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Information on EC 3.4.21.34 - plasma kallikrein and Organism(s) Homo sapiens and UniProt Accession P03952

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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
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This record set is specific for:
Homo sapiens
UNIPROT: P03952 not found.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
selective 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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-KAL
-
-
bradykininogenase
-
-
-
-
callicrein
-
-
-
-
depot-Padutin
-
-
-
-
dilminal D
-
-
-
-
Fletcher factor
-
-
-
-
glumorin
-
-
-
-
kallidinogenase
-
-
-
-
kallikrein
kallikrein B
-
-
kallikrein I
-
-
-
-
kallikrein II
-
-
-
-
kininogenase
-
-
-
-
kininogenin
-
-
-
-
KLK13
-
-
KLK2
-
-
KLK3
-
-
KLK4
-
-
KLK5
-
-
onokrein P
-
-
-
-
padreatin
-
-
-
-
padutin
-
-
-
-
pancreatic kallikrein
-
-
-
-
PKal
-
-
PKKS
-
-
plasma beta-kallikrein
-
-
plasma kallikrein
-
-
plasma kallikrein–kinin system
-
-
plasma KK
-
-
plasma PK
-
-
Plasma prekallikrein
prekallikrein
serum kallikrein
urinary kallikrein
-
-
-
-
urokallikrein
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
410538-33-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
?
factor FXII + H2O
activated factor XII + ?
show the reaction diagram
cleavage between Arg and Val
-
-
?
factor XII + H2O
?
show the reaction diagram
activation of the factor XII, bound to negatively charged surfaces
-
?, ir
factor XII + H2O
activated factor XII
show the reaction diagram
-
-
-
?
high-molecular-weight kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
cleavage between Lys and Arg as wekk as Arg and Ser
-
-
?
kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
Prorenin + H2O
Renin + ?
show the reaction diagram
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
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-MISLMKRPPGFSPFRSSRI-NH2 + H2O
2-aminobenzoyl-MISLMK + RPPGFSPFRSSRI-NH2
show the reaction diagram
-
-
-
-
?
Ac-AGLTR-4-nitroanilide + H2O
Ac-AGLTR + 4-nitroaniline
show the reaction diagram
-
chromogenic substrate based on the C1s cleavage site in complement component C4
-
?
Ac-Phe-Arg-4-nitroanilide
Ac-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
synthetic fluorogenic substrate
-
?
acetyl-Phe-Arg-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
apelin-17 + H2O
KFR + ?
show the reaction diagram
-
the enzyme cleaves the first three N-terminal amino acids (KFR) of apelin-17
-
-
?
benzoyl-Pro-Phe-Arg-4-nitroanilide + H2O
benzoyl-Pro-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
ir
complement component C4 + H2O
?
show the reaction diagram
-
substrate is only cleaved in vitro, not in vivo
-
?
D-butyl-cyclohexylalanine-arginine-4-nitroanilide + H2O
D-butyl-cyclohexylalanine-arginine + 4-nitroaniline
show the reaction diagram
-
-
-
?
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
show the reaction diagram
D-Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
D-Pro-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
D-Pro-Phe-Arg-p-nitroanilide + H2O
D-Pro-Phe-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
factor B + H2O
factor Bb + ?
show the reaction diagram
-
-
-
-
?
factor H + H2O
?
show the reaction diagram
-
-
-
-
?
factor XI + H2O
activated factor XI + ?
show the reaction diagram
factor XII + H2O
?
show the reaction diagram
factor XII + H2O
activated factor XII
show the reaction diagram
-
-
-
-
?
factor XII + H2O
activated factor XII + ?
show the reaction diagram
factor XII + H2O
factor XIIa + ?
show the reaction diagram
-
-
-
-
?
Glu-Pro-Arg-4-nitroanilide + H2O
Glu-Pro-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
?
H-D-Pro-Phe-Arg-4-nitroanilide + H2O
?
show the reaction diagram
-
i.e. S2302, a chromogenic substrate
-
-
?
high molecular weight kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
-
-
-
-
?
high-molecular-weight kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
-
-
-
-
?
high-molecular-weight kininogen + H2O
high-molecular-weight kinin + bradykinin
show the reaction diagram
ISLMKRPPGFSPFRSSR + H2O
ISLMKR + RPPGFSPFR + SSR
show the reaction diagram
-
RPPGFSPFR is bradykinin, synthetic peptide containing the internal kinin sequence, 2 cleavage sites, the C-terminal one being preferred
-
?
kininogen + H2O
?
show the reaction diagram
-
cleaves Lys-Arg and Arg-Ser bonds in kininogen to produce bradykinin, participates in early phase of intrinsic blood coagulation
-
-
?
kininogen + H2O
bradykinin + ?
show the reaction diagram
kininogen + H2O
bradykinin + fragment of kininogen
show the reaction diagram
kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
kininogen + H2O
heavy chain of kininogen + light chain of kininogen + bradykinin
show the reaction diagram
-
high molecular weight substrate, serine protease
bradykinin is an inflammatory peptide
ir
kininogen + H2O
heavy chain of kininogen + modified light chain of kininogen + bradykinin
show the reaction diagram
-
high molecular weight substrate, serine protease
MW of products: 63 kDa, 45 kDa, and 13 kDa, respectively
?
low-molecular-weight kininogen + H2O
low-molecular-weight kinin + kallidin
show the reaction diagram
-
-
kallidin is Lys-bradykinin or Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
?
modified kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
N-benzoyl-Pro-Phe-Arg-4-nitroanilide
N-benzoyl-Pro-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-butyl-(R)-cyclohexylalanyl-L-Arg-p-nitroanilide + H2O
N-butyl-(R)-cyclohexylalanyl-L-Arg + p-nitroaniline
show the reaction diagram
i.e. Pefachrome PK
-
-
?
Nalpha-Benzoyl-L-Arg ethyl ester + H2O
Nalpha-Benzoyl-L-Arg + ethanol
show the reaction diagram
-
-
-
-
?
Nalpha-toluenesulfonyl-L-arginine methyl ester + H2O
Nalpha-toluenesulfonyl-L-arginine + methanol
show the reaction diagram
-
-
-
-
?
neuropeptide Y3-36 + H2O
neuropeptide Y3-35 + L-tyrosine
show the reaction diagram
-
optimal kallikrein concentration is 5 microg/ml, cleavage of around 70% of neuropeptide Y3-36. Higher concentrations of kallikrein conversely results in a decrease of NPY3-35 levels without an increase of neuropeptide Y3-36 levels, suggesting that high concentrations of kallikrein enable additional and nonspecific neuropeptide Y cleavages
-
-
?
o-aminobenzoyl-FSAPMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSAPMK + RLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
identification by mass spectroscopy
?
o-aminobenzoyl-FSQPMKALTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQPMK + ALTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
show the reaction diagram
-
-
identification by mass spectroscopy
?
o-aminobenzoyl-FSQPMKRATLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQPMK + RATLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
identification by mass spectroscopy
?
o-aminobenzoyl-FSQPMKRLTLANTTQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-FSQPMK + RLTLANTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
synthetic fluorogenic substrate derived from the amino acid sequence of human prorenin cleavage site
identification by mass spectroscopy
?
o-aminobenzoyl-LGMISLMKRPPGFSPFRSSRI-NH2 + H2O
bradykinin + ?
show the reaction diagram
-
-
-
?
o-aminobenzoyl-VMIAALPRTMFIQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
?
show the reaction diagram
-
low activity, substrate sequence is based on the Bauhinia ungulata inhibitor protein reactive site sequence
-
?
o-aminobenzoyl-VVISALPRTMFIQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
?
show the reaction diagram
-
substrate sequence is based on the Bauhinia variegata inhibitor protein reactive site sequence
-
?
plasminogen + H2O
plasmin + ?
show the reaction diagram
pro-hepatocyte growth factor + H2O
hepatocyte growth factor beta-chain + hepatocyte growth factor alpha-chain + 10 kDa fragment of the alpha-chain
show the reaction diagram
-
i.e. HGF, two independent cleavage sites: Arg494-Val495, kinetically preferred, and Arg424-His425, recombinant mutant HGF R424A/R494E is no substrate
activation of hepatocyte growth factor
?
Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
pro-urokinase + H2O
urokinase + ?
show the reaction diagram
pro-urokinase type plasminogen activator + H2O
urokinase type plasminogen activator + ?
show the reaction diagram
-
-
-
-
?
Prorenin + H2O
Renin + ?
show the reaction diagram
RPGLPVRFESPLRINIIKE + H2O
RPGLPVR + FESPLRINIIKE
show the reaction diagram
-
peptide based on the reactive site of the Bauhinia bauhinioides inhibitor protein, similar to the kinin moiety in human kininogen
-
?
RPGLPVRFESPLRINIIKE + H2O
RPGLPVRFESPLR + INIIKE
show the reaction diagram
-
peptide based on the reactive site of the Bauhinia bauhinioides inhibitor protein, similar to the kinin moiety in human kininogen
main products
ir
S-2302 + H2O
?
show the reaction diagram
-
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
factor FXII + H2O
activated factor XII + ?
show the reaction diagram
cleavage between Arg and Val
-
-
?
factor XII + H2O
?
show the reaction diagram
activation of the factor XII, bound to negatively charged surfaces
-
ir
factor XII + H2O
activated factor XII
show the reaction diagram
-
-
-
?
high-molecular-weight kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
cleavage between Lys and Arg as wekk as Arg and Ser
-
-
?
kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
Prorenin + H2O
Renin + ?
show the reaction diagram
activation of prorenin, involved in the renin-angiotensin system
-
ir
factor B + H2O
factor Bb + ?
show the reaction diagram
-
-
-
-
?
factor H + H2O
?
show the reaction diagram
-
-
-
-
?
factor XI + H2O
activated factor XI + ?
show the reaction diagram
factor XII + H2O
activated factor XII
show the reaction diagram
-
-
-
-
?
factor XII + H2O
activated factor XII + ?
show the reaction diagram
factor XII + H2O
factor XIIa + ?
show the reaction diagram
-
-
-
-
?
high molecular weight kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
-
-
-
-
?
high-molecular-weight kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
-
-
-
-
?
high-molecular-weight kininogen + H2O
high-molecular-weight kinin + bradykinin
show the reaction diagram
kininogen + H2O
?
show the reaction diagram
-
cleaves Lys-Arg and Arg-Ser bonds in kininogen to produce bradykinin, participates in early phase of intrinsic blood coagulation
-
-
?
kininogen + H2O
bradykinin + ?
show the reaction diagram
kininogen + H2O
bradykinin + fragment of kininogen
show the reaction diagram
kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
kininogen + H2O
heavy chain of kininogen + light chain of kininogen + bradykinin
show the reaction diagram
-
high molecular weight substrate, serine protease
bradykinin is an inflammatory peptide
ir
low-molecular-weight kininogen + H2O
low-molecular-weight kinin + kallidin
show the reaction diagram
-
-
kallidin is Lys-bradykinin or Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
?
modified kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
-
high-molecular weight kininogen digested by human neutrophil elastase
-
ir
pro-urokinase type plasminogen activator + H2O
urokinase type plasminogen activator + ?
show the reaction diagram
-
-
-
-
?
Prorenin + H2O
Renin + ?
show the reaction diagram
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
BCX4161
low nanomolar inhibitory potency
benzamidine
-
C1-inhibitor
-
-
human IgG1 monoclonal antibody DX-2930
potently and specifically inhibits plasma kallikrein
-
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
2-mercaptoethanol
-
inhibition of prekallikrein activation
alpha1-antiprotease
-
-
-
alpha1-proteinase inhibitor-Leu-Gly-Arg
-
mutant of serpin alpha1-proteinase inhibitor with exchange at P3, P2 and P1 position, fast complexing, inhibition kinetics
-
alpha1-proteinase inhibitor-Pro-Phe-Arg
-
mutant of serpin alpha1-proteinase inhibitor with exchange at P3, P2 and P1 position, inhibition kinetics
-
alpha2-Macroglobulin
-
-
-
Alzheimer's amyloid beta-protein precursor
-
weak inhibition
-
antipain
-
inhibition of prekallikrein activation
antithrombin
-
inhibition by antithrombin is 3.4fold improved by heparin, forming a ternary complex with antithrombin
-
antithrombin III
-
-
-
Bauhinia unglata factor Xa inhibitor
-
-
-
Bauhinia ungulata factor Xa inhibitor protein
-
-
-
Bauhinia variegata trypsin inhibitor protein
-
-
-
benzamidine
-
-
bovine dermatan sulfate
-
68% inhibition at
-
C1 esterase inhibitor
-
-
-
C1 inhibitor
-
increased levels of kallikrein-C1 inhibitor complex are independently associated with increased risk for all-cause mortality and the combined endpoint of all-cause mortality or recurrent troponin T-positive events in patients with admission troponin T greater than/equal 0.05 ng/mL
-
C1-inhibitor
-
C1INH
-
-
-
cysteine
-
inhibition of prekallikrein activation
D-Arg-Hph-Arg-CH2OCH2CF3
-
-
D-Arg-Phe-Arg-CH2OCH2CF3
-
-
D-Arg-Phe-Arg-Ser-NH2
-
-
D-Phe-Phe-Arg-chloromethylketone
-
complete inhibition at 0.01 mM
D-Pro-Cha-ArgOH-CH2OCH2CF3
-
-
D-Pro-Phe-Arg-CH2OCH2CF3
-
-
D-Pro-Phe-Arg-H
-
-
diisopropylfluorophosphate
-
-
diphenylcarbamoylfluoride
-
-
dithiothreitol
-
inhibition of prekallikrein activation
ecallantide
-
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
-
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
-
futhan
-
-
glutathione
-
inhibition of prekallikrein activation
heparin
-
improves inhibition by other enzyme inhibitor 1.4-3.4fold, the enzyme binds to a heparin-matrix, but its secondary structure is not modified by heparin, circular dichroism, overview
hepatocyte growth factor activator inhibitor-1
-
i.e. HAI-1, Kunitz type inhibitor specific for serine proteases, relatively weak inhibition
-
hepatocyte growth factor activator inhibitor-1B
-
splicing variant of hepatocyte growth factor activator inhibitor-1, Kunitz type inhibitor specific for serine proteases, relatively weak inhibition
-
HgCl2
-
inhibition of prekallikrein activation
human C1 esterase inhibitor
-
63% inhibition at 0.04 mg/ml
-
leupeptin
-
-
N-alpha-tosyl-D,L-homophenylalanine-4-anilide hydrochloride
-
also known as Pefabloc PK, inhibits plasma kallikrein exclusively
o-aminobenzoyl-FESPLRINIIKE-N-(2,4-dinitrophenyl)-ethylene diamine
-
competitive inhibitors, based on the Bauhinia bauhinioides inhibitor protein reactive site sequence
o-aminobenzoyl-RPGLPVRFESPL-N-(2,4-dinitrophenyl)-ethylene diamine
-
competitive inhibitors, based on the Bauhinia bauhinioides inhibitor protein reactive site sequence
Oxyuranus microlepidotus inhibitor
-
-
-
p-Carboethoxyphenyl epsilon-guanidine caproate
-
-
plasma kallikrein serine protease inhibitor
-
highly specific
-
plasma kallikrein-specific Kunitz domain inhibitor
-
-
-
Pro-Phe-Arg-CH2Cl
-
-
Soybean trypsin inhibitor
-
-
-
specific serine protease inhibitor protein from Bauhinia bauhinioides seeds
-
Swartzia pickellii trypsin inhibitor
-
purified from seeds, serine protease inhibitor, contains a glycosylation site at Asn38, Kunitz type, but contains only 1 disulfide bridge
-
taicatoxin serine protease inhibitor
-
broad spectrum inhibitor with most potent inhibitory activity observed against plasma kallikrein
-
textilinin-1
-
-
-
trans-(4-aminomethylcyclohexanecarbonyl)-Tyr(O-2-Pyrim)-4-carboxyanilide
-
-
trans-(4-aminomethylcyclohexanecarbonyl)-Tyr(O-Pic)-octylamide
-
-
trans-4-aminomethylcyclohexanecarbonyl-D-phenylalanyl-PSI(CH2-NH)-4-aminophenyl acetic acid
-
PKSI-527 pseudo-peptide analogue, 5% inhibition at 1 mM
trans-4-aminomethylcyclohexanecarbonyl-L-phenylalanyl-4-aminophenyl acetic acid
-
i.e. PKSI-527, selective inhibitor, both carbonyl groups of the structure are required
trans-4-aminomethylcyclohexanecarbonyl-L-phenylalanyl-PSI(CH2-NH)-4-aminophenyl acetic acid
-
PKSI-527 pseudo-peptide analogue, 7% inhibition at 1 mM
trans-4-aminomethylcyclohexanecarbonyl-PSI(CH2-NH)-L-phenylalanyl-4-aminophenyl acetic acid
-
PKSI-527 pseudo-peptide analogue, 20% inhibition at 1 mM
triafestin-1
-
isolation and analysis of the enzyme inhibitor from salivary glands of instar nymphs of Triatoma infestans, SwissProt ID A7BJ45, recombinant production in insect or Escherichia coli cells, triafestin-1 specifically interacts with factor XII and high molecular weight kininogen in a Zn2+-dependent manner, and inhibit activation of the kallikrein-kinin system by interfering with the association of factor XII and high molecular weight kininogen with biological activating surfaces as well as inhibiting prekallikrein activation, overview
-
triafestin-2
-
isolation and analysis of enzyme inhibitors from salivary glands of instar nymphs of Triatoma infestans, SwissProt ID A7BJ46, recombinant production in insect or Escherichia coli cells, triafestin-2 specifically interacts with factor XII and high molecular weight kininogen in a Zn2+-dependent manner, and inhibit activation of the kallikrein-kinin system by interfering with the association of factor XII and high molecular weight kininogen with biological activating surfaces as well as inhibiting prekallikrein activation, overview
-
tuna dermatan sulfate
-
80% inhibition at
-
Type IV collagen
-
0.02 mg/ml of collagen causes a slight loss of activity even after 5 hours, whereas with 0.1 mg/ml of collagen, there is an initial rapid decrease of activity to about 40%
-
Z-Phe-OH
-
inhibition of prekallikrein activation
Zn2+
-
inhibits the activation of prekallikrein at concentrations above 0.01 mM, regulatory role
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
coagulation factor XIIa
-
-
factor XIIa
-
thrombin
-
-
dermatan sulfate
-
dermatan sulfate induces contact activation and activates plasma kallikrein-mediated cleavage of factor H
Factor XII
-
essential for activation on artificial surfaces
-
factor XIIa
-
kininogen
-
dependent on in vivo, high molecular weight, in complex with prekallikrein
-
Lima bean trypsin inhibitor
-
-
-
prolylcarboxypeptidase
-
-
-
Zn2+
-
prekallikrein, required, optimal activation on cells at 0.008 mM, activation range 0.005-0.01 mM, higher concentration inhibit, regulatory role
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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
0.736
acetyl-Phe-Arg-4-nitroanilide
-
pH 8.0, 37°C
0.097
apelin-17
-
at pH 7.4 and 37°C
0.091 - 0.117
D-butyl-cyclohexylalanine-arginine-4-nitroanilide
-
0.0024
Factor XII
-
pH 8.0, 37°C
-
0.269
H-D-Pro-Phe-Arg-4-nitroanilide
-
pH 8.0, 37°C
0.00075
high-molecular-weight kininogen
-
pH 8.0, 37°C
-
0.00075
kininogen
-
pH 8.0, 37°C
-
0.0136
Nalpha-benzoyl-L-arginine ethyl ester
-
-
0.136
Nalpha-toluenesulfonyl-L-arginine methyl ester
-
-
0.0281
neuropeptide Y3-36
-
at 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
0.0006
plasminogen
-
pH 8.0, 37°C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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
37.7
acetyl-Phe-Arg-4-nitroanilide
-
pH 8.0, 37°C
13.7
apelin-17
-
at pH 7.4 and 37°C
0.001
Factor XII
-
pH 8.0, 37°C
-
37.7
H-D-Pro-Phe-Arg-4-nitroanilide
-
pH 8.0, 37°C
0.0306
high-molecular-weight kininogen
-
pH 8.0, 37°C
-
1.86 - 2.94
kininogen
-
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 - 3.66
o-aminobenzoyl-VVISALPRTMFIQ-N-(2,4-dinitrophenyl)-ethylene diamine
0.00034
plasminogen
-
pH 8.0, 37°C
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
140
apelin-17
-
at pH 7.4 and 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00000012
human IgG1 monoclonal antibody DX-2930
at pH 7.5 and 30°C
-
0.0000164
Aprotinin
-
in 0.1 M Tris-HCl, pH 7.4, 0.01% (v/v) Tween 80 at 25°C
0.0000069
Bauhinia ungulata factor Xa inhibitor protein
-
pH 8.0, 37°C
-
0.000023
Bauhinia variegata trypsin inhibitor protein
-
pH 8.0, 37°C
-
0.000000011 - 0.000000186
ecotin
-
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
-
0.00000203
Swartzia pickellii trypsin inhibitor
-
-
-
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
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000002
BCX4161
Homo sapiens
at pH 7.4 and 23°C
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28.9
-
purified enzyme, substrate D-Pro-Phe-Arg-4-nitroanilide
81
-
purified enzyme, substrate D-Pro-Phe-Arg-4-nitroanilide
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
7.4
-
assay at
7.4 - 7.8
-
assay at
7.5
-
assay at
7.65
-
-
7.8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22 - 25
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.59
-
calculated from amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
synthesis of prekallikrein
Manually annotated by BRENDA team
single cells of the distal tubules, synthesis of prekallikrein
Manually annotated by BRENDA team
synthesis of prekallikrein
Manually annotated by BRENDA team
synthesis of prekallikrein
Manually annotated by BRENDA team
plasma prekallikrein is synthesised in hepatocytes and epithalial liver cells, and secreted into the blood
Manually annotated by BRENDA team
synthesis of prekallikrein
Manually annotated by BRENDA team
follicular and thecal granulosa cells
Manually annotated by BRENDA team
synthesis of prekallikrein
Manually annotated by BRENDA team
synthesis of prekallikrein
Manually annotated by BRENDA team
synthesis of prekallikrein
Manually annotated by BRENDA team
synthesis of prekallikrein
Manually annotated by BRENDA team
interstitial Leydig cells of the testes, synthesis of prekallikrein
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
-
surface, prekallikrein
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
-
in sections of hypothalamus and spinalcord, prekallikrein expression
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
-
of pons, hipocampus, and medulla, prekallikrein expression
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
-
prekallikrein
Manually annotated by BRENDA team
-
some fibre tracts, prekallikrein expression
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
-
prekellikrein expression
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
-
some fibre tracts, prekallikrein expression
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
-
secretory cells, prekallikrein expression
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
-
surface
Manually annotated by BRENDA team
-
some fibre tracts, prekallikrein expression
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
kallikrein
-
Manually annotated by BRENDA team
plasma
-
Manually annotated by BRENDA team
-
complexed with kininogen
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the activated form of PK is involved in blood pressure regulation
malfunction
-
enzyme deficiency leads to decreased immune cell trafficking in the course of neuroinflammation
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KLKB1_HUMAN
638
0
71370
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
163000
-
sedimentation equilibrium, kallikrein II
22000
-
1 * 36000, 1 * 28000, 1 * 22000, SDS-PAGE with reduction, 3 chains
28000
-
1 * 36000, 1 * 28000, 1 * 22000, SDS-PAGE with reduction, 3 chains
33000
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
36000
-
1 * 36000, 1 * 28000, 1 * 22000, SDS-PAGE with reduction, 3 chains
41000
-
x * 85000-88000, nonreducing SDS-PAGE, x * 33000-36000, light chain, + x * 41000, heavy chain, reducing SDS-PAGE
43000
-
1 * 43000, 1 * 33000, 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
79500
-
x * 79500, prekallikrein, calculated from amino acid sequence
85000
-
gel filtration, main peak
86000
-
? * 86000, SDS-PAGE, kallikrein II
86150
-
MALDI TOF mass spectroscopy
88000
95000
-
gel filtration
98000
-
? * 98000, SDS-PAGE
99800
-
sedimentation equilibrium, kallikrein I
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
1 * 43000, 1 * 33000, SDS-PAGE
monomer
-
1 * 88000, SDS-PAGE
trimer
-
1 * 36000, 1 * 28000, 1 * 22000, SDS-PAGE with reduction, 3 chains
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
prekallikrein is synthesized in hepatocytes and other cell types and secreted to the blood, and proteolytically activated to kallikrein
proteolytic modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S559A
active site mutant
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
IgG stabilizes
-
stable to freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-50°C, stable for several months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-Sepharose column chromatography and Superdex S200 gel filtration
466fold from plasma, affinity chromatography with inhibitor PKSI-527, i.e. trans-4-aminomethylcyclohexanecarbonyl-L-phenylalanyl-4-aminophenyl acetic acid, as ligand
-
48fold, affinity chromatography on soybean trypsin inhibitor-resin
-
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
-
dermatan sulfate affinity chromatography and hydroxyapatite column chromatography
-
prekallikrein
-
protease domain recombinantly expresed in Pichia pastoris or in the baculovirus/Sf9 system
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Drosophila S2 cells
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
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme levels are markedly enhanced in active central nervous system lesions of multiple sclerosis patients
-
the plasma kallikrein amidolytic activity is significantly higher on mesothelial cells treated with malignant pleural effusions than compared to those cultured with benign effusions
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
pharmacology
-
design of specific inhibitors for proteases like plasma kallikrein, but not protein C, to diminish the complement hydrolysis and coagulation during sepsis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nagase, H.; Barrett, A.J.
Human plasma kallikrein
Biochem. J.
193
187-192
1981
Homo sapiens
Manually annotated by BRENDA team
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
J. Biol. Chem.
257
14300-14305
1982
Homo sapiens
Manually annotated by BRENDA team
Heber, H.; Geiger, R.; Heimburger, N.
Human plasma kallikrein: Purification, enzyme characterization and quantitative determination in plasma
Hoppe-Seyler's Z. Physiol. Chem.
359
659-669
1978
Homo sapiens
Manually annotated by BRENDA team
Colman, R.W.; Bagdasarian, A.
Human kallikrein and prekallikrein
Methods Enzymol.
45
303-322
1976
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Sampaio, C.; Wong, S.C.; Shaw, E.
Human plasma kallikrein
Arch. Biochem. Biophys.
165
133-139
1974
Homo sapiens
Manually annotated by BRENDA team
Evans, D.M.; Jones, D.M.; Pitt, G.R.; Suerias-Diaz, J.; Horton, J.; Ashworth, D.; Olsson, H.; Szelke, M.
Selective inhibitors of plasma kallikrein
Immunopharmacology
32
115-116
1996
Homo sapiens
Manually annotated by BRENDA team
Oliva, M.L.V.; Andrade, S.; Batista, I.F.C.; Sampaio, M.U.; Juliano, M.; Fritz, H.; Auerswald, E.A.; Sampaio, C.A.M.
Human plasma kallikrein and tissue kallikrein binding to a substrate based on the reactive site of a factor Xa inhibitor isolates from Bauhinia ungulata seeds
Immunopharmacology
45
145-149
1999
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
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
Biol. Pharm. Bull.
21
105-108
1998
Homo sapiens
Manually annotated by BRENDA team
Heimark, R.L.; Davie, E.W.
Bovine and human plasma prekallikrein
Methods Enzymol.
80
157-173
1981
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
Boeckmann, B.; Bairoch, A.; Apweiler, R.; Blatter, M.C.; Estreicher, A.; Gasteiger, E.; Martin M.J.; Michoud, K.; O'Donovan, C.; Phan, I.; Pilbout, S.; Schneider, M.
The SWISS-PROT protein knowledgebase and its supplement TrEMBL
Nucleic Acids Res.
31
365-370
2003
Homo sapiens (P03952), Mus musculus (P26262), Rattus norvegicus (P14272)
Manually annotated by BRENDA team
Cavalcanti, M.d.S.M.; Oliva, M.L.V.; Fritz, H.; Jochum, M.; Mentele, R.; Sampaio, M.; Coelho, L.C.B.B.; Batista, I.F.C.; Sampaio, C.A.M.
Characterization of a Kunitz trypsin inhibitor with one disulfide bridge purified from Swartzia pickellii
Biochem. Biophys. Res. Commun.
291
635-639
2002
Homo sapiens
Manually annotated by BRENDA team
Parthasarathy, N.; Torti, S.V.; Torti, F.M.
Ferritin binds to light chain of human H-kininogen and inhibits kallikrein-mediated bradykinin release
Biochem. J.
365
279-286
2002
Homo sapiens
Manually annotated by BRENDA team
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
Biochim. Biophys. Acta
1479
83-90
2000
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Oliva, M.L.; Santomauro-Vaz, E.M.; Andrade, S.A.; Juliano, M.A.; Pott, V.J.; Sampaio, M.U.; Sampaio, C.A.
Synthetic peptides and fluorogenic substrates related to the reactive site sequence of Kunitz-type inhibitors isolated from Bauhinia: interaction with human plasma kallikrein
Biol. Chem.
382
109-113
2001
Homo sapiens
Manually annotated by BRENDA team
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
Biol. Chem.
384
929-937
2003
Homo sapiens
Manually annotated by BRENDA team
Tada, M.; Tsuda, Y.; Wanaka, K.; Hijikata-Okunomiya, A.; Horie, N.; Okamoto, U.; Okamoto, S.; Okada, Y.
Isolation of plasma kallikrein by high efficiency affinity chromatography and its characterization
Biol. Pharm. Bull.
24
520-524
2001
Homo sapiens
Manually annotated by BRENDA team
Fukumizu, A.; Tsuda, Y.; Wanaka, K.; Tada, M.; Okamoto, S.; Hijikata-Okunomiya, A.; Okada, Y.
Amino acids and peptides. LIII. Synthesis and biological activities of some pseudo-peptide analogs of PKSI-527, a plasma kallikrein selective inhibitor: the importance of the peptide backbone
Chem. Pharm. Bull.
47
1141-1144
1999
Homo sapiens
Manually annotated by BRENDA team
Okada, Y.; Tsuda, Y.; Tada, M.; Wanaka, K.; Okamoto, U.; Hijikata-Okunomiya, A.; Okamoto, S.
Development of potent and selective plasmin and plasma kallikrein inhibitors and studies on the structure-activity relationship
Chem. Pharm. Bull.
48
1964-1972
2000
Homo sapiens
Manually annotated by BRENDA team
Oliva, M.L.; Mendes, C.R.; Santomauro-Vaz, E.M.; Juliano, M.A.; Mentele, R.; Auerswald, E.A.; Sampaio, M.U.; Sampaio, C.A.
Bauhinia bauhinioides plasma kallikrein inhibitor: interaction with synthetic peptides and fluorogenic peptide substrates related to the reactive site sequence
Curr. Med. Chem.
8
977-984
2001
Homo sapiens
Manually annotated by BRENDA team
Rojkjaer, R.; Schmaier, A.H.
Activation of the plasma kallikrein/kinin system on endothelial cell membranes
Immunopharmacology
43
109-114
1999
Homo sapiens
Manually annotated by BRENDA team
Hayashi, J.; Salomon, D.R.; Hugli, T.E.
Elevated kallikrein activity in plasma from stable liver transplant recipients
Int. Immunopharmacol.
2
1667-1680
2002
Homo sapiens
Manually annotated by BRENDA team
Gozzo, A.J.; Nunes, V.A.; Carmona, A.K.; Nader, H.B.; von Dietrich, C.P.; Silveira, V.L.; Shimamoto, K.; Ura, N.; Sampaio, M.U.; Sampaio, C.A.; Araujo, M.S.
Glycosaminoglycans affect the action of human plasma kallikrein on kininogen hydrolysis and inflammation
Int. Immunopharmacol.
2
1861-1865
2002
Homo sapiens
Manually annotated by BRENDA team
Peek, M.; Moran, P.; Mendoza, N.; Wickramasinghe, D.; Kirchhofer, D.
Unusual proteolytic activation of pro-hepatocyte growth factor by plasma kallikrein and coagulation factor XIa
J. Biol. Chem.
277
47804-47809
2002
Homo sapiens
Manually annotated by BRENDA team
Kirchhofer, D.; Peek, M.; Li, W.; Stamos, J.; Eigenbrot, C.; Kadkhodayan, S.; Elliott, J.M.; Corpuz, R.T.; Lazarus, R.A.; Moran, P.
Tissue expression, protease specificity, and Kunitz domain functions of hepatocyte growth factor activator inhibitor-1B (HAI-1B), a new splice variant of HAI-1
J. Biol. Chem.
278
36341-36349
2003
Homo sapiens
Manually annotated by BRENDA team
Cerf, M.E.; Raidoo, D.M.
Immunolocalization of plasma kallikrein in human brain
Metab. Brain Dis.
15
315-323
2000
Homo sapiens
Manually annotated by BRENDA team
Sulikowski, T.; Bauer, B.A.; Patston, P.A.
alpha1-Proteinase inhibitor mutants with specificity for plasma kallikrein and C1s but not C1
Protein Sci.
11
2230-2236
2002
Homo sapiens
Manually annotated by BRENDA team
Briseid, K.; Johannesen, S.
Part of purified human plasma kallikrein removed together with a remaining IgG fraction - immunoblot experiments and functional tests
Scand. J. Clin. Lab. Invest.
62
21-24
2002
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Br. J. Dermatol.
152
650-657
2005
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Schmaier, A.H.
Assembly, activation, and physiologic influence of the plasma kallikrein/kinin system
Int. Immunopharmacol.
8
161-165
2008
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Saito, A.
Plasma kallikrein is activated on dermatan sulfate and cleaves factor H
Biochem. Biophys. Res. Commun.
370
646-650
2008
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Kenniston, J.; Faucette, R.; Martik, D.; Comeau, S.; Lindberg, A.; Kopacz, K.; Conley, G.; Chen, J.; Viswanathan, M.; Kastrapeli, N.; Cosic, J.; Mason, S.; DiLeo, M.; Abendroth, J.; Kuzmic, P.; Ladner, R.; Edwards, T.; TenHoor, C.; Adelman, B.; Nixon, A.;
Inhibition of plasma kallikrein by a highly specific active site blocking antibody
J. Biol. Chem.
289
23596-23608
2014
Macaca fascicularis, Mus musculus, Rattus norvegicus, Homo sapiens (P03952), Homo sapiens
Manually annotated by BRENDA team
Koumandou, V.L.; Scorilas, A.
Evolution of the plasma and tissue kallikreins, and their alternative splicing isoforms
PLoS ONE
8
e68074
2013
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Bjoerkqvist, J.; Jaemsae, A.; Renne, T.
Plasma kallikrein: the bradykinin-producing enzyme
Thromb. Haemost.
110
399-407
2013
Homo sapiens
Manually annotated by BRENDA team
Pathak, M.; Wong, S.S.; Dreveny, I.; Emsley, J.
Structure of plasma and tissue kallikreins
Thromb. Haemost.
110
423-433
2013
Homo sapiens (P03952)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Schmaier, A.H.
Plasma prekallikrein its role in hereditary angioedema and health and disease
Front. Med.
5
3-3
2018
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Goebel, K.; Asaridou, C.M.; Merker, M.; Eichler, S.; Herrmann, A.M.; Geuss, E.; Ruck, T.; Schuengel, L.; Groeneweg, L.; Narayanan, V.; Schneider-Hohendorf, T.; Gross, C.C.; Wiendl, H.; Kehrel, B.E.; Kleinschnitz, C.; Meuth, S.G.
Plasma kallikrein modulates immune cell trafficking during neuroinflammation via PAR2 and bradykinin release
Proc. Natl. Acad. Sci. USA
116
271-276
2019
Homo sapiens, Mus musculus
Manually annotated by BRENDA team