Information on EC 3.4.21.34 - plasma kallikrein

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The expected taxonomic range for this enzyme is: Bilateria

EC NUMBER
COMMENTARY
3.4.21.34
-
RECOMMENDED NAME
GeneOntology No.
plasma kallikrein
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
show the reaction diagram
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
bradykininogenase
-
-
-
-
callicrein
-
-
-
-
depot-Padutin
-
-
-
-
dilminal D
-
-
-
-
Fletcher factor
-
-
-
-
glumorin
-
-
-
-
kallidinogenase
-
-
-
-
kallikrein
-
-
-
-
kallikrein I
-
-
-
-
kallikrein II
-
-
-
-
kininogenase
-
-
-
-
kininogenin
-
-
-
-
onokrein P
-
-
-
-
padreatin
-
-
-
-
padutin
-
-
-
-
pancreatic kallikrein
-
-
-
-
Plasma prekallikrein
-
-
-
-
serum kallikrein
-
-
-
-
urinary kallikrein
-
-
-
-
urokallikrein
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
410538-33-9
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
gene KLK3 or KLKB1, plasma kallikrein precursor
SwissProt
Manually annotated by BRENDA team
kallikrein I, kallikrein II
-
-
Manually annotated by BRENDA team
patients with pemphigus foliaceus (autoimmune blistering disease) and control
-
-
Manually annotated by BRENDA team
purified enzyme
-
-
Manually annotated by BRENDA team
gene KLKB1 or KLK3 or PK, plasma kallikrein precursor
SwissProt
Manually annotated by BRENDA team
gene KLKB1 or PK, plasma kallikrein precursor
SwissProt
Manually annotated by BRENDA team
from golden hamster liver or Biomphalaria glabrata
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
physiological function
-
plasma kallikrein is the carboxypeptidase/esterase enzyme responsible for tyrosinamide removal from neuropeptide Y
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
-
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
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
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
-
-
-
-
?
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-Phe-Phe-Arg-4-methylcoumarin 7-amide
D-Phe-Phe-Arg + 7-amino-4-methylcoumarin
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-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
ir
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
ir
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
ir
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
ir
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
ir
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
ir
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
ir
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
synthetic fluorogenic substrate
-
?
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
plasma kallikrein-selective substrate
-
-
?
D-Pro-Phe-Arg-p-nitroanilide + H2O
D-Pro-Phe-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
D-Val-Leu-Arg-4-nitroanilide + H2O
D-Val-Leu-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
factor H + H2O
?
show the reaction diagram
-
-
-
-
?
factor XI + H2O
activated factor XI + ?
show the reaction diagram
-
proteolytic activation
-
-
?
factor XI + H2O
activated factor XI + ?
show the reaction diagram
-
proteolytic activation, part of the coagulation cascade
-
-
?
factor XII + H2O
?
show the reaction diagram
-
activation of factor XII
-
?
factor XII + H2O
?
show the reaction diagram
-
activation of factor XII
-
?
factor XII + H2O
?
show the reaction diagram
P03952
activation of the factor XII, bound to negatively charged surfaces
-
?, ir
factor XII + H2O
?
show the reaction diagram
P14272
activation of the factor XII, bound to negatively charged surfaces
-
?, ir
factor XII + H2O
?
show the reaction diagram
P26262
activation of the factor XII, bound to negatively charged surfaces
-
?, ir
factor XII + H2O
activated factor XII + ?
show the reaction diagram
-
-
-
-
?
factor XII + H2O
activated factor XII + ?
show the reaction diagram
-
proteolytic activation
-
-
?
factor XII-2 + H2O
activated factor XII-2 + H2O
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
high-molecular-weight kinin + bradykinin
show the reaction diagram
-
-
bradykinin is Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
?
high-molecular-weight kininogen + H2O
high-molecular-weight kinin + bradykinin
show the reaction diagram
-
pathways involving high-molecular-weight kininogen/high-molecular-weight kinin, overview
bradykinin is Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
?
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
?
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
show the reaction diagram
-
-
-
-
?
kininogen + H2O
bradykinin
show the reaction diagram
-
-
-
?
kininogen + H2O
bradykinin
show the reaction diagram
-
-
-
-
?
kininogen + H2O
bradykinin
show the reaction diagram
-
-
-
?
kininogen + H2O
bradykinin
show the reaction diagram
-
cleaves Lys-Arg and Arg-Ser bonds in kininogen to produce bradykinin
-
?
kininogen + H2O
bradykinin
show the reaction diagram
-
the presence of S at P1' position for bradykinin release by human plasma kallikrein appears to be essential
-
-
?
kininogen + H2O
bradykinin + fragment of kininogen
show the reaction diagram
-
-
-
?
kininogen + H2O
bradykinin + fragment of kininogen
show the reaction diagram
-
-
-
?
kininogen + H2O
bradykinin + fragment of kininogen
show the reaction diagram
-
-
-
?
kininogen + H2O
bradykinin + fragment of kininogen
show the reaction diagram
-
-
-
?
kininogen + H2O
bradykinin + fragment of kininogen
show the reaction diagram
-
-
-
?
kininogen + H2O
bradykinin + fragment of kininogen
show the reaction diagram
-
-
-
?
kininogen + H2O
bradykinin + fragment of kininogen
show the reaction diagram
-
-
-
ir
kininogen + H2O
bradykinin + fragment of kininogen
show the reaction diagram
-
-
-
ir
kininogen + H2O
bradykinin + fragment of kininogen
show the reaction diagram
-
-
-
ir
kininogen + H2O
bradykinin + fragment of kininogen
show the reaction diagram
-
-
-
ir
kininogen + H2O
bradykinin + fragment of kininogen
show the reaction diagram
-
high-molecular weight substrate, serine protease
-
?
kininogen + H2O
bradykinin + fragment of kininogen
show the reaction diagram
-
enzyme is a cofactor in blood coagulation and modulates inflammation through release of bradykinin
-
ir
kininogen + H2O
bradykinin + fragment of kininogen
show the reaction diagram
-
part of kallikrein-kininsystem
bradykinin is a potent mediator of inflammatory response
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
?
kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
-
-
-
-
?
kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
-
-
-
-
?
kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
P03952
high-molecular weight kininogen
-
?, ir
kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
P14272
high-molecular weight kininogen
-
?, ir
kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
P26262
high-molecular weight kininogen
-
ir
kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
-
high-molecular weight kininogen, preferred substrate
-
?
kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
P26262
human high-molecular weight kininogen
-
?
kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
-
low-molecular weight kininogen, low activity
-
?
kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
-
high-molecular weight kininogen, involved in inflammatory reaction
-
ir
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
N-acetyl-Phe-Arg-4-nitroanilide + H2O
N-acetyl-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-benzoyl-Phe-Val-Arg-4-nitroanilide + H2O
N-benzoyl-Phe-Val-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-benzoyl-Pro-Phe-Arg-4-nitroanilide
N-benzoyl-Pro-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-Ala-Lys-Arg-4-methylcoumarin 7-amide
N-benzyloxycarbonyl-Ala-Lys-Arg + 7-amino-4-methylcoumarin
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
Q92876
i.e. Pefachrome PK
-
-
?
Nalpha-Benzoyl-L-Arg ethyl ester + H2O
Nalpha-Benzoyl-L-Arg + ethanol
show the reaction diagram
-
-
-
-
?
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-FSAPMKR + LTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
show the reaction diagram
-
-
82% of product formed, identification by mass spectroscopy
?
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-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-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-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-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-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-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-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-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-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-FSQPMKR + ATLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
show the reaction diagram
-
-
87% of product formed, 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-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-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-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-FSQPMKR + LTLANTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
show the reaction diagram
-
-
80% of product formed, 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-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-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-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-GEFIKKSSFQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-GEFIKK + SSFQ-N-(2,4-dinitrophenyl)-ethylene diamine
show the reaction diagram
-
synthetic fluorogenic substrate
33% of product formation, identification by mass spectroscopy
?
o-aminobenzoyl-GEFIKKSSFQ-N-(2,4-dinitrophenyl)-ethylene diamine + H2O
o-aminobenzoyl-GEFIK + KSSFQ-N-(2,4-dinitrophenyl)-ethylene diamine
show the reaction diagram
-
synthetic fluorogenic substrate
67% 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
show the reaction diagram
-
synthetic fluorogenic substrate
38% 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
show the reaction diagram
-
synthetic fluorogenic substrate
62% 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
show the reaction diagram
-
synthetic fluorogenic substrate
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
-
-
-
-
?
plasminogen + H2O
plasmin + ?
show the reaction diagram
-
activation of plasminogen
-
ir
plasminogen + H2O
plasmin + ?
show the reaction diagram
-
activation of plasminogen
-
ir
plasminogen + H2O
plasmin + ?
show the reaction diagram
-
proteolytic activation
-
-
?
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
-
activation of pro-urokinase
-
?
pro-urokinase + H2O
urokinase + ?
show the reaction diagram
-
activation of pro-urokinase
-
?
Prorenin + H2O
Renin + ?
show the reaction diagram
-
activation of human prorenin, activation of prorenin
-
ir
Prorenin + H2O
Renin + ?
show the reaction diagram
P03952
activation of prorenin
-
ir
Prorenin + H2O
Renin + ?
show the reaction diagram
P14272
activation of prorenin
-
ir
Prorenin + H2O
Renin + ?
show the reaction diagram
P26262
activation of prorenin
-
ir
Prorenin + H2O
Renin + ?
show the reaction diagram
-
rat prorenin, very low activity
-
ir
Prorenin + H2O
Renin + ?
show the reaction diagram
P03952
activation of prorenin, involved in the renin-angiotensin system
-
ir
Prorenin + H2O
Renin + ?
show the reaction diagram
P14272
activation of prorenin, involved in the renin-angiotensin system
-
ir
Prorenin + H2O
Renin + ?
show the reaction diagram
P26262
activation of prorenin, involved in the renin-angiotensin system
-
ir
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
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
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
modified kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
-
low-molecular weight kininogen digested by human neutrophil elastase, 26 amino acids cleaved off, is a better substrate than native low-molecular weight kininogen
-
?
additional information
?
-
-
based on the reactive site sequence of Bauhinia ungulata Xa inhibitor peptides
-
-
-
additional information
?
-
P03952
belongs to the peptidase family S1, plasma kallikrein subfamily
-
?
additional information
?
-
P14272
belongs to the peptidase family S1, plasma kallikrein subfamily
-
?
additional information
?
-
P26262
belongs to the peptidase family S1, plasma kallikrein subfamily
-
?
additional information
?
-
-
no activity with o-aminobenzoyl-RPGLPVRFESPL-N-(2,4-dinitrophenyl)-ethylene diamine and o-aminobenzoyl-FESPLRINIIKE-N-(2,4-dinitrophenyl)-ethylene diamine, which are based on the Bauhinia bauhinioides inhibitor protein reactive site sequence
-
?
additional information
?
-
-
substrate specificity requirements
-
?
additional information
?
-
-
substrate specificity requirements, very low activity with the equivalent of rat prorenin to the cleavage site and with the peptide o-aminobenzoyl-NVTSPVQ-N-(2,4-dinitrophenyl)-ethylene diamine, activation of rat prorenin requires a different enzyme and/or mechanism
-
?
additional information
?
-
P03952
defects in gene KLKB1 cause Fletcher factor deficiency, a blood coagulation defect
-
?
additional information
?
-
-
enzyme activity is enhanced in orthotopic liver transplant recipients
-
?
additional information
?
-
-
involved in inflammatory processes via hydrolysis of complement
-
?
additional information
?
-
-
involved in plasma and vascular fibrinolytic activity
-
?
additional information
?
-
Q9TYH4
may play a role in invasion of the host immune response
-
?
additional information
?
-
-
cathepsin may control the activity of plasma prekallikrein/kallikrein system proteins associated with either the cell surface or the extracellular matrix in (patho)physiological processes
-
-
-
additional information
?
-
-
overexpression of prolylcarboxypeptidase in CHO cells enhances plasma prekallikrein activation
-
-
-
additional information
?
-
-
the review indicates how the plasma kallikrein/kinin system and the plasma renin-angiotensin system are activated and interact in endotoxin or related forms of induced sepsis. Activation of both the plasma kallikrein/kinin system and the plasma renin-angiotensin system can lead to increased nitric oxide and prostaglandin formation
-
-
-
additional information
?
-
P03952
kallikrein participates in the surface-dependent activation of blood coagulation, fibrinolysis, kinin generation and inflammation, it has different specific cellular functions dependent on the tissue, overview
-
-
-
additional information
?
-
-
plasma kallikrein activates neutrophil aggregation and degranulation, the enzyme is part of the kallikrein-kininogen-kinin system, KKS, kininogen plays a role in signaling pathways via the kininogen receptors, mechanism of inflammation related to KKS, overview
-
-
-
additional information
?
-
-
the enzyme involved in intrinsic blood clotting, the kallikrein-kinin system and fibrinolysis
-
-
-
additional information
?
-
-
the enzyme is part of the kallikrein-kininogen-kinin system, KKS, overview
-
-
-
additional information
?
-
-
the enzyme is part of the plasma kallikrein-kininogen-kinin system, PKKS, which is involved in cardiovascular disease and artherothrombosis, e.g. coronary heart disease and stroke in middle-aged men, overview
-
-
-
additional information
?
-
-
the enzyme is part of the plasma kallikrein/kinin system that consists of the protein factor XII, prekallikrein, and high-molecular-weight kininogen, intravascular assembly of the plasma kallikrein/kinin system, overview, it acts as a surface-activated coagulation system arising when blood or plasma interacts with artificial surfaces, kallikrein is involved in development of arterial thrombosis, mechanisms, overview
-
-
-
additional information
?
-
-
kininogen domain structure, overview
-
-
-
additional information
?
-
-
active plasma kallikrein localizes to mast cells and regulates epithelial cell apoptosis, adipocyte differentiation and stromal remodeling during mammary gland involution
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
factor H + H2O
?
show the reaction diagram
-
-
-
-
?
factor XI + H2O
activated factor XI + ?
show the reaction diagram
-
proteolytic activation
-
-
?
factor XI + H2O
activated factor XI + ?
show the reaction diagram
-
proteolytic activation, part of the coagulation cascade
-
-
?
factor XII + H2O
?
show the reaction diagram
P03952
activation of the factor XII, bound to negatively charged surfaces
-
ir
factor XII + H2O
?
show the reaction diagram
P14272
activation of the factor XII, bound to negatively charged surfaces
-
ir
factor XII + H2O
?
show the reaction diagram
P26262
activation of the factor XII, bound to negatively charged surfaces
-
ir
factor XII + H2O
activated factor XII + ?
show the reaction diagram
-
-
-
-
?
factor XII + H2O
activated factor XII + ?
show the reaction diagram
-
proteolytic activation
-
-
?
high-molecular-weight kininogen + H2O
high-molecular-weight kinin + bradykinin
show the reaction diagram
-
-
bradykinin is Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
?
high-molecular-weight kininogen + H2O
high-molecular-weight kinin + bradykinin
show the reaction diagram
-
pathways involving high-molecular-weight kininogen/high-molecular-weight kinin, overview
bradykinin is Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
?
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
?
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
show the reaction diagram
-
-
-
-
?
kininogen + H2O
bradykinin
show the reaction diagram
-
the presence of S at P1' position for bradykinin release by human plasma kallikrein appears to be essential
-
-
?
kininogen + H2O
bradykinin + fragment of kininogen
show the reaction diagram
-
-
-
ir
kininogen + H2O
bradykinin + fragment of kininogen
show the reaction diagram
-
-
-
ir
kininogen + H2O
bradykinin + fragment of kininogen
show the reaction diagram
-
-
-
ir
kininogen + H2O
bradykinin + fragment of kininogen
show the reaction diagram
-
-
-
ir
kininogen + H2O
bradykinin + fragment of kininogen
show the reaction diagram
-
enzyme is a cofactor in blood coagulation and modulates inflammation through release of bradykinin
-
ir
kininogen + H2O
bradykinin + fragment of kininogen
show the reaction diagram
-
part of kallikrein-kininsystem
bradykinin is a potent mediator of inflammatory response
ir
kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
-
-
-
-
?
kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
-
-
-
-
?
kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
P03952
high-molecular weight kininogen
-
ir
kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
P14272
high-molecular weight kininogen
-
ir
kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
P26262
high-molecular weight kininogen
-
ir
kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
-
high-molecular weight kininogen, involved in inflammatory reaction
-
ir
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
-
?
plasminogen + H2O
plasmin + ?
show the reaction diagram
-
-
-
-
?
Prorenin + H2O
Renin + ?
show the reaction diagram
-
activation of prorenin
-
ir
Prorenin + H2O
Renin + ?
show the reaction diagram
P03952
activation of prorenin, involved in the renin-angiotensin system
-
ir
Prorenin + H2O
Renin + ?
show the reaction diagram
P14272
activation of prorenin, involved in the renin-angiotensin system
-
ir
Prorenin + H2O
Renin + ?
show the reaction diagram
P26262
activation of prorenin, involved in the renin-angiotensin system
-
ir
modified kininogen + H2O
bradykinin + fragments of kininogen
show the reaction diagram
-
high-molecular weight kininogen digested by human neutrophil elastase
-
ir
additional information
?
-
P03952
defects in gene KLKB1 cause Fletcher factor deficiency, a blood coagulation defect
-
?
additional information
?
-
-
enzyme activity is enhanced in orthotopic liver transplant recipients
-
?
additional information
?
-
-
involved in inflammatory processes via hydrolysis of complement
-
?
additional information
?
-
-
involved in plasma and vascular fibrinolytic activity
-
?
additional information
?
-
Q9TYH4
may play a role in invasion of the host immune response
-
?
additional information
?
-
-
cathepsin may control the activity of plasma prekallikrein/kallikrein system proteins associated with either the cell surface or the extracellular matrix in (patho)physiological processes
-
-
-
additional information
?
-
-
overexpression of prolylcarboxypeptidase in CHO cells enhances plasma prekallikrein activation
-
-
-
additional information
?
-
-
the review indicates how the plasma kallikrein/kinin system and the plasma renin-angiotensin system are activated and interact in endotoxin or related forms of induced sepsis. Activation of both the plasma kallikrein/kinin system and the plasma renin-angiotensin system can lead to increased nitric oxide and prostaglandin formation
-
-
-
additional information
?
-
P03952
kallikrein participates in the surface-dependent activation of blood coagulation, fibrinolysis, kinin generation and inflammation, it has different specific cellular functions dependent on the tissue, overview
-
-
-
additional information
?
-
-
plasma kallikrein activates neutrophil aggregation and degranulation, the enzyme is part of the kallikrein-kininogen-kinin system, KKS, kininogen plays a role in signaling pathways via the kininogen receptors, mechanism of inflammation related to KKS, overview
-
-
-
additional information
?
-
-
the enzyme involved in intrinsic blood clotting, the kallikrein-kinin system and fibrinolysis
-
-
-
additional information
?
-
-
the enzyme is part of the kallikrein-kininogen-kinin system, KKS, overview
-
-
-
additional information
?
-
-
the enzyme is part of the plasma kallikrein-kininogen-kinin system, PKKS, which is involved in cardiovascular disease and artherothrombosis, e.g. coronary heart disease and stroke in middle-aged men, overview
-
-
-
additional information
?
-
-
the enzyme is part of the plasma kallikrein/kinin system that consists of the protein factor XII, prekallikrein, and high-molecular-weight kininogen, intravascular assembly of the plasma kallikrein/kinin system, overview, it acts as a surface-activated coagulation system arising when blood or plasma interacts with artificial surfaces, kallikrein is involved in development of arterial thrombosis, mechanisms, overview
-
-
-
additional information
?
-
-
active plasma kallikrein localizes to mast cells and regulates epithelial cell apoptosis, adipocyte differentiation and stromal remodeling during mammary gland involution
-
-
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-benzyl-1H-pyrazole-4-carboxylic acid 4-carbamimidoyl-benzylamide
-
ASP-440, small molecule inhibitor of plasma kallikrein
2-mercaptoethanol
-
inhibition of prekallikrein activation
2-[3'-acetyl-5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxybiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-2',6-dihydroxybiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-2'-fluoro-6-hydroxybiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-3',6-dihydroxybiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-3'-carbamoyl-6-hydroxybiphenyl-3-yl]butanedioic acid
-
inhibitor with the best potency and selectivity profile for plasma kallikrein versus related serine proteases. This compound is highly stable in vivo and could be further developed for the treatment and inflammatory or coagulation disorders. Pharmacokinetic data
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-3'-chloro-6-hydroxybiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-3'-cyano-6-hydroxybiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-4'-chloro-6-hydroxybiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-2'-methoxybiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-2'-methylbiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-3'-methoxybiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-3'-methylbiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-4'-methoxybiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-4'-methylbiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxybiphenyl-3-yl]butanedioic acid
-
-
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
antipain
-
-
antipain
-
-
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
-
activation of plasma kallikrein and generation of bradykinin are responsible for the angioedema attacks observed with C-1 inhibitor deficiency. C1-inhibitor concentration of greater than 0.001 mM is needed to inhibit 3 nM kallikrein
-
C1-inhibitor
-
inhibition by C1-inhibitor is 1.4fold improved by heparin
-
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
-
-
diisopropylfluorophosphate
-
-
diisopropylfluorophosphate
-
-
diphenylcarbamoylfluoride
-
-
dithiothreitol
-
inhibition of prekallikrein activation
DX-88
-
DX-88 has a strong neuroprotective effect in the early phases of brain ischemia preventing reperfusion injury and indicates that inhibition of plasma kallikrein may be useful tool in the strategy aimed at reducing the detrimental effects linked to reperfusion
-
ecallantide
-
also called DX-88, C305H442N86O91S8, potent and specific inhibitor of plasma kallikrein
-
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 inhibtior 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
-
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
-
-
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
-
-
-
Soybean trypsin inhibitor
-
-
-
Soybean trypsin inhibitor
-
-
-
specific serine protease inhibitor protein from Bauhinia bauhinioides seeds
-
Kunitz type, purified 20 kDa protein
-
specific serine protease inhibitor protein from Bauhinia bauhinioides seeds
-
Kunitz type, purified 20 kDa protein, thermolabile inhibition, optimal at pH 8.0 for trypsin, characterization
-
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
-
Z-Phe-OH
-
inhibition of prekallikrein activation
Zn2+
-
inhibits the activation of prekallikrein at concentrations above 0.01 mM, regulatory role
Leupeptin
-
-
additional information
-
inhibitory potential of diverse trans-(4-aminomethylcyclohexanecarbonyl)-derivatives, structure-activity relationship study, overview
-
additional information
-
no inhibition by hirudin, bdellin, and corn trypsin inhibitor
-
additional information
-
no inhibition by corn trypsin inhibitor
-
additional information
-
angiotensin II inhibits plasma prekallikrein activation by 11%. 2-Mercaptoethanol, EDTA, benzamidine, 2-aminoethyl benzenesulfonyl fluoride, antipain or leupeptin have little effect on activation, whereas cysteine inhibits activation by approximately 65% at 10 mM. Incubation with 500 mM des-arg9-bradykinin, bradykinin fragment 1-7 or bradykinin fragment 1-5 inhibit plasma prekallikrein activation on A-549 cells by 6%, 20% and 4%, respectively. Plasma prekallikrein activation on A-549 cells is not significantly inhibited by Plummers inhibitor, phosphoramidon, captropril, or apstatin
-
additional information
-
preplasma kallikrein activation on MeT-5A, NCI-H2052, NCI-H28 and primary murine mesothelial cells is strongly inhibited by 10 mM cysteine, 100 mM bradykinin, 100 mg/ml protamine sulfate and 5 mM novobiocin. Moderate inhibition is observed with 2-mercaptoethanol, 2-aminoethyl benzenesulfonyl fluoride, antipain and leupeptin on most cell lines. Angiotensin II, benzamidine and EDTA do not inhibit activation
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
P03952
activation by cleavage into light- and heavy-chain, that are linked by one or more disulfide bridges after cleavage
-
factor XIIa
P26262
activation by cleavage into light- and heavy-chain, that are linked by one or more disulfide bridges after cleavage
-
factor XIIa
P14272
activation by cleavage into light- and heavy-chain, that are linked by one or more disulfide bridges after cleavage
-
factor XIIa
-
activation of prekallikrein
-
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
Lima bean trypsin inhibitor
-
-
-
additional information
P03952
binding to negatively charged surfaces activates the enzyme
-
additional information
P26262
binding to negatively charged surfaces activates the enzyme
-
additional information
P14272
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
-
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
-
mesothelial cells activate the plasma kallikrein-kinin system during pleural inflammation
-
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, 37C
0.091
2AcOH-H-D-butyl-CHA-Arg
Q92876
catalytic domain expressed after mutagenizing three asparagines to glutamate in a baculovirus/Sf9 system
0.108
2AcOH-H-D-butyl-CHA-Arg
Q92876
full-length kallikrein
0.117
2AcOH-H-D-butyl-CHA-Arg
Q92876
protease domain in Pichia pastoris as a heterologously glycosylated zymogen that is activated by limited trypsin digestion and treated with endoglycosidase H deglycosidase
0.736
acetyl-Phe-Arg-4-nitroanilide
-
pH 8.0, 37C
3
D-Val-Leu-Arg-4-nitroanilide
-
-
0.0024
Factor XII
-
pH 8.0, 37C
-
0.269
H-D-Pro-Phe-Arg-4-nitroanilide
-
pH 8.0, 37C
0.00075
high-molecular-weight kininogen
-
pH 8.0, 37C
-
0.00075
Kininogen
-
pH 8.0, 37C
-
1.81
N-acetyl-Phe-Arg-4-nitroanilide
-
-
1.7
N-benzoyl-Phe-Val-Arg-4-nitroanilide
-
-
0.0136
Nalpha-benzoyl-L-arginine ethyl ester
-
-
0.0962
Nalpha-benzoyl-L-arginine ethyl ester
-
-
0.00156
Nalpha-toluenesulfonyl-L-arginine methyl ester
-
-
0.136
Nalpha-toluenesulfonyl-L-arginine methyl ester
-
-
0.0281
neuropeptide Y3-36
-
at 37C
-
0.0045
o-aminobenzoyl-FSAPMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
0.012
o-aminobenzoyl-FSQAMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
0.0033
o-aminobenzoyl-FSQFMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
0.005
o-aminobenzoyl-FSQGMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
0.0018
o-aminobenzoyl-FSQPAKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
0.008
o-aminobenzoyl-FSQPMARLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
0.0022
o-aminobenzoyl-FSQPMKRATLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
0.0007
o-aminobenzoyl-FSQPMKRLALGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
0.001
o-aminobenzoyl-FSQPMKRLTAGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
0.0013
o-aminobenzoyl-FSQPMKRLTLANTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
0.0027
o-aminobenzoyl-FSQPMKRLTLGATTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
0.0117
o-aminobenzoyl-FSQPMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
0.00043
o-aminobenzoyl-VMIAALPRTMFIQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
0.00142
o-aminobenzoyl-VVISALPRTMFIQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
0.0006
Plasminogen
-
pH 8.0, 37C
-
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, 37C
37.7
acetyl-Phe-Arg-4-nitroanilide
-
pH 8.0, 37C
0.001
Factor XII
-
pH 8.0, 37C
-
37.7
H-D-Pro-Phe-Arg-4-nitroanilide
-
pH 8.0, 37C
0.0306
high-molecular-weight kininogen
-
pH 8.0, 37C
-
1.86
Kininogen
-
pH 8.0, 37C
-
2.94
Kininogen
-
pH 8.0, 37C
-
46.2
o-aminobenzoyl-FSAPMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
192
o-aminobenzoyl-FSQAMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
90
o-aminobenzoyl-FSQFMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
480
o-aminobenzoyl-FSQGMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
18
o-aminobenzoyl-FSQPAKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
48
o-aminobenzoyl-FSQPMARLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
72
o-aminobenzoyl-FSQPMKRATLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
42
o-aminobenzoyl-FSQPMKRLALGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
18
o-aminobenzoyl-FSQPMKRLTAGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
3 - 6
o-aminobenzoyl-FSQPMKRLTLANTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
60
o-aminobenzoyl-FSQPMKRLTLGATTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
60
o-aminobenzoyl-FSQPMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
0.01
o-aminobenzoyl-VMIAALPRTMFIQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
3.13
o-aminobenzoyl-VVISALPRTMFIQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
3.66
o-aminobenzoyl-VVISALPRTMFIQ-N-(2,4-dinitrophenyl)-ethylene diamine
-
pH 8.0, 37C
0.00034
Plasminogen
-
pH 8.0, 37C
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
-
-
0.00001
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
-
-
0.0000164
Aprotinin
-
in 0.1 M Tris-HCl, pH 7.4, 0.01% (v/v) Tween 80 at 25C
0.0000069
Bauhinia ungulata factor Xa inhibitor protein
-
pH 8.0, 37C
-
0.000023
Bauhinia variegata trypsin inhibitor protein
-
pH 8.0, 37C
-
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
-
0.000000066
ecotin
-
wild-type ecotin, 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
-
0.0000017
Oxyuranus microlepidotus inhibitor
-
in 0.1 M Tris-HCl, pH 7.4, 0.01% (v/v) Tween 80 at 25C
-
0.00000035
specific serine protease inhibitor protein from Bauhinia bauhinoides seeds
-
pH 8.0, 37C
-
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 25C
-
0.00483
textilinin-1
-
in 0.1 M Tris-HCl, pH 7.4, 0.01% (v/v) Tween 80 at 25C
-
0.00081
trans-4-aminomethylcyclohexanecarbonyl-L-phenylalanyl-4-aminophenyl acetic acid
-
37C
0.000000186
ecotin
-
ecotin with mutation H53P in the 50s loop and mutations R108S/N110S in the 100s loop, at room temperature
-
additional information
additional information
-
inhibition kinetics and secondorder rate constants
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28.9
-
purified enzyme, substrate D-Pro-Phe-Arg-4-nitroanilide
81
-
purified enzyme, substrate D-Pro-Phe-Arg-4-nitroanilide
additional information
-
activity in pancreas and brain
additional information
-
activity with different substrates
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
assay at
7.4 - 7.8
-
assay at
7.4
-
assay at
7.5
-
assay at
7.65
-
-
7.8
-
assay at
8.8
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22 - 25
-
assay at
37
-
assay at
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
prekallikrein expression
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
-
activity in plasma of patients with pemphigus foliaceus is significantly increased compared with controls
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
P03952
synthesis of prekallikrein
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
-
prekallikrein expression
Manually annotated by BRENDA team
P03952
single cells of the distal tubules, synthesis of prekallikrein
Manually annotated by BRENDA team
P03952
synthesis of prekallikrein
Manually annotated by BRENDA team
-
prekellikrein expression
Manually annotated by BRENDA team
P03952
synthesis of prekallikrein
Manually annotated by BRENDA team
-
prekallikrein, secretion into blood circulation
Manually annotated by BRENDA team
P03952
plasma prekallikrein is synthesised in hepatocytes and epithalial liver cells, and secreted into the blood
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
-
mouse plasma kallikrein is differentially expressed in the developing mammary gland
Manually annotated by BRENDA team
-
active plasma kallikrein is localized to connective tissue-type mast cells in the mammary gland
Manually annotated by BRENDA team
-
some fibre tracts, prekallikrein expression
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
P03952
synthesis of prekallikrein
Manually annotated by BRENDA team
P03952
follicular and thecal granulosa cells
Manually annotated by BRENDA team
P03952
synthesis of prekallikrein
Manually annotated by BRENDA team
-
secretory cells, prekallikrein expression
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
-
Cohn's fraction IV
Manually annotated by BRENDA team
-
from normal persons and orthotopic liver transplant recipients
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
-
some fibre tracts, prekallikrein expression
Manually annotated by BRENDA team
P03952
synthesis of prekallikrein
Manually annotated by BRENDA team
P03952
synthesis of prekallikrein
Manually annotated by BRENDA team
P03952
synthesis of prekallikrein
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
P03952
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
-
the kallikrein-kininogen-kinin system is biologically active during establishment of pregnancy in the pig
Manually annotated by BRENDA team
-
prekallikrein expression
Manually annotated by BRENDA team
additional information
-
no expression of prekallikrein in the choroid plexus or the cerebellum
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
additional information
-
intravascular assembly of the plasma kallikrein/kinin system
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
ependymal cells
Manually annotated by BRENDA team
P03952
prekallikrein
Manually annotated by BRENDA team
-
complexed with kininogen
Manually annotated by BRENDA team
-
in the blood, prekallikrein
-
Manually annotated by BRENDA team
P26262
plasma
-
Manually annotated by BRENDA team
-
plasma, in orthotopic liver transplant recipients in complex with alpha-2-macroglonulin
-
Manually annotated by BRENDA team
-
prekallikrein, plasma
-
Manually annotated by BRENDA team
Q9TYH4
dorsal, male worm
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
82000
-
sedimentation equilibrium
95372
85000
-
gel filtration, main peak
653878
86150
-
MALDI TOF mass spectroscopy
650493
95000
-
gel filtration
95363
95000
-
gel filtration
95364
99800
-
sedimentation equilibrium, kallikrein I
95363
163000
-
sedimentation equilibrium, kallikrein II
95363
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
Q9TYH4
x * 35000, amino acid sequence determination and SDS-PAGE
?
-
x * 85000-88000, nonreducing SDS-PAGE, x * 33000-36000, light chain, + x * 41000, heavy chain, reducing SDS-PAGE
?
-
x * 86000-88000, SDS-PAGE
?
-
x * 88000, prekallikrein, SDS-PAGE, x * 33000, kallikrein light chain, SDS-PAGE, x * 55000, kallikrein heavy chain, SDS-PAGE
?
-
x * 88000
?
-
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
dimer
-
1 * 43000, 1 * 33000, SDS-PAGE
trimer
-
1 * 36000, 1 * 28000, 1 * 22000, SDS-PAGE with reduction, 3 chains
monomer
-
1 * 88000, SDS-PAGE
additional information
-
? * 86000, SDS-PAGE, kallikrein II, ? * 88000, SDS-PAGE, kallikrein I
additional information
-
? * 98000, SDS-PAGE
additional information
-
? * 88000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
-
glycoprotein
-
-
proteolytic modification
-
prekallikrein is activated by factor XIIa
proteolytic modification
P03952
prekallikrein is synthesized in hepatocytes and other cell types and secreted to the blood, and proteolytically activated to kallikrein
proteolytic modification
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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
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
Q92876
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
IgG stabilizes
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stable to freezing and thawing
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-50C, stable for several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
prekallikrein
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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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48fold, affinity chromatography on soybean trypsin inhibitor-resin
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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
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protease domain recombinantly expresed in Pichia pastoris or in the baculovirus/Sf9 system
Q92876
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
Q92876
screening of genomic library, DNA and amino acid sequence determination and analysis
Q9TYH4
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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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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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
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design of specific inhibitors for proteases like plasma kallikrein, but not protein C, to diminish the complement hydrolysis and coagulation during sepsis
medicine
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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
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porcine pancreatic kallikrein is absorbed after oral administration and to exert its pharmacological action via kinins produced by kininogen degradation in dogs