Information on EC 3.4.21.34 - plasma kallikrein

New: Word Map on EC 3.4.21.34
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bilateria

EC NUMBER
COMMENTARY hide
3.4.21.34
-
RECOMMENDED NAME
GeneOntology No.
plasma kallikrein
REACTION
REACTION DIAGRAM
COMMENTARY hide
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase
-
CAS REGISTRY NUMBER
COMMENTARY hide
410538-33-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
from golden hamster liver or Biomphalaria glabrata
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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-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 B + H2O
factor Bb + ?
show the reaction diagram
-
-
-
-
?
factor FXII + H2O
activated factor XII + ?
show the reaction diagram
-
cleavage between Arg and Val
-
-
?
factor H + H2O
?
show the reaction diagram
-
-
-
-
?
factor X + H2O
factor XIIa + ?
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
factor XIIa + ?
show the reaction diagram
-
-
-
-
?
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
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
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-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
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-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-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-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-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-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
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 SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
factor B + H2O
factor Bb + ?
show the reaction diagram
-
-
-
-
?
factor FXII + H2O
activated factor XII + ?
show the reaction diagram
-
cleavage between Arg and Val
-
-
?
factor H + H2O
?
show the reaction diagram
-
-
-
-
?
factor X + H2O
factor XIIa + ?
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
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
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
plasminogen + H2O
plasmin + ?
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
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
-
-
alpha 2 macroglobulin
-
-
-
alpha1-antiprotease
-
-
-
alpha1-proteinase inhibitor-Leu-Gly-Arg
-
mutant of serpin alpha1-proteinase inhibitor with exchange at P3, P2 and P1 position, fast complexing, inhibition kinetics
-
alpha1-proteinase inhibitor-Pro-Phe-Arg
-
mutant of serpin alpha1-proteinase inhibitor with exchange at P3, P2 and P1 position, inhibition kinetics
-
alpha2-Macroglobulin
-
-
-
Alzheimer's amyloid beta-protein precursor
-
weak inhibition
-
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
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
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
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
-
human IgG1 monoclonal antibody DX-2930
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
-
-
Protein C inhibitor
-
-
-
Soybean trypsin inhibitor
specific serine protease inhibitor protein from Bauhinia bauhinioides seeds
Swartzia pickellii trypsin inhibitor
-
purified from seeds, serine protease inhibitor, contains a glycosylation site at Asn38, Kunitz type, but contains only 1 disulfide bridge
-
taicatoxin serine protease inhibitor
-
broad spectrum inhibitor with most potent inhibitory activity observed against plasma kallikrein
-
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
activated factor XII
-
-
-
coagulation factor XIIa
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
-
-
-
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, 37C
0.091 - 0.117
2AcOH-H-D-butyl-CHA-Arg
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
1.81
N-acetyl-Phe-Arg-4-nitroanilide
-
-
1.7
N-benzoyl-Phe-Val-Arg-4-nitroanilide
-
-
0.0136 - 0.0962
Nalpha-benzoyl-L-arginine ethyl ester
0.00156 - 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 hide
LITERATURE
IMAGE
0.1
2-aminobenzoic acid-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 8.0, 37C
37.7
acetyl-Phe-Arg-4-nitroanilide
Homo sapiens
-
pH 8.0, 37C
0.001
Factor XII
Homo sapiens
-
pH 8.0, 37C
-
37.7
H-D-Pro-Phe-Arg-4-nitroanilide
Homo sapiens
-
pH 8.0, 37C
0.0306
high-molecular-weight kininogen
Homo sapiens
-
pH 8.0, 37C
-
1.86 - 2.94
kininogen
46.2
o-aminobenzoyl-FSAPMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
Homo sapiens
-
pH 8.0, 37C
192
o-aminobenzoyl-FSQAMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
Homo sapiens
-
pH 8.0, 37C
90
o-aminobenzoyl-FSQFMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
Homo sapiens
-
pH 8.0, 37C
480
o-aminobenzoyl-FSQGMKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
Homo sapiens
-
pH 8.0, 37C
18
o-aminobenzoyl-FSQPAKRLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
Homo sapiens
-
pH 8.0, 37C
48
o-aminobenzoyl-FSQPMARLTLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
Homo sapiens
-
pH 8.0, 37C
72
o-aminobenzoyl-FSQPMKRATLGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
Homo sapiens
-
pH 8.0, 37C
42
o-aminobenzoyl-FSQPMKRLALGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
Homo sapiens
-
pH 8.0, 37C
18
o-aminobenzoyl-FSQPMKRLTAGNTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
Homo sapiens
-
pH 8.0, 37C
3 - 6
o-aminobenzoyl-FSQPMKRLTLANTTQ-N-(2,4-dinitrophenyl)-ethylene diamine
Homo sapiens
-
pH 8.0, 37C
60
o-aminobenzoyl-FSQPMKRLTLGATTQ-N-(2,4-dinitrophenyl)-ethylene diamine
0.01
o-aminobenzoyl-VMIAALPRTMFIQ-N-(2,4-dinitrophenyl)-ethylene diamine
Homo sapiens
-
pH 8.0, 37C
3.13 - 3.66
o-aminobenzoyl-VVISALPRTMFIQ-N-(2,4-dinitrophenyl)-ethylene diamine
0.00034
plasminogen
Homo sapiens
-
pH 8.0, 37C
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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 - 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
0.000005
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 - 0.000000186
ecotin
0.00000007 - 0.00000017
human IgG1 monoclonal antibody DX-2930
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
additional information
additional information
-
inhibition kinetics and secondorder rate constants
-
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 - 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 hide
LITERATURE
22 - 25
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.59
-
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
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
-
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
-
synthesis of prekallikrein
Manually annotated by BRENDA team
-
prekellikrein expression
Manually annotated by BRENDA team
-
synthesis of prekallikrein
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
-
prekallikrein expression
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
-
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
-
synthesis of prekallikrein
Manually annotated by BRENDA team
-
synthesis of prekallikrein
Manually annotated by BRENDA team
-
synthesis of prekallikrein
Manually annotated by BRENDA team
-
prekallikrein expression
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
-
the kallikrein-kininogen-kinin system is biologically active during establishment of pregnancy in the pig
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
prekallikrein
Manually annotated by BRENDA team
-
complexed with kininogen
Manually annotated by BRENDA team
dorsal, male worm
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
82000
-
sedimentation equilibrium
85000
-
gel filtration, main peak
86150
-
MALDI TOF mass spectroscopy
99800
-
sedimentation equilibrium, kallikrein I
163000
-
sedimentation equilibrium, kallikrein II
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
1 * 43000, 1 * 33000, SDS-PAGE
monomer
trimer
-
1 * 36000, 1 * 28000, 1 * 22000, SDS-PAGE with reduction, 3 chains
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with human IgG1 monoclonal antibody DX-2930, hanging drop vapor diffusion method, using 0.1 M Bis-Tris, pH 6.5, 20% (w/v) PEG 5000 MME
-
protease domain recombinantly expressed in Pichia pastoris or in the baculovirus/Sf9 system. Structure for the endoglycosidase H-deglycosylated protease domain produced from Pichia pastoris is determined at 1.4 A. Structure for the mutagenically deglycosylated form produced from Sf9 cells is determined at 1.4 A
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
IgG stabilizes
-
stable to freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-50C, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
466fold from plasma, affinity chromatography with inhibitor PKSI-527, i.e. trans-4-aminomethylcyclohexanecarbonyl-L-phenylalanyl-4-aminophenyl acetic acid, as ligand
-
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
expression of the protease domain in Pichia pastoris as a heterologously glycosylated zymogen that is activated by limited trypsin digestion and treated with endoglycosidase H deglycosidase to reduce heterogeneity from the glycosylation. In the baculovirus/Sf9 system, homogenous, crystallizable, and nonglycosylated protein is expressed after mutagenizing three asparagines to glutamate. The activity of the catalytic domain is similar to that of the full-length protein
screening of genomic library, DNA and amino acid sequence determination and analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
after oral administration of porcine pancreatic kallikrein formulation (10 units/kg or 20 unis/kg) to dogs, enzyme concentration in plasma reaches maximum 3 h after administration, and then decreases time-dependently
-
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
pharmacology
-
design of specific inhibitors for proteases like plasma kallikrein, but not protein C, to diminish the complement hydrolysis and coagulation during sepsis