreased immune cell trafficking in the course of neuroinflammation
malfunction
-
plasma prekallikrein-deficient mice have reduced thrombosis risk and plasma kallikrein inhibition is associated with reduced experimental gastroenterocolitis and arthritis in rodents
malfunction
in PM2.5-induced lung injury model, Klkb1-/- mouse strain lacking the gene for pKal exhibits a decrease in total protein, cells numbers in bronchoalveolar lavage fluid (BALF) and histologic lung injury score. The TNF-alpha and IL-6 levels in BALF are significantly decreased in PM2.5-treated Klkb1-/- mice. Plasma thrombin-antithrombin (TAT) complex levels are significantly decreased in PM2.5-treated Klkb1-/- mice. PM2.5 induces pKal activation, HK cleavage and bradykinin production. PM2.5-induced HK cleavage in plasma is completely blocked by a Kal inhibitor, as well as in pKal-deficient plasma. PM2.5 markedly induces thrombin generation in human plasma and wild-type mouse plasma, which is inhibited by both blockade and deficiency of pKal. pKal deficiency ameliorates PM2.5-induced lung injury and coagulation
malfunction
mice deficient in the PK gene (Klkb1-/-) show an alternative mechanism for thrombosis protection, in addition to reduced contact activation, mediated by increased receptor Mas, prostacyclin, Sirt1, and KLF4
malfunction
-
in PM2.5-induced lung injury model, Klkb1-/- mouse strain lacking the gene for pKal exhibits a decrease in total protein, cells numbers in bronchoalveolar lavage fluid (BALF) and histologic lung injury score. The TNF-alpha and IL-6 levels in BALF are significantly decreased in PM2.5-treated Klkb1-/- mice. Plasma thrombin-antithrombin (TAT) complex levels are significantly decreased in PM2.5-treated Klkb1-/- mice. PM2.5 induces pKal activation, HK cleavage and bradykinin production. PM2.5-induced HK cleavage in plasma is completely blocked by a Kal inhibitor, as well as in pKal-deficient plasma. PM2.5 markedly induces thrombin generation in human plasma and wild-type mouse plasma, which is inhibited by both blockade and deficiency of pKal. pKal deficiency ameliorates PM2.5-induced lung injury and coagulation
-
metabolism
factors XIa (FXIa), XIIa (FXIIa), and plasma kallikrein (PKa) of the contact system of coagulation appear to contribute to thrombosis while playing a limited role in hemostasis. Contact activation is initiated upon autoactivation of FXII on negatively charged surfaces. FXIIa activates plasma prekallikrein (PK) to PKa, which in turn activates FXII and initiates the kallikrein-kinin pathway. FXI is also activated by FXIIa, leading to activation of FIX and finally to thrombin formation, which in turn activates FXI in an amplification loop. Animal studies have shown that arterial and venous thrombosis can be reduced by the inhibition of FXI(a) or PKa. Role of factor XIa and plasma kallikrein in arterial and venous thrombosis, overview
metabolism
factors XIa (FXIa), XIIa (FXIIa), and plasma kallikrein (PKa) of the contact system of coagulation appear to contribute to thrombosis while playing a limited role in hemostasis. Contact activation is initiated upon autoactivation of FXII on negatively charged surfaces. FXIIa activates plasma prekallikrein (PK) to PKa, which in turn activates FXII and initiates the kallikrein-kinin pathway. FXI is also activated by FXIIa, leading to activation of FIX and finally to thrombin formation, which in turn activates FXI in an amplification loop. Arterial and venous thrombosis can be reduced by the inhibition of FXI(a) or PKa. Role of factor XIa and plasma kallikrein in arterial and venous thrombosis, overview
metabolism
plasma kallikrein contributes to ambient particulate matter-induced lung injury. Particulate matter (PM) is a key component of air pollutants and is associated with mortality of cardiovascular and respiratory diseases. PM-induced tissue injury involves inflammation and coagulation. Plasma prekallikrein (pKal), along with coagulation factor XII (FXII) and high-molecular-weight kininogen (HK), form the plasma kallikrein-kinin system (KKS), a component of the innate immune response that generates proinflammatory products in response to injury. When the KKS proteins contact with activation surface such as negatively charged molecules, this system becomes activated. Activated kallikrein (Kal) activates FXII to initiate the intrinsic coagulation pathway, and cleaves HK to release bradykinin to enhance vascular permeability and systemic inflammation. Role of plasma pKal in the PM2.5-induced lung injury
metabolism
role of plasma kallikrein, Factor XII in activating the plasma kallikrein-kinin system (KKS), the mechanism of activity and control in the KKS, and the function of high-molecular weight kininogen (HK) on contact activation proteins on cell membranes, overview. Relevant observations about the physiological control of PKa are its clearance from circulation by hepatocytes, inhibition by the plasma-circulating protein inhibitors, and inactivation by proteolysis. In the eye, the consequences of diabetes are microvascular abnormalities, the proliferation of retinal vessels, and increased retinal vascular permeability. The involvement of either kallikrein-kinin or renin-angiotensin systems has been reported in diabetic retinopathy, glaucoma, uveitis, diabetic macular edema, and age-related macular degeneration
metabolism
-
plasma kallikrein contributes to ambient particulate matter-induced lung injury. Particulate matter (PM) is a key component of air pollutants and is associated with mortality of cardiovascular and respiratory diseases. PM-induced tissue injury involves inflammation and coagulation. Plasma prekallikrein (pKal), along with coagulation factor XII (FXII) and high-molecular-weight kininogen (HK), form the plasma kallikrein-kinin system (KKS), a component of the innate immune response that generates proinflammatory products in response to injury. When the KKS proteins contact with activation surface such as negatively charged molecules, this system becomes activated. Activated kallikrein (Kal) activates FXII to initiate the intrinsic coagulation pathway, and cleaves HK to release bradykinin to enhance vascular permeability and systemic inflammation. Role of plasma pKal in the PM2.5-induced lung injury
-
physiological function
-
while the insertion/deletion angiotensin I-converting enzyme polymorphism affects differently the C- and N-domains as well as the kallikrein-kinin system of young normotensive individuals, this polymorphism can not be associated with effects on handgrip strength
physiological function
-
plasma kallikrein is the carboxypeptidase/esterase enzyme responsible for tyrosinamide removal from neuropeptide Y
physiological function
-
hyperglycemia increases cerebral hematoma expansion by plasma kallikrein-mediated osmotic sensitive inhibition of hemostasis, plasma kallikrein-mediated inhibition of collagen-induced platelet aggregation is enhanced by hyperglycemia
physiological function
-
plasma kallikrein directly activates G protein-coupled protease-activated receptors (PAR) 1 and 2. Plasma kallikrein stimulates ADAM (a disintegrin and metalloprotease) 17 activity via a PAR1/2 receptor-dependent mechanism, leading sequentially to release of the endogenous ADAM17 substrates, amphiregulin and tumor necrosis factor-alpha, metalloprotease-dependent transactivation of epidermal growth factor receptors, and metalloprotease and epidermal growth factor receptor-dependent ERK1/2 activation
physiological function
the activated form of PK is involved in blood pressure regulation
physiological function
-
the enzyme drives multiple proteolytic reaction cascades in the cardiovascular system such as the intrinsic pathway of coagulation, the kallikrein-kinin system, the fibrinolytic system, the renin-angiotensin system and the alternative complement pathway
physiological function
-
diabetes is associated with increased intrinsic pathway activity, which is mediated in part by plasma kallikrein (PK). PK-mediated activation of the plasminogen cascade is implicated in adipocyte differentiation and adipogenesis during mammary gland involution via activation of plasmin-mediated cleavage of preadipocyte stromal matrix
physiological function
-
the enzyme drives procoagulant and proinflammatory reactions via the intrinsic pathway of coagulation and the kallikrein-kinin system, respectively
physiological function
-
plasma kallikrein regulates tissue factor expression that is mediated by the kallikrein-kinin and renin-angiotensin systems independently of factor XII contact activation
physiological function
-
the enzyme functions in the blood coagulation pathway, and in regulating blood pressure
physiological function
-
the enzyme modulates endothelial cell function in a protease-activated receptor-2-dependent manner, leading to an up-regulation of the cellular adhesion molecules intercellular adhesion molecule 1 and vascular cell adhesion molecule 1, thereby amplifying leukocyte trafficking. The enzyme is an important direct regulator of blood-brain barrier integrity
physiological function
-
the enzyme modulates endothelial cell function in a protease-activated receptor-2-dependent manner, leading to an up-regulation of the cellular adhesion molecules intercellular adhesion molecule 1 and vascular cell adhesion molecule 1, thereby amplifying leukocyte trafficking. The enzyme is an important direct regulator of blood-brain barrier integrity
physiological function
-
the enzyme sensitizes human platelets by binding to platelet integrins through its KGD (Lys488-Gly489-Asp490 and Lys556-Gly557-Asp558) and KGE (Lys509-Gly510-Glu511) motifs and to cleave PAR-1. These actions enhance platelet activation by subthreshold doses of ADP leading to Ca2+ mobilization, MAPK-related signaling, and ATP release
physiological function
-
plasma prekallikrein has a critical role in acute attacks of hereditary angioedema. High prekallikrein is associated with accelerated vascular disease in diabetes and polymorphisms of prekallikrein that reduce high-molecular-weight kininogen binding are associated with protection from cardiovascular events
physiological function
-
plasma prekallikrein has a critical role in acute attacks of hereditary angioedema. High prekallikrein is associated with accelerated vascular disease in diabetes and polymorphisms of prekallikrein that reduce high-molecular-weight kininogen binding are associated with protection from cardiovascular events
physiological function
-
the enzyme plays a central role in a variety of proteolytic systems, such as the intrinsic pathway of coagulation, the plasma kallikrein-kinin system, the fibrinolysis pathway, the renin-angiotensin system, and the complement pathways. Therefore, it is an important regulator in the pathogenesis of thrombosis, inflammation, and blood pressure
physiological function
structure and function of FXI(a) and PK(a) and their involvement in the development of venous and arterial thrombosis, overview. Both, FXI and PK, play a role in the development of thrombosis
physiological function
structure and function of FXI(a) and PK(a) and their involvement in the development of venous and arterial thrombosis, overview. Both, FXI and PK, play a role in the development of thrombosis
physiological function
plasma kallikrein contributes to ambient particulate matter-induced lung injury. Plasma prekallikrein (pKal), along with coagulation factor XII (FXII) and high-molecular-weight kininogen (HK), form the kallikrein-kinin system (KKS), also named as plasma contact system. The KKS is a component of the innate immune response that generates proinflammatory products in response to injury. Activated kallikrein (Kal) activates FXII to initiate the intrinsic coagulation pathway, and cleaves HK to release bradykinin to enhance vascular permeability and systemic inflammation. Role of plasma pKal in the PM2.5-induced lung injury, overview
physiological function
PKal displays various biological functions in the plasma contact activation system, kallikrein-kinin system (KKS), complement pathway and renin-angiotensin system (RAS). In addition, it is involved in fibrinolysis and inflammation process. Roles of PKal in intrinsic pathway of coagulation and platelet aggregation, overview. PKal displays an important role in human platelet aggregation. At low concentration, PKal facilitates platelet aggregation induced by adenosine diphosphate, collagen and adrenaline. On the contrary, PKal inhibits platelet aggregation induced by thrombin. The stable metabolite bradykinin (BK), which is a product from HK cleaved by PKal, also inhibits thrombin-induced platelet aggregation. In the kallikrein-kinin system (KKS), PKal cleaves HK, producing a potent inflammatory mediator, BK, which further stimulates bradykinin 1 receptor (B1R) and B2R. B1R is mostly expressed during tissue injury, inflammation, administration of lipopolysaccharides like endotoxin and is regulated by mediators such as interleukin (IL)-1beta or tumor necrosis factor (TNF)-alpha. Different from B1R, B2R is constitutively expressed in multiple cells and tissues, including neural and vascular tissues. Both of B1R and B2R activations increase Ca2+ levels in smooth muscle and endothelial cells, further mediating a variety of signaling cascades by stimulating the release of intermediaries such as eicosanoids, endothelial-derived hyperpolarizing factor, NO, epoprostenol, tissue-type plasminogen activator (tPA) and glucose transporter-1/2 (GLU-1/2) which is associated with inflammation, angiogenesis, vasodilation, increased vessel permeability and pain. PKal in plasma, on the one hand, can directly convert plasminogen to plasmin, on the other hand, it can activate urokinase-type plasminogen activator (uPA) from its proenzyme (pro-uPA). Additionally, BK generated in KKS, also stimulates endothelial cells to release tPA. PKal can directly activate the alternative complement pathway, in addition, it can cleave the alpha-FXIIa to beta-FXIIa which further activates the classical complement pathway. PKal activates prorenin to renin, promoting the conversion of angiotensinogen to angiotensin I (Ang I)
physiological function
PKal displays various biological functions in the plasma contact activation system, kallikrein-kinin system (KKS), complement pathway and renin-angiotensin system (RAS). In addition, it is involved in fibrinolysis and inflammation process. Roles of PKal in intrinsic pathway of coagulation and platelet aggregation, overview
physiological function
human PKa and tissue kallikreins are serine proteases from the same family, having high- and low-molecular weight kininogens (HKs and LKs) as substrates, releasing bradykinin (Bk) and Lysbradykinin (Lys-Bk), respectively. Human PKa has a role in cell biology regarding the contact system and KSS, particularly the endothelial cells, and neutrophils, in inflammatory processes and infectious diseases. In addition to the contact system of the intrinsic coagulation pathway, PKa plays a role in pathophysiological processes as a potent prourokinase (pro-uPA) activator, in the renin-angiotensin system as a prorenin activator, as an activator of C3 convertase, and as factor B of the complement system. In the aortic VSMC, PKa activates the ERK1/2 mitogen-activated protein kinase cascade with the stimulation of ADAM 17 (a disintegrin-metalloprotease) via a PAR1/2 receptor-dependent mechanism, without the involvement of BK receptors. The BK-independent PKa action may regulate vascular responses in pathophysiologic states, such as diabetes mellitus. In the central nervous system inflammatory processes, PKa acts as a neuromodulator by engaging PAR-2 and BK-B2 receptors, and the complex biology of kinins also affects cancer progression. In liver injury, PKa cleaves the transforming growth factor (TGF)-beta 1
physiological function
-
plasma kallikrein contributes to ambient particulate matter-induced lung injury. Plasma prekallikrein (pKal), along with coagulation factor XII (FXII) and high-molecular-weight kininogen (HK), form the kallikrein-kinin system (KKS), also named as plasma contact system. The KKS is a component of the innate immune response that generates proinflammatory products in response to injury. Activated kallikrein (Kal) activates FXII to initiate the intrinsic coagulation pathway, and cleaves HK to release bradykinin to enhance vascular permeability and systemic inflammation. Role of plasma pKal in the PM2.5-induced lung injury, overview
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Show AA Sequence and Transmembrane Helices (158 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000
35000
41000
-
x * 85000-88000, nonreducing SDS-PAGE, x * 33000-36000, light chain, + x * 41000, heavy chain, reducing SDS-PAGE
52000
-
x * 52000 + x * 35000, the purified sample exhibits several bands on SDS-PAGE, and the most intense band is found to be the 52000 Da N-terminal subunit of kallikrein by mass spectrometric analysis, two other minor bands around 35000 Da are both C-terminal subunits of kallikrein
55000
-
x * 88000, prekallikrein, SDS-PAGE, x * 33000, kallikrein light chain, SDS-PAGE, x * 55000, kallikrein heavy chain, SDS-PAGE
88000
95000
33000
-
x * 88000, prekallikrein, SDS-PAGE, x * 33000, kallikrein light chain, SDS-PAGE, x * 55000, kallikrein heavy chain, SDS-PAGE
35000
-
x * 52000 + x * 35000, the purified sample exhibits several bands on SDS-PAGE, and the most intense band is found to be the 52000 Da N-terminal subunit of kallikrein by mass spectrometric analysis, two other minor bands around 35000 Da are both C-terminal subunits of kallikrein
88000
-
x * 88000, prekallikrein, SDS-PAGE, x * 33000, kallikrein light chain, SDS-PAGE, x * 55000, kallikrein heavy chain, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
-
x * 85000-88000, nonreducing SDS-PAGE, x * 33000-36000, light chain, + x * 41000, heavy chain, reducing SDS-PAGE
?
-
x * 88000, prekallikrein, SDS-PAGE, x * 33000, kallikrein light chain, SDS-PAGE, x * 55000, kallikrein heavy chain, SDS-PAGE
?
-
x * 52000 + x * 35000, the purified sample exhibits several bands on SDS-PAGE, and the most intense band is found to be the 52000 Da N-terminal subunit of kallikrein by mass spectrometric analysis, two other minor bands around 35000 Da are both C-terminal subunits of kallikrein
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
proteolytic modification
-
the proform PK is cleaved generating the active form PKa. The american alligator possesses a factor FXII and a high-molecular weight kininogen (BK), but no FXI
proteolytic modification
prekallikrein is synthesized in hepatocytes and other cell types and secreted to the blood, and proteolytically activated to kallikrein
proteolytic modification
-
the plasma kallikrein/kinin system has two mechanisms for its activation: one that is dependent and another independent of factor XII, the latter is realized by autoactivation on a negatively charged artificial or biologic surface or by serine protease prolylcarboxypeptidase, a PK activator on endothelial cell surfaces, while factor XIIa performs proteolytic activation of the zymogen prekallikrein, overview
proteolytic modification
enzyme PKa inactivation by proteolysis, PK is activated by cleavage of the Arg371-Ile372 bond. The active enzyme PKa consists of a heavy chain (371 residues) and a light chain (248 residues) that are connected to each other via a disulfide bond. A conformational change occurs upon activation of PK. Autoactivation of factor XII (FXIIa) by negatively charged substances, such as platelet-derived polyphosphates and DNA, from neutrophil extracellular traps that are the contact platforms. Functional FXIIa cleaves the proform PK, generating PKa, the activated enzyme form, and releasing bradykinin (BK) from high-molecular weight kininogen (HK). HK facilitates the activation of PK by FXIIa and on the other hand, serves as a natural substrate for PKa, which cleaves HK to liberate the potent pro-inflammatory peptide bradykinin (BK). The complex with HK also allows PK to interact with cells such as endothelial cells, platelets, and neutrophils. The HK binding sites in PK are situated in the domains A1, A2, and A4, whereby the A2 domain seems to be most important for complex formation with the D6H domain of HK. Prekallikrein activation and function, overview
proteolytic modification
enzyme PKa inactivation by proteolysis. Autoactivation of factor XII (FXIIa) by negatively charged substances, such as platelet-derived polyphosphates and DNA, from neutrophil extracellular traps that are the contact platforms. Once functional, FXIIa cleaves the proform PK, generating PKa, releasing bradykinin (BK) from high-molecular weight kininogen (HK), and initiating inflammation. The endothelial cells and platelet membranes assemble HKs, on endothelial cells and the extracellular matrix, PK binds mainly through assembled HK, and this interaction allows PKa formation independent of the FXII assembly on the cell membrane. Heat-shock protein 90 (Hsp-90) and prolylcarboxypeptidase (PRCP) are two other activators of PK besides FXIIa
proteolytic modification
the proform PK is cleaved generating the active form PKa. The catfish possesses a factor FXI, but no FXII or high-molecular weight kininogen (BK)
proteolytic modification
Latimeria sp.
-
the proform PK is cleaved generating the active form PKa. The Coelacanth possesses a factor high-molecular weight kininogen (BK), but no FXII or FXI
proteolytic modification
the proform PK is cleaved generating the active form PKa. The opossum possesses a factor FXI, a FXII, and a high-molecular weight kininogen (BK)
proteolytic modification
enzyme PKa inactivation by proteolysis. Autoactivation of factor XII (FXIIa) by negatively charged substances, such as platelet-derived polyphosphates and DNA, from neutrophil extracellular traps that are the contact platforms. Functional FXIIa cleaves the proform PK, generating PKa, the activated enzyme form, and releasing bradykinin (BK) from high-molecular weight kininogen (HK)
proteolytic modification
enzyme PKa inactivation by proteolysis. Autoactivation of factor XII (FXIIa) by negatively charged substances, such as platelet-derived polyphosphates and DNA, from neutrophil extracellular traps that are the contact platforms. Once functional, FXIIa cleaves the proform PK, generating PKa, releasing bradykinin (BK) from high-molecular weight kininogen (HK), and initiating inflammation. The endothelial cells and platelet membranes assemble HKs, on endothelial cells and the extracellular matrix, PK binds mainly through assembled HK, and this interaction allows PKa formation independent of the FXII assembly on the cell membrane. Heat-shock protein 90 (Hsp-90) and prolylcarboxypeptidase (PRCP) are two other activators of PK besides FXIIa
proteolytic modification
-
the proform PK is cleaved generating the active form PKa. The duck-billed platypus possesses a factor FXII and a high-molecular weight kininogen (BK), but no FXI
proteolytic modification
-
the proform PK is cleaved generating the active form PKa. The west african lung fish possesses a factor FXII and a high-molecular weight kininogen (BK), but no FXI
proteolytic modification
the proform PK is cleaved generating the active form PKa. The african clawed frog possesses a factor FXII and a high-molecular weight kininogen (BK), but no FXI
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of the human plasma kallikrein: PDB IDs 8A3Q, 7N7X, 6O1G, 6O1S, 5TJX, 5F8Z, 5F8T, 5F8X, 4ZOT, 4OGY, 4OGX, 2ANW, 2ANY, and 7QOX at 1.4-2.4 A resolutions
enzyme bound to inhibitor, hanging drop vapor diffusion method, using 0.2 M potassium dihydrogen phosphate, 23% (w/v) PEG3350
in complex with human IgG1 monoclonal antibody DX-2930, hanging drop vapor diffusion method, using 0.1 M Bis-Tris, pH 6.5, 20% (w/v) PEG 5000 MME
protease domain recombinantly expressed in Pichia pastoris or in the baculovirus/Sf9 system. Structure for the endoglycosidase H-deglycosylated protease domain produced from Pichia pastoris is determined at 1.4 A. Structure for the mutagenically deglycosylated form produced from Sf9 cells is determined at 1.4 A
sitting drop vapor diffusion method, using 0.1 M carboxylic acids, 0.1 M HEPES/MOPS pH 7.5, 12.5% (v/v) 2-methyl-2,4-pentanediol, 12.5% (w/v) PEG1000, 12.5% (w/v) PEG3350 and a drop containing 0.1 M carboxylic acids, 0.1 M Tris/Bicine pH 8.5, 20% (w/v) PEG 500 MME
apoenzyme and in complex with mupain-1-16, sitting drop vapor diffusion method, using 25% (w/v) poly(ethylene glycol) 3350, 0.1 M Tris-HCl pH8.5, 0.1 M NaCl
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
generation of Klkb1 knockout mice using TALEN technology. Klkb1 exon 4 is selected as TALEN target site. TALEN mRNAs are microinjected into fertilized eggs from C57BL/6 strain. The chimeric mice are mated with C57BL/6 mice for transmission into germ line. In the offsprings, the knockout allele with 1 base deletion (T, 248 of the ORF) is detected by PCR. The genotyping and sequencing result confirms the deletion of 1 bp in the knockout allele (T, 248 of the open reading frame). pKal antigen in plasma of Klkb-/- mice is absent
additional information
-
generation of Klkb1 knockout mice using TALEN technology. Klkb1 exon 4 is selected as TALEN target site. TALEN mRNAs are microinjected into fertilized eggs from C57BL/6 strain. The chimeric mice are mated with C57BL/6 mice for transmission into germ line. In the offsprings, the knockout allele with 1 base deletion (T, 248 of the ORF) is detected by PCR. The genotyping and sequencing result confirms the deletion of 1 bp in the knockout allele (T, 248 of the open reading frame). pKal antigen in plasma of Klkb-/- mice is absent
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
466fold from plasma, affinity chromatography with inhibitor PKSI-527, i.e. trans-4-aminomethylcyclohexanecarbonyl-L-phenylalanyl-4-aminophenyl acetic acid, as ligand
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copurifies with IgG3 in an inactive complex, but can be separated, 2 activity peaks in gel filtration: peak 1 is kallikrein complexed with factor XI, peak 2 is the main one and uncomplexed enzyme
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dermatan sulfate affinity chromatography and hydroxyapatite column chromatography
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prekallikrein
protease domain recombinantly expresed in Pichia pastoris or in the baculovirus/Sf9 system
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the protease domain in Pichia pastoris as a heterologously glycosylated zymogen that is activated by limited trypsin digestion and treated with endoglycosidase H deglycosidase to reduce heterogeneity from the glycosylation. In the baculovirus/Sf9 system, homogenous, crystallizable, and nonglycosylated protein is expressed after mutagenizing three asparagines to glutamate. The activity of the catalytic domain is similar to that of the full-length protein
screening of genomic library, DNA and amino acid sequence determination and analysis
the genomic structure of PK (also KLKB1) comprises a single gene in the human genome that maps to chromosome 4 (q34-q35)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
after oral administration of porcine pancreatic kallikrein formulation (10 units/kg or 20 unis/kg) to dogs, enzyme concentration in plasma reaches maximum 3 h after administration, and then decreases time-dependently
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enzyme levels are markedly enhanced in active central nervous system lesions of multiple sclerosis patients
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the plasma kallikrein amidolytic activity is significantly higher on mesothelial cells treated with malignant pleural effusions than compared to those cultured with benign effusions
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
pharmacology
-
design of specific inhibitors for proteases like plasma kallikrein, but not protein C, to diminish the complement hydrolysis and coagulation during sepsis
medicine
-
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
medicine
-
porcine pancreatic kallikrein is absorbed after oral administration and to exert its pharmacological action via kinins produced by kininogen degradation in dogs
medicine
-
targeting plasma kallikrein may offer a strategy for prevention or treatment of thrombosis
medicine
-
enzyme inhibition can decrease blood-brain barrier damage and cell invasion during neuroinflammation and may offer a strategy for the treatment of multiple sclerosis
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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Human plasma kallikrein
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Homo sapiens
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Van der Graaf, F.; Tans, G.; Bouma, B.N.; Griffin, J.H.
Isolation and functional properties of the heavy and light chains of human plasma kallikrein
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1982
Homo sapiens
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Human plasma kallikrein: Purification, enzyme characterization and quantitative determination in plasma
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Homo sapiens
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Human kallikrein and prekallikrein
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Homo sapiens, Bos taurus
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Human plasma kallikrein
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165
133-139
1974
Homo sapiens
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Mashiko, H.; Kato, K.; Fujii, K.I.; Takahashi, H.
Studies on factor XII in porcine plasma: purification and its conversion to activated form by porcine plasma kallikrein
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198-206
1996
Sus scrofa
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Selective inhibitors of plasma kallikrein
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115-116
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Homo sapiens
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Homo sapiens, Sus scrofa
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Diniz, M.R.V.; Oliveira, E.B.
Purification and properties of a kininogenin from the venom of Lachesis muta (bushmaster)
Toxicon
30
247-258
1992
Lachesis muta
brenda
Tada, M.; Wanaka, K.; Okamoto, S.; Okamoto, U.; Nakaya, Y.; Horie, N.; Hijkata-Okunomiya, A.; Tsuda, Y.; Okada, Y.
Purification method for human plasma kallikrein by a new affinity chromatography
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21
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1998
Homo sapiens
brenda
Seidah, N.G.; Sawyer, N.; Hamelin, J.; Mion, P.; Beaubien, G.; Brachpapa, L.; Rochemont, J.; Mbikay, M.; Chretien, M.
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DNA Cell Biol.
9
737-748
1990
Mus musculus
brenda
Paquin, J.; Benjannet, S.; Sawyer, N.; Lazure, C.; Chretien, M.; Seidah, N.G.
Rat plasma kallikrein: purification, NH2-terminal sequencing and development of a specific radioimmunoassay
Biochim. Biophys. Acta
999
103-110
1989
Rattus norvegicus
brenda
Heimark, R.L.; Davie, E.W.
Bovine and human plasma prekallikrein
Methods Enzymol.
80
157-173
1981
Homo sapiens, Bos taurus
brenda
Naess, F.; Roeise, O.; Johansen, H.T.; Stadaas, J.O.; Aasen, A.O.
Hemodynamic and proteolytic effects of intravenous injection of purified human plasma kallikrein
Am. J. Physiol.
263
405-409
1992
Homo sapiens
-
brenda
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The SWISS-PROT protein knowledgebase and its supplement TrEMBL
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31
365-370
2003
Homo sapiens (P03952), Mus musculus (P26262), Rattus norvegicus (P14272)
brenda
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Characterization of a Kunitz trypsin inhibitor with one disulfide bridge purified from Swartzia pickellii
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291
635-639
2002
Homo sapiens
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Ferritin binds to light chain of human H-kininogen and inhibits kallikrein-mediated bradykinin release
Biochem. J.
365
279-286
2002
Homo sapiens
brenda
Almeida, P.C.; Chagas, J.R.; Cezari, M.H.; Juliano, M.A.; Juliano, L.
Hydrolysis by plasma kallikrein of fluorogenic peptides derived from prorenin processing site
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1479
83-90
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Rattus norvegicus, Homo sapiens
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382
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2001
Homo sapiens
brenda
Dulinski, R.; Suder, P.; Guevara-Lora, I.; Rapala-Kozik, M.; Potempa, J.; Silberring, J.; Imamura, T.; Travis, J.; Kozik, A.
Attenuated kinin release from human neutrophil elastase-pretreated kininogens by tissue and plasma kallikreins
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384
929-937
2003
Homo sapiens
brenda
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24
520-524
2001
Homo sapiens
brenda
Fukumizu, A.; Tsuda, Y.; Wanaka, K.; Tada, M.; Okamoto, S.; Hijikata-Okunomiya, A.; Okada, Y.
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47
1141-1144
1999
Homo sapiens
brenda
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Homo sapiens
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Homo sapiens
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43
109-114
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Homo sapiens
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Homo sapiens
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Homo sapiens
brenda
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Homo sapiens
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Immunolocalization of plasma kallikrein in human brain
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15
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Homo sapiens
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Cocude, C.; Pierrot, C.; Cetre, C.; Fontaine, J.; Godin, C.; Capron, A.; Khalife, J.
Identification of a developmentally regulated Schistosoma mansoni serine protease homologous to mouse plasma kallikrein and human factor I
Parasitology
118
389-396
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Schistosoma mansoni (Q9TYH4)
-
brenda
Sulikowski, T.; Bauer, B.A.; Patston, P.A.
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11
2230-2236
2002
Homo sapiens
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Briseid, K.; Johannesen, S.
Part of purified human plasma kallikrein removed together with a remaining IgG fraction - immunoblot experiments and functional tests
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62
21-24
2002
Homo sapiens
brenda
Shariat-Madar, Z.; Rahimy, E.; Mahdi, F.; Schmaier, A.H.
Overexpression of prolylcarboxypeptidase enhances plasma prekallikrein activation on Chinese hamster ovary cells
Am. J. Physiol. Heart Circ. Physiol.
289
H2697-H2703
2005
Cricetulus griseus
brenda
Barros, N.M.; Puzer, L.; Tersariol, I.L.; Oliva, M.L.; Sampaio, C.A.; Carmona, A.K.; da Motta, G.
Plasma prekallikrein/kallikrein processing by lysosomal cysteine proteases
Biol. Chem.
385
1087-1091
2004
Homo sapiens
brenda
Neth, P.; Arnhold, M.; Sidarovich, V.; Bhoola, K.D.; Fink, E.
Expression of the plasma prekallikrein gene: utilization of multiple transcription start sites and alternative promoter regions
Biol. Chem.
386
101-109
2005
Homo sapiens, Rattus norvegicus
brenda
Vonnahme, K.A.; Fernando, S.C.; Ross, J.W.; Ashworth, M.D.; DeSilva, U.; Malayer, J.R.; Geisert, R.D.
Porcine endometrial expression of kininogen, factor XII, and plasma kallikrein in cyclic and pregnant gilts
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70
132-138
2004
Sus scrofa
brenda
Young, W.B.; Rai, R.; Shrader, W.D.; Burgess-Henry, J.; Hu, H.; Elrod, K.C.; Sprengeler, P.A.; Katz, B.A.; Sukbuntherng, J.; Mordenti, J.
Small molecule inhibitors of plasma kallikrein
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16
2034-2036
2006
Rattus norvegicus
brenda
Rosatelli, T.B.; Roselino, A.M.; Dellalibera-Joviliano, R.; Reis, M.L.; Donadi, E.A.
Increased activity of plasma and tissue kallikreins, plasma kininase II and salivary kallikrein in pemphigus foliaceus (fogo selvagem)
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152
650-657
2005
Homo sapiens
brenda
Tang, J.; Yu, C.L.; Williams, S.R.; Springman, E.; Jeffery, D.; Sprengeler, P.A.; Estevez, A.; Sampang, J.; Shrader, W.; Spencer, J.; Young, W.; McGrath, M.; Katz, B.A.
Expression, crystallization, and three-dimensional structure of the catalytic domain of human plasma kallikrein
J. Biol. Chem.
280
41077-41089
2005
Homo sapiens (Q92876), Homo sapiens
brenda
Shariat-Madar, Z.; Schmaier, A.H.
The plasma kallikrein/kinin and renin angiotensin systems in blood pressure regulation in sepsis
J. Endotoxin Res.
10
3-13
2004
Homo sapiens
brenda
Storini, C.; Bergamaschini, L.; Gesuete, R.; Rossi, E.; Maiocchi, D.; De Simoni, M.G.
Selective inhibition of plasma kallikrein protects brain from reperfusion injury
J. Pharmacol. Exp. Ther.
318
849-854
2006
Mus musculus
brenda
Ravindran, S.; Grys, T.E.; Welch, R.A.; Schapira, M.; Patston, P.A.
Inhibition of plasma kallikrein by C1-inhibitor: role of endothelial cells and the amino-terminal domain of C1-inhibitor
Thromb. Haemost.
92
1277-1283
2004
Homo sapiens
brenda
Gozzo, A.J.; Nunes, V.A.; Cruz-Silva, I.; Carmona, A.K.; Nader, H.B.; Faljoni-Alario, A.; Sampaio, M.U.; Araujo, M.S.
Heparin modulation of human plasma kallikrein on different substrates and inhibitors
Biol. Chem.
387
1129-1138
2006
Homo sapiens
brenda
Fink, E.; Bhoola, K.D.; Snyman, C.; Neth, P.; Figueroa, C.D.
Cellular expression of plasma prekallikrein in human tissues
Biol. Chem.
388
957-963
2007
Homo sapiens (P03952), Homo sapiens
brenda
Isawa, H.; Orito, Y.; Jingushi, N.; Iwanaga, S.; Morita, A.; Chinzei, Y.; Yuda, M.
Identification and characterization of plasma kallikrein-kinin system inhibitors from salivary glands of the blood-sucking insect Triatoma infestans
FEBS J.
274
4271-4286
2007
Homo sapiens
brenda
Schmaier, A.H.
Assembly, activation, and physiologic influence of the plasma kallikrein/kinin system
Int. Immunopharmacol.
8
161-165
2008
Homo sapiens
brenda
Govers-Riemslag, J.W.; Smid, M.; Cooper, J.A.; Bauer, K.A.; Rosenberg, R.D.; Hack, C.E.; Hamulyak, K.; Spronk, H.M.; Miller, G.J.; ten Cate, H.
The plasma kallikrein-kinin system and risk of cardiovascular disease in men
J. Thromb. Haemost.
5
1896-1903
2007
Homo sapiens
brenda
Sainz, I.M.; Pixley, R.A.; Colman, R.W.
Fifty years of research on the plasma kallikrein-kinin system: from protein structure and function to cell biology and in-vivo pathophysiology
Thromb. Haemost.
98
77-83
2007
Homo sapiens
brenda
Saito, A.
Plasma kallikrein is activated on dermatan sulfate and cleaves factor H
Biochem. Biophys. Res. Commun.
370
646-650
2008
Homo sapiens
brenda
Lima, A.R.; Alves, F.M.; Angelo, P.F.; Andrade, D.; Blaber, S.I.; Blaber, M.; Juliano, L.; Juliano, M.A.
S(1) and S(2) subsite specificities of human plasma kallikrein and tissue kallikrein 1 for the hydrolysis of peptides derived from the bradykinin domain of human kininogen
Biol. Chem.
389
1487-1494
2008
Homo sapiens
brenda
Planque, C.; Li, L.; Zheng, Y.; Soosaipillai, A.; Reckamp, K.; Chia, D.; Diamandis, E.P.; Goodglick, L.
A multiparametric serum kallikrein panel for diagnosis of non-small cell lung carcinoma
Clin. Cancer Res.
14
1355-1362
2008
Homo sapiens
brenda
Lehmann, A.
Ecallantide (DX-88), a plasma kallikrein inhibitor for the treatment of hereditary angioedema and the prevention of blood loss in on-pump cardiothoracic surgery
Expert. Opin. Biol. Ther.
8
1187-1199
2008
Homo sapiens
brenda
Phipps, J.A.; Clermont, A.C.; Sinha, S.; Chilcote, T.J.; Bursell, S.E.; Feener, E.P.
Plasma kallikrein mediates angiotensin II type 1 receptor-stimulated retinal vascular permeability
Hypertension
53
175-181
2009
Rattus norvegicus
brenda
Lilla, J.N.; Joshi, R.V.; Craik, C.S.; Werb, Z.
Active plasma kallikrein localizes to mast cells and regulates epithelial cell apoptosis, adipocyte differentiation and stromal remodeling during mammary gland involution
J. Biol. Chem.
284
13792-13803
2009
Mus musculus
brenda
Sexton, D.J.; Chen, T.; Martik, D.; Kuzmic, P.; Kuang, G.; Chen, J.; Nixon, A.E.; Zuraw, B.L.; Forteza, R.M.; Abraham, W.M.; Wood, C.R.
Specific inhibition of tissue kallikrein 1 with a human monoclonal antibody reveals a potential role in airway diseases
Biochem. J.
422
383-392
2009
Homo sapiens
brenda
Stoop, A.A.; Joshi, R.V.; Eggers, C.T.; Craik, C.S.
Analysis of an engineered plasma kallikrein inhibitor and its effect on contact activation
Biol. Chem.
391
425-433
2010
Homo sapiens
brenda
Abid, K.; Rochat, B.; Lassahn, P.G.; Stoecklin, R.; Michalet, S.; Brakch, N.; Aubert, J.F.; Vatansever, B.; Tella, P.; De Meester, I.; Grouzmann, E.
Kinetic study of neuropeptide Y (NPY) proteolysis in blood and identification of NPY3-35: a new peptide generated by plasma kallikrein
J. Biol. Chem.
284
24715-24724
2009
Homo sapiens
brenda
Pnitz, V.; Govers-Riemslag, J.; Brgger-Andersen, T.; Ten Cate, H.; Nilsen, D.
Inhibitor complexes of the plasma kallikrein-kinin system and outcome prediction in patients following admission for chest pain
J. Thromb. Haemost.
7
1231-1233
2009
Homo sapiens
brenda
Almeida, S.S.; Barros, C.C.; Moraes, M.R.; Russo, F.J.; Haro, A.S.; Rosa, T.S.; Alves, M.F.; Pesquero, J.B.; Carmona, A.K.; Bacurau, R.F.; Araujo, R.C.
Plasma Kallikrein and Angiotensin I-converting enzyme N- and C-terminal domain activities are modulated by the insertion/deletion polymorphism
Neuropeptides
44
139-143
2010
Homo sapiens
brenda
Earl, S.T.; Richards, R.; Johnson, L.A.; Flight, S.; Anderson, S.; Liao, A.; de Jersey, J.; Masci, P.P.; Lavin, M.F.
Identification and characterisation of Kunitz-type plasma kallikrein inhibitors unique to Oxyuranus sp. snake venoms
Biochimie
94
365-373
2011
Homo sapiens
brenda
Vergiliana, J.F.; Asokananthan, N.; Stewart, G.A.
Activation of the plasma kallikrein-kinin system on human lung epithelial cells
Biol. Chem.
391
1067-1077
2010
Homo sapiens
brenda
Varano Della Vergiliana, J.F.; Lansley, S.; Tan, A.L.; Creaney, J.; Lee, Y.C.; Stewart, G.A.
Mesothelial cells activate the plasma kallikrein-kinin system during pleural inflammation
Biol. Chem.
392
633-642
2011
Homo sapiens
brenda
Yasuda, Y.; Lu, Z.; Kato, N.; Jomori, T.
Change in blood kinin and plasma porcine pancreatic kallikrein concentrations after oral administration of kallikrein formulation in dog
Biol. Pharm. Bull.
34
1518-1521
2011
Sus scrofa
brenda
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
Homo sapiens (P03952), Homo sapiens, Mus musculus, Rattus norvegicus, Macaca fascicularis
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
Mus musculus, Homo sapiens
brenda
Li, M.; Srp, J.; Gustchina, A.; Dauter, Z.; Mares, M.; Wlodawer, A.
Crystal structures of the complex of a kallikrein inhibitor from Bauhinia bauhinioides with trypsin and modeling of kallikrein complexes
Acta Crystallogr. Sect. D
75
56-69
2019
Homo sapiens (P03952)
brenda
Wang, B.; Yan, X.; Chen, F.; Yang, A.; Lu, Y.; Wu, Y.
Plasma kallikrein contributes to ambient particulate matter-induced lung injury
Biochem. Biophys. Res. Commun.
518
409-415
2019
Mus musculus (P26262), Mus musculus C57BL/6 (P26262)
brenda
Xie, Z.; Li, Z.; Shao, Y.; Liao, C.
Discovery and development of plasma kallikrein inhibitors for multiple diseases
Eur. J. Med. Chem.
190
112137
2020
Homo sapiens (P03952), Rattus norvegicus (P14272)
brenda
Motta, G.; Juliano, L.; Chagas, J.R.
Human plasma kallikrein roles in coagulation, fibrinolysis, inflammation pathways, and beyond
Front. Physiol.
14
1188816
2023
Monodelphis domestica (A0A5F8GV34), Homo sapiens (P03952), Mus musculus (P26262), Ictalurus punctatus (A0A2D0PX86), Xenopus laevis (A0A974I2J2), Alligator mississippiensis, Ornithorhynchus anatinus, no activity in Pseudorca crassidens, no activity in Petromyzon marinus, no activity in Rhincodon typus, no activity in Danio rerio, Latimeria sp., Protopterus annectens
brenda
Kotian, P.L.; Wu, M.; Vadlakonda, S.; Chintareddy, V.; Lu, P.; Juarez, L.; Kellogg-Yelder, D.; Chen, X.; Muppa, S.; Chambers-Wilson, R.; Davis Parker, C.; Williams, J.; Polach, K.J.; Zhang, W.; Raman, K.; Babu, Y.S.
Berotralstat (BCX7353) structure-guided design of a potent, selective, and oral plasma kallikrein inhibitor to prevent attacks of hereditary angioedema (HAE)
J. Med. Chem.
64
12453-12468
2021
Rattus norvegicus (P14272)
brenda
Visser, M.; Heitmeier, S.; Ten Cate, H.; Spronk, H.M.H.
Role of factor XIa and plasma kallikrein in arterial and venous thrombosis
Thromb. Haemost.
120
883-993
2020
Homo sapiens (P03952), Mus musculus (P26262)
brenda
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