Information on EC 3.4.21.35 - tissue kallikrein

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The expected taxonomic range for this enzyme is: Euteleostomi

EC NUMBER
COMMENTARY
3.4.21.35
-
RECOMMENDED NAME
GeneOntology No.
tissue kallikrein
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Preferential cleavage of Arg-/- bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-/- or Leu-/-. The rat enzyme is unusual in liberating bradykinin directly from autologous kininogens by cleavage at two Arg-/- bonds
show the reaction diagram
substrate binding pocket contains an Asp residue; trypsin-like serine protease
-
Preferential cleavage of Arg-/- bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-/- or Leu-/-. The rat enzyme is unusual in liberating bradykinin directly from autologous kininogens by cleavage at two Arg-/- bonds
show the reaction diagram
serine at position P1' and arginine at position P2' result in high activity
-
Preferential cleavage of Arg-/- bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-/- or Leu-/-. The rat enzyme is unusual in liberating bradykinin directly from autologous kininogens by cleavage at two Arg-/- bonds
show the reaction diagram
S1 subsite accepts both Arg and Phe and has a preference for basic residues
-
Preferential cleavage of Arg-/- bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-/- or Leu-/-. The rat enzyme is unusual in liberating bradykinin directly from autologous kininogens by cleavage at two Arg-/- bonds
show the reaction diagram
strict preference for Arg in P1 position, wich is further enhanced by Ser in P1' position
-
Preferential cleavage of Arg-/- bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-/- or Leu-/-. The rat enzyme is unusual in liberating bradykinin directly from autologous kininogens by cleavage at two Arg-/- bonds
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
bradykininogenase
-
-
-
-
callicrein
-
-
-
-
depot-Padutin
-
-
-
-
dilminal D
-
-
-
-
EC 3.4.21.8
-
-
formerly
-
EC 3.4.4.21
-
-
formerly
-
glandular kallikrein
-
-
-
-
glandular kallikrein
-
-
glandular kallikrein
-
-
glandular kallikrein
-
-
glandular kallikrein
-
-
glandular kallikrein 2
-
-
glandular kallikrein 24
-
-
glandular kallikrein-2
-
-
glumorin
-
-
-
-
hK10
-
-
hK13
-
-
hK14
-
-
kallidinogenase
-
-
-
-
kallidinogenase
-
-
kallidinogenase
-
-
kallikrein
-
-
-
-
kallikrein
-
part of the kallikrein-kinin system
kallikrein
-
-
kallikrein 1
-
-
-
-
kallikrein 1
P06870
-
kallikrein 24
-
-
kallikrein-related peptidase
-
-
kallikrein-related peptidase 2
-
-
kidney/pancreas/salivary gland kallikrein
-
-
-
-
kininogenase
-
-
-
-
kininogenin
-
-
-
-
KLK-L3
-
hK9
KLK-S3
-
-
-
-
KLK1
-
-
KLK1
-
-
KLK4
-
-
KLK5
-
-
KLK6
-
-
KLK9
-
-
mK13
-
-
mK22
-
-
mK24
-
-
onokrein P.
-
-
-
-
P1 kallikrein
-
-
-
-
padreatin
-
-
-
-
padutin
-
-
-
-
pancreatic kallikrein
-
-
-
-
pancreatic/renal kallikrein
P06870
-
PPK
-
-
-
-
Prk
-
-
-
-
pro-renin-converting enzyme
-
-
prostase/KLK-L1/ARM1/PRSS17
-
hK4
prostate specific antigen
-
-
PS kallikrein
-
-
-
-
PSA/KLK3
-
-
renal kallikrein
P06870
-
renal tissue kallikrein
-
-
-
-
RSGK-50
-
-
-
-
RUK
-
-
-
-
S01.160
-
-
-
-
S1 kallikrein
-
-
-
-
S2 kallikrein
-
-
-
-
S3 kallikrein
-
-
-
-
salivary kallikrein
-
-
-
-
SEV
-
-
-
-
skeletal muscle kallikrein
-
-
submandibular enzymatic vasoconstrictor
-
-
-
-
T-kininogenase
-
-
-
-
tissue kallidinogenase
-
-
tissue kallikrein
P06870
-
tissue kallikrein
-
-
tissue kallikrein
-
-
tissue kallikrein
-
-
tissue kallikrein 1
-
-
tissue kallikrein 1
-
-
tissue kallikrein 11
-
-
tissue kallikrein 4
-
-
tissue kallikrein 9
-
-
trypsin-like serine protease
-
TLSP/hippostasin/hK11
UKLK
-
-
urinary kallidinogenase
-
-
urinary kallikrein
-
-
-
-
urinary kallikrein
-
-
urinary kallikrein
-
-
urinary tissue kallikrein
-
-
urokallikrein
-
-
-
-
additional information
-
KLK1, KLK4, and KLK11 are serine proteases with trypsin-like activity, while KLK9 has chymotrypsin-like activity
CAS REGISTRY NUMBER
COMMENTARY
389069-73-2
-
9001-01-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
kallikrein A and B
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
gene KLK1
SwissProt
Manually annotated by BRENDA team
glandular kallikrein 1 precursor
SwissProt
Manually annotated by BRENDA team
glandular kallikrein; kallikrein genes are located in a cluster on chromosome 19q13.4
-
-
Manually annotated by BRENDA team
men with localized prostate cancer
-
-
Manually annotated by BRENDA team
patients with pemphigus foliaceus (autoimmune blistering disease) and control
-
-
Manually annotated by BRENDA team
precursor
SwissProt
Manually annotated by BRENDA team
gene KLK1, glandular kallikrein 1 precursor
SwissProt
Manually annotated by BRENDA team
african soft-furred rat; gene KLK1, renal glanduar kallikrein precursor
SwissProt
Manually annotated by BRENDA team
gene KLK1, glandular kallikrein 1 precursor
SwissProt
Manually annotated by BRENDA team
gene KLK1, glandular kallikrein 1 precursor
SwissProt
Manually annotated by BRENDA team
gene KLK1, pancreatic glandular kallikrein 1 precursor
SwissProt
Manually annotated by BRENDA team
strains WKY and SHR
-
-
Manually annotated by BRENDA team
beta-kallikrein; form B
-
-
Manually annotated by BRENDA team
commercial product
-
-
Manually annotated by BRENDA team
different forms of beta-kallikrein, i.e. Cbeta-kallikrein, Abeta-kallikrein, and Tbeta-kallikrein, are built from alpha-kallikrein via chymotrypsin digestion
-
-
Manually annotated by BRENDA team
form B
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
genetically ablating tissue kallikrein in mice results in dilated decompensated cardiomyopathy
malfunction
-
human tissue kallikrein 1 (KLK1) silencing reduces proangiogenic cell's migratory, invasive, and proangiogenic activities
malfunction
-
tissue kallkrein deficient mice exhibit net transepithelial potassium absorption in cortical collecting ducts because of abnormal activation of the colonic H+,K+-ATPase in intercalated cells and reduced potassium secretion by principal cells secondary to decreased epithelial sodium channel activity
malfunction
-
cortical collecting ducts s from tissue kallikrein deficient mice reabsorb potassium. Colonic H+, K+-ATPase activity is increased in intercalated cells of cortical collecting ducts from tissue kallikrein deficient mice
physiological function
-
treatment with recombinant adeno-associated virus-tissue kallikrein decreases cell apoptosis in the target organs of spontaneous hypertensive rats and also inhibits lipopolysaccharide-induced HEK-293 apoptosis. The recombinant adeno-associated virus-tissue kallikrein delivery system increases the levels of apoptosis-inhibiting proteins bcl-2 and bcl-x(L), and decreases the level of Bax and the activity of caspase 3, two promoters of apoptosis. In addition to its role in the inhibition of apoptosis, adeno-associated virus-tissue kallikrein activates the cell survival and proliferation signaling pathways ERK1/2 and PI3K/AKT
physiological function
-
elicits a hypotensive action. It is effective in the treatment of patients with acute brain infarction when injected within 48 h after stroke onset. Overexpression of human tissue kallikrein in transgenic rats causes a decrease of isoproterenol-induced cardiac hypertrophy and fibrosis. Human tissue kallikrein gene transfer rescues ischemic tissues in normal mice, and in hypertensive or diabetic animals. Transgenic rats expressing human tissue kallikrein have reduced interstitial fibrosis. Intracerebro-ventribular injection of adenovirus carrying the human tissue kallikrein gene immediately after reperfusion provides neuroprotection against cerebral ischemia injury in a rat model with middle cerebral artery occlusion and in cultured cells by enhancing glial cell migration and inhibiting apoptosis through suppression of oxidative stress and activation of Akt-Bcl-2 signaling pathway
physiological function
-
tissue kallikrein/kinin infusion not only prevents but also reverses kidney injury, inflammation and fibrosis in salt-induced hypertensive rats. Wide time window for kallikrein administration in protection against ischemic brain infarction: delayed kallikrein infusion for 24 h after cerebral ischemia in rats is effective in reducing neurological deficits, infarct size, apoptosis and inflammation. Tissue kallikrein induces contraction of isolated rat uterus in the absence of kinin formation, and elicites cardioprotection by direct kinin B2 receptor activation in kininogen-deficient Brown Norway rats. A subdepressor dose of kallikrein protein or kinin peptide restores impaired cardiac function in rats with postinfarction failure by inhibiting hypertrophy and fibrosis and promoting angiogenesis through increased NO formation and inhibition of oxidative stress and TGF-beta expression. Local application of tissue kallikrein promotes skin wound healing in rats
physiological function
-
oral administration of tissue kallikrein purified from porcine pancreas results in blood pressure reduction in hypertensive patients
physiological function
-
purified tissue kallikrein promotes DU145 prostate cancer cell migration in a similar manner than rat tissue kallikrein
physiological function
-
tissue kallikrein promotes DU145 prostate cancer cell migration in a concentration-dependent manner, but has no effect on A549 lung cancer cells. Tissue kallikrein stimulates DU145 cell proliferation through activation of the kinin B2 receptor, but not PAR1 and EGFR activation. Tissue kallikrein promotes migration and invasion of DU145 cells through PAR1-PKC-Src-MMP activation and EGFR-ERK transactivation. Tissue kallikrein stimulates ERK activation through EGFR transactivation. Differential signaling pathways mediated by tissue kallikrein in promoting prostate cancer cell migration and invasion via PAR1 activation, and proliferation via kinin B2 receptor stimulation. Stimulates ERK phosphorylation
physiological function
-
beneficial effects of kallidinogenase on increased retinal vascular permeability and vascular endothelial growth factor in diabetic rats. Improvement in abnormal NO metabolism by kallidinogenase suggesting that the kallikrein-kinin system disturbance is corrected
physiological function
-
tissue kallikrein promotes cell migration and proliferation of HaCaT keratinocytes in a concentration- and time-dependent manner. Active TK stimulates keratinocyte migration independent of kinin, kinin B2 receptor and NO formation. Tissue kallikrein-induced keratinocyte migration is dependent on PAR1 activation and EGFR phosphorylation. Local application of tissue kallikrein promotes skin wound healing. Signaling pathways mediated by tissue kallikrein promote keratinocyte migration through activation of the PAR1-PKC-Src-MMP pathway and HB-EGF/AR shedding-dependent EGFR transactivation
physiological function
-
tissue kallikrein has antioxidant characteristics and is capable of alleviating ischemia-acidosis/reperfusion-induced injury, inhibiting apoptosis and promoting cell survival in vitro: pretreatment of cultured cortical neurons from rats with tissue kallikrein reduces cell death induced by either acidosis or oxygen and glucose deprivation-acidosis/reoxygenation. It exerts the neuroprotective effects by reducing production of reactive oxygen species, stabilizing the mitochondrial membrane potential and inhibiting caspase-3 activation, and thereby attenuating oxidative stress and apoptosis. Activation of the extracellular signal-regulated kinase1/2 signaling cascade but not the PI3K/Akt signaling pathway is required for the survival-promoting effect of tissue kallikrein on neurons exposed to oxygen and glucose deprivation-acidosis/reoxygenation
physiological function
-
HUK reduces brain damage in experimental stroke: in a mouse middle cerebral artery occlusion model, HUK significantly improves neurofunction, decreases infarct size, and suppresses edema, as well as inflammatory mediators as compared with the vehicle group. Furthermore, HUK inhibits the NF-kappaB pathway and activates the MAPK/ERK pathway in this neuroprotection
physiological function
-
pretreatment of cultured cortical neurons from rats with tissue kallikrein largely prevents glutamate-induced morphological changes and cell death: tissue kallikrein pretreatment alleviates glutamate-induced oxidative stress by inhibiting neuronal nitric oxide synthase activity, thereby reducing the generation of nitric oxide and reactive oxygen species. Extracellular signal-regulated kinase 1/2 cascade (ERK1/2), particularly ERK1, and nuclear factor-kappaB are involved in tissue kallikrein neuroprotection against glutamate-induced neurotoxicity. Tissue kallikrein pretreatment activates ERK1 and nuclear factor-kappaB, leading to enhanced expression of brain-derived neurotrophic factor mRNA and antiapoptotic gene Bcl-2 protein
physiological function
-
role of the kallikrein-kinin system in diabetic nephropathy
physiological function
-
tumour-induced, vascular-derived tissue kallikrein that surrounds angiogenic endothelial cells likely aids in stromal remodelling to allow angiogenesis and the release of contributing co-factors, contributes to neo-vasculature invasiveness and produces a tempero-spatial chemotactic message that may be recognised by cell signaling systems
physiological function
-
tissue kallikrein inhibits vascular endothelial growth factor-165-induced tube formation, proliferation, and migration in vitro angiogenesis model via suppression of the vascular endothelial growth factor-165-induced phosphorylation of vascular endothelial growth factor receptor-2. Tissue kallikrein is partly involved in pathogenesis of proliferative diabetic retinopathy
physiological function
-
tissue kallikrein prevents neurons from hypoxia/reoxygenation damage by influencing the activity of bradykinin B2 receptor followed by activating the ERK1/2 signal pathway, and thus promoting the survival of cortical neurons subjected to ischemia/reperfusion insults
physiological function
-
human tissue kallikrein is produced and released by gastrointestinal stromal tumor and participates in tumor invasion. Human tissue kallikrein released by gastrointestinal stromal tumor cells promotes endothelial cell migration and network formation through kinin-dependent mechanisms
physiological function
-
tissue kallikrein is essential for invasive capacity of circulating proangiogenic cells
physiological function
-
tissue kallikrein acts directly on epithelial sodium channel in order to modulate its activity but is not critical for the regulation of renal sodium homeostasis. Tissue kallikrein is a kaliuretic factor that provides a rapid abd aldosterone-independent protection against hyperkalemia after a dietary potassium load
physiological function
-
human tissue kallikrein promotes activation of the ipsilesional sensorimotor cortex after acute cerebral infarction. Tissue kallikrein improves neural function effectively and quickly after stroke, and promoting cerebral reorganization is an important mechanism for tissue kallikrein in the treatment of acute cerebral infarction
physiological function
-
tissue kallikrein is a unique kalliuretic factor that protects against hyperkalemia after a dietary potassium load
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-aminobenzoyl-MISLMKRPPGFSPFRSS(PO3H2)RI-NH2 + H2O
2-aminobenzoyl-MISLM + KRPPGFSPFRSS(PO3H2)RI-NH2
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-MISLMKRPPGFSPFRSSRI-NH2 + H2O
2-aminobenzoyl-MISLM + KRPPGFSPFRSSRI-NH2
show the reaction diagram
-
-
-
-
?
Ac-GKAFRR-L12ADT + H2O
?
show the reaction diagram
-
peptide coupled to cytotoxin thapsigarin, L12ADT, as an enzyme-activated prodrug. Enzyme cleaves at R-residue adjacent to L12ADT
-
-
?
acetyl-Ala-Arg methyl ester + H2O
acetyl-Ala-Arg + methanol
show the reaction diagram
-
-
-
-
?
acetyl-Ala-Arg-Arg methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Ala-Leu-Arg-p-nitroanilide + H2O
acetyl-Ala-Leu-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-Ala-Phe-Arg methyl ester + H2O
acetyl-Ala-Phe-Arg + methanol
show the reaction diagram
-
-
-
-
?
acetyl-Ala-Phe-Arg-Ala-NH2 + H2O
acetyl-Ala-Phe-Arg + Ala-NH2
show the reaction diagram
-
-
-
-
?
acetyl-Ala-Phe-Arg-p-nitroanilide + H2O
acetyl-Ala-Phe-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-Ala-Thr-Arg-p-nitroanilide + H2O
acetyl-Ala-Thr-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-Arg methyl ester + H2O
acetyl-Arg + methanol
show the reaction diagram
-
-
-
-
?
acetyl-Arg-Ala-NH2 + H2O
acetyl-Arg + Ala-NH2
show the reaction diagram
-
-
-
-
?
acetyl-Arg-p-nitroanilide + H2O
acetyl-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-D-Ala-Arg methyl ester + H2O
acetyl-D-Ala-Arg + methanol
show the reaction diagram
-
-
-
-
?
acetyl-D-Phe-Arg methyl ester + H2O
acetyl-D-Phe-Arg + methanol
show the reaction diagram
-
-
-
-
?
acetyl-Glu-Leu-Arg-p-nitroanilide + H2O
acetyl-Glu-Leu-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-Glu-Lys-Arg-p-nitroanilide + H2O
acetyl-Glu-Lys-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-Glu-Phe-Arg-p-nitroanilide + H2O
acetyl-Glu-Phe-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-Glu-Thr-Arg-p-nitroanilide + H2O
acetyl-Glu-Thr-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-Gly-Arg methyl ester + H2O
acetyl-Gly-Arg + methanol
show the reaction diagram
-
-
-
-
?
acetyl-Gly-Arg-Ser-Val-Gln + H2O
acetyl-Gly-Arg + Ser-Val-Gln
show the reaction diagram
-
-
-
?
acetyl-Ile-Arg methyl ester + H2O
acetyl-Ile-Arg + methanol
show the reaction diagram
-
-
-
-
?
acetyl-Leu-Arg methyl ester + H2O
acetyl-Leu-Arg + methanol
show the reaction diagram
-
-
-
-
?
acetyl-Met-Arg methyl ester + H2O
acetyl-Met-Arg + methanol
show the reaction diagram
-
-
-
-
?
acetyl-Phe-Arg methyl ester + H2O
acetyl-Phe-Arg + methanol
show the reaction diagram
-
-
-
-
?
acetyl-Phe-Arg methyl ester + H2O
acetyl-Phe-Arg + methanol
show the reaction diagram
-
-
-
-
?
acetyl-Phe-Arg-p-nitroanilide + H2O
acetyl-Phe-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-Phe-Arg-Ser-NH2 + H2O
acetyl-Phe-Arg + Ser-NH2
show the reaction diagram
-
-
-
?
acetyl-Phe-Arg-Ser-Val-Gln + H2O
acetyl-Phe-Arg + Ser-Val-Gln
show the reaction diagram
-
-
-
?
acetyl-Phe-Arg-Ser-Val-NH2 + H2O
acetyl-Phe-Arg + Ser-Val-NH2
show the reaction diagram
-
-
-
?
acetyl-Pro-Arg methyl ester + H2O
acetyl-Pro-Arg + methanol
show the reaction diagram
-
-
-
-
?
acetyl-Pro-Phe-Arg methyl ester + H2O
acetyl-Pro-Phe-Arg + methanol
show the reaction diagram
-
-
-
-
?
acetyl-Pro-Phe-Arg-Ala-NH2 + H2O
acetyl-Pro-Phe-Arg + Ala-NH2
show the reaction diagram
-
-
-
-
?
acetyl-Pro-Phe-Arg-p-nitroanilide + H2O
acetyl-Pro-Phe-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-Trp-2-aminohexanoic acid methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Tyr-Arg methyl ester + H2O
acetyl-Tyr-Arg + methanol
show the reaction diagram
-
-
-
-
?
acetyl-Val-Arg methyl ester + H2O
acetyl-Val-Arg + methanol
show the reaction diagram
-
-
-
-
?
Ala-Ala-Arg-7-amido-4-methylcoumarin + H2O
Ala-Ala-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Angiotensin I + H2O
?
show the reaction diagram
-
reaction with prostate enzyme, very low reaction with submandibular enzyme
-
-
?
angiotensinogen + H2O
angiotensin
show the reaction diagram
-, P06870
-
-
-
?
angiotensinogen + H2O
?
show the reaction diagram
-
reaction with prostate enzyme, no reaction with submandibular enzyme
-
-
?
benzoyl-Phe-Val-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-Phe-Val-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
benzoyl-Pro-Phe-Arg-p-nitroanilide + H2O
benzoyl-Pro-Phe-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Arg methyl ester + H2O
benzyloxycarbonyl-Arg + methanol
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Arg methyl ester + H2O
benzyloxycarbonyl-Arg + methanol
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Arg-Ala-NH2 + H2O
benzyloxycarbonyl-Arg + Ala-NH2
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Arg-p-nitroanilide + H2O
benzyloxycarbonyl-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
-
benzyloxycarbonyl-Arg-p-nitroanilide + H2O
benzyloxycarbonyl-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-Lys methyl ester + H2O
Benzyloxycarbonyl-Lys + methanol
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
about 30% of the activity with Pro-Phe-Arg-4-methylcoumarin 7-amide
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amino-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Pro-Gly-Arg methyl ester + H2O
benzyloxycarbonyl-Pro-Gly-Arg + methanol
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Pro-Phe-Arg methyl ester + H2O
benzyloxycarbonyl-Pro-Phe-Arg + methanol
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Tyr-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Tyr + 4-nitrophenol
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
citrated dog plasma + H2O
?
show the reaction diagram
-
-
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
show the reaction diagram
-
weak activity
-
-
?
D-Pro-Phe-Arg-4-methylcoumarin-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
weak activity
-
-
?
D-Pro-Phe-Phe-4-methylcoumarin-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
D-Pro-Phe-Phe-7-amido4-methylcoumarin + H2O
D-Pro-Phe-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
-
D-Val-Leu-Arg-4-nitroanilide + H2O
D-Val-Leu-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
D-Val-Leu-Arg-4-nitroanilide + H2O
D-Val-Leu-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
D-Val-Leu-Arg-4-nitroanilide + H2O
D-Val-Leu-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
D-Val-Leu-Arg-4-nitroanilide + H2O
D-Val-Leu-Arg + 4-nitroaniline
show the reaction diagram
-
also known as S2266, a chromogenic substrate for tissue kallikrein
-
-
?
D-Val-Leu-Arg-4-nitroanilide + H2O
D-Val-Leu-Arg + 4-nitroaniline
show the reaction diagram
-
S-2266, selective tissue kallikrein substrate
-
-
?
D-Val-Leu-Arg-7-amido-4-trifluoromethylcoumarin + H2O
D-Val-Leu-Arg + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
D-Val-Leu-Arg-p-nitroanilide + H2O
D-Val-Leu-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
D-Val-Leu-Arg-p-nitroanilide + H2O
D-Val-Leu-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
D-Val-Leu-Arg-p-nitroanilide + H2O
D-Val-Leu-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
D-Val-Leu-Arg-p-nitroanilide + H2O
D-Val-Leu-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
D-Val-Leu-Arg-p-nitroanilide + H2O
D-Val-Leu-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
D-Val-Leu-Arg-p-nitroanilide + H2O
D-Val-Leu-Arg + p-nitroaniline
show the reaction diagram
-
weak activity
-
-
-
D-Val-Leu-Arg-p-nitroanilide + H2O
D-Val-Leu-Arg + p-nitroaniline
show the reaction diagram
-
weak activity
-
-
?
D-Val-Leu-Lys-4-nitroanilide + H2O
D-Val-Leu-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
D-Val-Leu-Lys-4-nitroanilide + H2O
D-Val-Leu-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
D-Val-Leu-Lys-4-nitroanilide + H2O
D-Val-Leu-Lys + 4-nitroaniline
show the reaction diagram
-
weak activity
-
-
?
DL-Val-Leu-Arg-p-nitroanilide + H2O
DL-Val-Leu-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
-
DL-Val-Leu-Arg-p-nitroanilide + H2O
DL-Val-Leu-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
DL-Val-Leu-Arg-p-nitroanilide + H2O
DL-Val-Leu-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
FSPFRSVQ + H2O
FSPFR + SVQ
show the reaction diagram
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
Gln-Ala-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
Q9UBX7
-
-
-
?
Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
Gly-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
Q9UBX7
-
-
-
?
H-D-Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
H-D-Pro-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
i.e. S-2302
-
-
?
insulin-like growth factor binding protein + H2O
?
show the reaction diagram
-
-
-
-
?
insulin-like growth factor binding proteins
insulin-like growth factor binding protein fragments
show the reaction diagram
-
i.e. IGFBP, degradation of IGFBP 2-5
identification of products
?
insulin-like growth factor binding proteins
?
show the reaction diagram
-
i.e. IGFBP, degradation of IGFBP 2-5, enhancement of IGF bioavailability, role in tumor progression
-
-
?
kinin B2 receptor + H2O
?
show the reaction diagram
-
tissue kallikrein directly activates kinin B2 receptor in the absence of kininogen
-
-
?
kininogen + H2O
kinin + ?
show the reaction diagram
-
-
-
-
?
kininogen + H2O
kinin + ?
show the reaction diagram
-
-
-
-
-
kininogen + H2O
kinin + ?
show the reaction diagram
-
-
-
?
kininogen + H2O
kinin + ?
show the reaction diagram
-
-
-
?
kininogen + H2O
kinin + ?
show the reaction diagram
-
-
-
?
kininogen + H2O
kinin + ?
show the reaction diagram
-
-
-
?
kininogen + H2O
kinin + ?
show the reaction diagram
-
-
-
?
kininogen + H2O
kinin + ?
show the reaction diagram
-
-
-
-
?
kininogen + H2O
kinin + ?
show the reaction diagram
-
-
-
?
kininogen + H2O
kinin + ?
show the reaction diagram
-
-
-
?
kininogen + H2O
kinin + ?
show the reaction diagram
-
-
-
-
?
kininogen + H2O
kinin + ?
show the reaction diagram
-
-
-
?
kininogen + H2O
kinin + ?
show the reaction diagram
-
-
-
-
?
kininogen + H2O
kinin + ?
show the reaction diagram
-
-
-
?
kininogen + H2O
kinin + ?
show the reaction diagram
-
wild-type and recombinant enzyme
-
-
?
kininogen + H2O
kinin + ?
show the reaction diagram
-
high molecular weight kininogen from human and rat
-
-
?
kininogen + H2O
kinin + ?
show the reaction diagram
-
high molecular weight kininogen from human and rat
-
?
kininogen + H2O
kinin + ?
show the reaction diagram
-
high-molecular weight kininogen
-
-
?
kininogen + H2O
kinin + ?
show the reaction diagram
-
acts preferentially in low molecular weight kininogen
-
-
?
kininogen + H2O
kinin + ?
show the reaction diagram
-
rat low molecular weight kininogen and bovine low molecular weight kininogen, T-kininogen
-
?
kininogen + H2O
bradykinin + kinin heavy chain + kinin light chain
show the reaction diagram
-
high-molecular weight kininogen
-
?
kininogen + H2O
bradykinin + kinin heavy chain + kinin light chain
show the reaction diagram
-
cleavage of rat kininogen at Arg-Arg and Arg-Ser
-
?
kininogen + H2O
bradykinin + kinin heavy chain + kinin light chain
show the reaction diagram
-
3 additional cleavage sites at Arg427, Arg437, and Arg457
-
?
kininogen + H2O
bradykinin + kinin heavy chain + kinin light chain
show the reaction diagram
-
important role in bradykinin release in seminal fluid
-
?
kininogen + H2O
bradykinin + kinin
show the reaction diagram
-
high-molecular weight kininogen, 3 additional claevage sites at Arg427, Arg437, and Arg457
-
?
kininogen + H2O
bradykinin + ?
show the reaction diagram
-
-
-
-
?
kininogen + H2O
kallidin + kinin heavy chain + kinin light chain
show the reaction diagram
-
-
-
-
?
kininogen + H2O
kallidin + kinin heavy chain + kinin light chain
show the reaction diagram
-, P06870
best substrate
-
-
?
kininogen + H2O
kallidin + kinin heavy chain + kinin light chain
show the reaction diagram
-, P06870
enzyme is involved in inflammation, sepsis, pancreatitis, bone metabolism, heart disease, renal disease, and cancer through release of kallidin, i.e. Lys-bradykinin
-
-
?
kininogen + H2O
kinin + bradykinin
show the reaction diagram
-
-
-
-
?
L-Pro-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Pro-L-Phe-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Laminin + H2O
?
show the reaction diagram
-
-
-
-
?
Leu-Leu-Arg-7-amido-4-methylcoumarin + H2O
Leu-Leu-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
low density lipoprotein + H2O
?
show the reaction diagram
-, P06870
-
-
-
?
low molecular weight kininogen + H2O
kallidin + kinin
show the reaction diagram
-
-
-
-
?
low-molecular-weight kininogen + H2O
kallidin + kinin
show the reaction diagram
-
-
-
?
low-molecular-weight kininogen + H2O
kallidin + kinin
show the reaction diagram
-
-
-
?
low-molecular-weight kininogen + H2O
kallidin + kinin
show the reaction diagram
-
-
-
?
low-molecular-weight kininogen + H2O
kallidin + kinin
show the reaction diagram
-
-
-
?
low-molecular-weight kininogen + H2O
kallidin + kinin
show the reaction diagram
-
-
-
?
low-molecular-weight kininogen + H2O
kallidin + kinin
show the reaction diagram
-
-
-
?
low-molecular-weight kininogen + H2O
kallidin + kinin
show the reaction diagram
-
-
-
?
low-molecular-weight kininogen + H2O
kallidin + kinin
show the reaction diagram
-
-
-
-
?
low-molecular-weight kininogen + H2O
kallidin + kinin
show the reaction diagram
-
-
-
?
low-molecular-weight kininogen + H2O
kallidin + kinin
show the reaction diagram
-
-
-
?
low-molecular-weight kininogen + H2O
kallidin + kinin
show the reaction diagram
-
-
-
?
low-molecular-weight kininogen + H2O
kallidin + kinin
show the reaction diagram
-
-
-
?
low-molecular-weight kininogen + H2O
kallidin + kinin
show the reaction diagram
-
-
-
-
?
low-molecular-weight kininogen + H2O
kallidin + kinin
show the reaction diagram
-
-
-
?
low-molecular-weight kininogen + H2O
kallidin + kinin
show the reaction diagram
-, P06870
-
kallidin is Lys-bradykinin
?
low-molecular-weight kininogen + H2O
kallidin + kinin
show the reaction diagram
-
-
kallidin is Lys-bradykinin
?
low-molecular-weight kininogen + H2O
kallidin + kinin
show the reaction diagram
-
-
kallidin is Lys-bradykinin
?
low-molecular-weight kininogen + H2O
kallidin + kinin
show the reaction diagram
-
-
kallidin is Lys-bradykinin
?
low-molecular-weight kininogen + H2O
kallidin + kinin
show the reaction diagram
-
human
-
?
low-molecular-weight kininogen + H2O
kallidin + kinin
show the reaction diagram
-
bovine or human
-
?
N-alpha-acetyl-Phe-Arg ethyl ester + H2O
N-alpha-acetyl-Phe-Arg + ethanol
show the reaction diagram
-
-
-
-
?
N-alpha-acetyl-Tyr ethyl ester + H2O
N-alpha-acetyl-Tyr + ethanol
show the reaction diagram
-
-
-
-
?
N-alpha-acetyl-Tyr ethyl ester + H2O
N-alpha-acetyl-Tyr + ethanol
show the reaction diagram
-
-
-
-
?
N-alpha-benzoyl-L-Arg ethyl ester + H2O
N-alpha-benzoyl-L-Arg + ethanol
show the reaction diagram
-
-
-
-
?
N-alpha-benzoyl-L-Arg ethyl ester + H2O
N-alpha-benzoyl-L-Arg + ethanol
show the reaction diagram
-
-
-
-
?
N-alpha-benzoyl-L-Arg methyl ester + H2O
N-alpha-benzoyl-L-Arg + methanol
show the reaction diagram
-
-
-
-
?
N-alpha-benzoyl-L-Arg methyl ester + H2O
N-alpha-benzoyl-L-Arg + methanol
show the reaction diagram
-
-
-
-
?
N-alpha-benzoyl-L-citrulline methyl ester + H2O
N-alpha-benzoyl-L-citrulline + methanol
show the reaction diagram
-
-
-
-
?
N-alpha-benzoyl-L-Lys methyl ester + H2O
N-alpha-benzoyl-L-Lys + methanol
show the reaction diagram
-
-
-
-
?
N-alpha-benzoyl-L-Lys methyl ester + H2O
N-alpha-benzoyl-L-Lys + methanol
show the reaction diagram
-
-
-
-
?
N-alpha-benzoyl-L-Orn methyl ester + H2O
N-alpha-benzoyl-L-Orn + methanol
show the reaction diagram
-
-
-
-
?
N-alpha-tosyl-L-arginine methyl ester + H2O
N-alpha-tosyl-L-arginine + methanol
show the reaction diagram
-
-
-
-
?
N-methoxysuccinyl-Arg-Pro-Tyr-4-nitroanilide + H2O
N-methoxysuccinyl-Arg-Pro-Tyr + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-AIKFFIRE-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-AIKFF + IRE-N-(2,4-dinitrophenyl)ethylene diamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-AIKFFQRE-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-AIKFF + QRE-N-(2,4-dinitrophenyl)ethylene diamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-AIKFFSAE-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-AIKFF + SAE-N-(2,4-dinitrophenyl)ethylene diamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-AIKFFSKE-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-AIKFF + SKE-N-(2,4-dinitrophenyl)ethylene diamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-AIKFFSPE-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-AIKFF + SPE-N-(2,4-dinitrophenyl)ethylene diamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-AIKFFSRE-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-AIKFF + SRE-N-(2,4-dinitrophenyl)ethylene diamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-AIKFFSRQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-AIKFF + SRQ-N-(2,4-dinitrophenyl)ethylene diamine
show the reaction diagram
-
substrate sequence is derived from the kallistatin reactive centre loop sequence
-
?
o-aminobenzoyl-AIKFFSSE-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-AIKFF + SSE-N-(2,4-dinitrophenyl)ethylene diamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-AIKFFTRE-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-AIKFF + TRE-N-(2,4-dinitrophenyl)ethylene diamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-FRAPR-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-FRLVR-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-FRSSR-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-FR + SSR-N-(2,4-dinitrophenyl)ethylene diamine
show the reaction diagram
-
sequence spanning the scissile Arg-Ser bond in human kininogen
-
?
o-aminobenzoyl-FRSVQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-FR + SVQ-N-(2,4-dinitrophenyl)ethylene diamine
show the reaction diagram
-
sequence spanning the scissile Arg-Ser bond in bovine kininogen
-
?
o-aminobenzoyl-GFSPF-4-(aminocyclohexyl)alanine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
show the reaction diagram
-
synthetic internally quenched fluorescent peptides with substitution for a non-natural amino acid, sequence is based on the human kininogen sequence at the C-terminal region of bradykinin
-
-
?
o-aminobenzoyl-GFSPF-4-(aminomethyl)-N-isopropylphenylalanine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
show the reaction diagram
-
synthetic internally quenched fluorescent peptides with substitution for a non-natural amino acid, sequence is based on the human kininogen sequence at the C-terminal region of bradykinin
-
-
?
o-aminobenzoyl-GFSPF-4-(aminomethyl)phenylalanine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
show the reaction diagram
-
synthetic internally quenched fluorescent peptides with substitution for a non-natural amino acid, sequence is based on the human kininogen sequence at the C-terminal region of bradykinin
-
-
?
o-aminobenzoyl-GFSPF-4-piperidinylalanine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
show the reaction diagram
-
synthetic internally quenched fluorescent peptides with substitution for a non-natural amino acid, sequence is based on the human kininogen sequence at the C-terminal region of bradykinin
-
-
?
o-aminobenzoyl-GFSPF-Nim-(dimethyl)histidine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
show the reaction diagram
-
synthetic internally quenched fluorescent peptides with substitution for a non-natural amino acid, sequence is based on the human kininogen sequence at the C-terminal region of bradykinin
-
-
?
o-aminobenzoyl-GFSPFRAPRVQ-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-GFSPFR + APRVQ-ethylenediamine 2,4-dinitrophenol + o-aminobenzoyl-GFSPF + RAPRVQ-ethylenediamine 2,4-dinitrophenol
show the reaction diagram
-
preferentially hydrolyzed at Phe-Arg bond compared with Phe-Arg
-
-
?
o-aminobenzoyl-GFSPFRSSRIGEIKEEQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-GFSPFR + SSRIGEIKEEQ-N-(2,4-dinitrophenyl)ethylene diamine
show the reaction diagram
-
sequence spanning the scissile Arg-Ser bond in human kininogen
-
?
o-aminobenzoyl-GFSPFRSSRQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-GFSPFR + SSRQ-N-(2,4-dinitrophenyl)ethylene diamine
show the reaction diagram
-
sequence spanning the scissile Arg-Ser bond in human kininogen
-
?
o-aminobenzoyl-GFSPFRSVQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-GFSPFR + SVQ-N-(2,4-dinitrophenyl)ethylene diamine
show the reaction diagram
-
sequence spanning the scissile Arg-Ser bond in bovine kininogen
-
?
o-aminobenzoyl-GFSPFRSVQVMKYEGSQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-GFSPFR + SVQVMKYEGSQ-N-(2,4-dinitrophenyl)ethylene diamine
show the reaction diagram
-
sequence spanning the scissile Arg-Ser bond in bovine kininogen
-
?
o-aminobenzoyl-GFSPFRSVTVQ-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-GFSPFR + SVTVQ-ethylenediamine 2,4-dinitrophenol
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-LMKRP-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-LM + KRP-N-(2,4-dinitrophenyl)ethylene diamine
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-LMKRP-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-LM + KRP-N-(2,4-dinitrophenyl)ethylene diamine
show the reaction diagram
-
low activity
-
?
o-aminobenzoyl-LMKRP-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-LM + KRP-N-(2,4-dinitrophenyl)ethylene diamine
show the reaction diagram
-
sequence spanning the scissile Met-Lys bond in human and bovine kininogen
-
?
o-aminobenzoyl-LPRTMFIQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
show the reaction diagram
-
shortened, quenched fluorescent substrate, synthesized based on Bauhinia ungulata factor Xa inhibitor reactive sequence site
-
-
?
o-aminobenzoyl-LPRTMQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
show the reaction diagram
-
shortened, quenched fluorescent substrate, synthesized based on Bauhinia ungulata factor Xa inhibitor reactive sequence site
-
-
?
o-aminobenzoyl-MTEMARRPPGFSPFRSVTVQ-NH2 + H2O
o-aminobenzoyl-MTEMAR + RPPGFSPFR + SVTVQ-NH2
show the reaction diagram
-
-
RPPGFSPFR is bradykinin
-
?
o-aminobenzoyl-MTEMARRPQ-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-MTEMAR + RPQ-ethylenediamine 2,4-dinitrophenol
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-MTSVIRRPPGFSPFRAPRV-NH2 + H2O
des[Arg9] bradykinin + ?
show the reaction diagram
-
preferential hydrolysis of Phe-Arg compared with Arg-Ala bond, preferential release of des[Arg9] bradykinin
-
-
?
o-aminobenzoyl-MTSVIRRPPGFSPFRAPRV-NH2 + H2O
o-aminobenzoyl-MTSVIR + RPPGFSPFR + APRV-NH2
show the reaction diagram
-
-
RPPGFSPFR is bradykinin
-
?
o-aminobenzoyl-MTSVIRRPQ-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-MTSVIR + RPQ-ethylenediamine 2,4-dinitrophenol
show the reaction diagram
-
slow hydrolysis
-
-
?
o-aminobenzoyl-Phe-4-(aminomethyl)phenylalanine-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-Phe-4-(aminomethyl)phenylalanine-Ser-Arg + Gln-N-(2,4-dinitrophenyl)ethylene diamine
show the reaction diagram
-
synthetic internally quenched fluorescent peptides with substitution for a non-natural amino acid, sequence is based on the human kininogen sequence at the C-terminal region of bradykinin
-
-
?
o-aminobenzoyl-Phe-Arg-Arg--ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-Phe-Arg + Arg-ethylenediamine 2,4-dinitrophenol
show the reaction diagram
-
slow hydrolysis
-
-
?
o-aminobenzoyl-Phe-Arg-Arg-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-Phe-Arg + Arg-ethylenediamine 2,4-dinitrophenol
show the reaction diagram
-
slow hydrolysis
-
-
?
o-aminobenzoyl-Phe-Arg-Lys-GFSPFRSVTVQ-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-Phe-Arg + Lys-ethylenediamine 2,4-dinitrophenol
show the reaction diagram
-
slow hydrolysis
-
-
?
o-aminobenzoyl-Phe-Nim-(dimethyl)histidine-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-Phe-Nim-(dimethyl)histidine-Ser-Arg + Gln-N-(2,4-dinitrophenyl)ethylene diamine
show the reaction diagram
-
synthetic internally quenched fluorescent peptides with substitution for a non-natural amino acid, sequence is based on the human kininogen sequence at the C-terminal region of bradykinin
-
-
?
o-aminobenzoyl-QPLGMISLMKRP-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-QPLGMISLM + KRP-N-(2,4-dinitrophenyl)ethylene diamine
show the reaction diagram
-
sequence spanning the scissile Met-Lys bond in human kininogen
-
?
o-aminobenzoyl-QPLGQTSLMKRP-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-QPLGQTSLM + KRP-N-(2,4-dinitrophenyl)ethylene diamine
show the reaction diagram
-
sequence spanning the scissile Met-Lys bond in bovine kininogen
-
?
o-aminobenzoyl-SVIRRVQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-TSVIRRPQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-VMIAALPRTMFIQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
show the reaction diagram
-
low activity, quenched fluorescent substrate, synthesized based on Bauhinia ungulata factor Xa inhibitor reactive sequence site
-
-
?
o-aminobenzoyl-VMIAALPRTMQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
show the reaction diagram
-
low activity, quenched fluorescent substrate, synthesized based on Bauhinia ungulata factor Xa inhibitor reactive sequence site
-
-
?
PFRSVQ + H2O
PFR + SVQ
show the reaction diagram
-
-
-
?
Phe-Arg-Ser-Val-Gln + H2O
Phe-Arg + Ser-Val-Gln
show the reaction diagram
-
-
-
?
Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
Phe-Ser-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
Q9UBX7
-
-
-
?
poly-L-Arg + H2O
?
show the reaction diagram
-
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-, P06870
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
P06870
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
S1' and S2' subsites of the enzyme play a determinant role in the recognition and hydrolysis of substrates, serine at position P1' and arginine at position P2' result in high activity, serine at position P1' and arginine at position P2' results in high activity
-
?
polypeptide + H2O
peptides
show the reaction diagram
-, P06870
implicated in processing of growth factrors and peptide hormones
-
?
precursor of atrial natriuretic factor + H2O
natriuretic factor
show the reaction diagram
-, P06870
-
-
-
?
pro-collagenase + H2O
collagease
show the reaction diagram
-, P06870
-
-
-
?
pro-insulin + H2O
insulin + fragment
show the reaction diagram
-, P06870
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
reaction catalyzed by mK13
-
-
?
Pro-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
Pro-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
Q9UBX7
-
-
-
?
Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
pro-renin + H2O
renin
show the reaction diagram
-, P06870
-
-
-
?
pro-urokinase + H2O
urokinase
show the reaction diagram
-
-
-
-
?
protein C inhibitor + H2O
?
show the reaction diagram
-
-
-
-
?
RPPGFSPFRSVQ + H2O
RPPGFSPFR + SVQ
show the reaction diagram
-
-
-
?
salmine + H2O
?
show the reaction diagram
-
-
-
-
?
semenogelin I + H2O
semenogelin I fragments
show the reaction diagram
-
-
-
-
?
semenogelin II + H2O
semenogelin II fragments
show the reaction diagram
-
-
-
-
?
single-chain tissue-type plasminogen activator + H2O
?
show the reaction diagram
-
-, glandular kallikrein 24 may play a role in degradation of extracellular matrix proteins in the interstitial area surrounding the Leydig cells of the adult mouse testis, due not only to its own activity, but also to that of plasmin produced by the single-chain tissue-type plasminogen activator-converting activity of glandular kallikrein 24
-
-
?
succinyl-Val-Pro-Phe-thiobenzyl ester + H2O
succinyl-Val-Pro-Phe + phenylmethanethiol
show the reaction diagram
-
-
-
-
?
tert-butyloxycarbonyl-Gln-Ala-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
about 15% of the activity with Pro-Phe-Arg-4-methylcoumarin 7-amide
-
-
?
tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
about 50% of the activity with Pro-Phe-Arg-4-methylcoumarin 7-amide
-
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
about 20% of the activity with Pro-Phe-Arg-4-methylcoumarin 7-amide
-
-
?
Tosyl-Arg methyl ester + H2O
Tosyl-Arg + methanol
show the reaction diagram
-
-
-
-
?
Tosyl-Arg methyl ester + H2O
Tosyl-Arg + methanol
show the reaction diagram
-
-
-
-
?
Tosyl-Arg methyl ester + H2O
Tosyl-Arg + methanol
show the reaction diagram
-
-
-
-
?
tosyl-Gly-Pro-Arg-p-nitroanilide + H2O
tosyl-Gly-Pro-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
Val-Leu-Arg-4-nitroanilide + H2O
Val-Leu-Arg + 4-nitroaniline
show the reaction diagram
-
tracheobronchial epithelial cells grown at the air/liquid interface
-
-
?
Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
Val-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
Val-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
Q9UBX7
-
-
-
?
vascular endothelial growth factor-165 + H2O
?
show the reaction diagram
-
-
-
-
?
Vasoactive intestinal peptide + H2O
?
show the reaction diagram
-, P06870
-
-
-
?
WDDDDNLLVCDVPIR + H2O
WDDDDNL + LVCDVPIR
show the reaction diagram
-
-
-
-
?
Z-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
zymogen of prostate-specific antigen + H2O
prostate-specific antigen + APLILSR
show the reaction diagram
-
-
-
-
?
zymogen of urokinase-type plasminogen activator + H2O
urokinase-type plasminogen activator
show the reaction diagram
-
activation of inactive zymogen to mature active enzyme
-
?
low-molecular-weight kininogen + H2O
kallidin + kinin
show the reaction diagram
-, P06870
cleavage sequence and sites
kallidin is Lys-bradykinin
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
substrate specificity study
-
-
-
additional information
?
-
-
substrate specificity study
-
-
-
additional information
?
-
-
no activity with substrate o-aminobenzoyl-FXSRQ-N-(2,4-dinitrophenyl)ethylene diamine harboring at position X a non-natural amino acid like 4-guanidine phenylalanine, 3-pyridylalanine, 4-(aminomethyl)cyclohexylalanine, 4-(aminomethyl)-N-isopropylphenylalanine, 4-piperidinylalanine, and 4-(aminocyclohexyl)alanine, K1, sustrate specificty of S1 subsite, accepts both Arg and Phe, no activity with substrate o-aminobenzoyl-GFSPFXSSRPQ-N-(2,4-dinitrophenyl)ethylene diamine harboring at position X a non-natural amino acid like 4-guanidine phenylalanine, 3-pyridylalanine, and 4-(aminomethyl)cyclohexylalanine
-
-
-
additional information
?
-
-
substrate specificty study by phage display
-
-
-
additional information
?
-
-
the enzyme is implicated in the pathology of various inflammatory disorders, the enzyme is an attractive target for therapeutic intervention in diseases such as asthma, pancreatitis and rheumatoid arthritis
-
-
-
additional information
?
-
-
likely the physiological activator of the zymogen form of prostate-specific antigen in the prostate
-
-
-
additional information
?
-
-
involved in prostate cancer development
-
-
-
additional information
?
-
-
involved in blood pressure regulation and inflammation processes
-
-
-
additional information
?
-
-
decrease in activity of tissue kallikrein results from a genetic mutation in humans and is associated with a newly discovered form of arterial dysfunction characterized by an inward remodeling of the brachial artery, which is not adapted to a chronic increase in wall shear stress
-
-
-
additional information
?
-
-
kallikrein 24 may play a role in the degradation of extracellular matrix proteins in the interstitial area surrounding the Leydig cells of the adult mouse testis
-
-
-
additional information
?
-
-
tissue kallikrein 4 regulates the structure and functions of the tumor-associated urokinase-type plasminogen activator receptor
-
-
-
additional information
?
-
-
tissue kallikrein plays an important role in the airways by processing the pro-form of the epidermal growth factor to mature epidermal growth factor in airway submucosal gland cells. The activity of tissue kallikrein is regulated by hyaluronan. Tissue kallikrein is inhibited in the presence of native hyaluronan in the airway and in the submucosal gland duct. Hyaluronan depolymerization is expected to cause activation of tissue kallikrein, release of epidermal growth factor and signaling of epidermal growth factor receptor and to lead to hypertrophy of tracheal submucosal gland cells and hyperplasia as well as mucus hypersecretion with subsequent airflow obstruction
-
-
-
additional information
?
-
-
tissue kallikreins may be causally involved in carcinogenesis, particularly in tumor metastasis and invasion, and thus, may represent attractive drug targets to consider for therapeutic intervention
-
-
-
additional information
?
-
Q9UBX7
the enzyme cleaves synthetic peptides after arginine but not lysine residues. It does not cleave chymotrypsin
-
-
-
additional information
?
-
-
tissue kallikrein stimulates capillary tube formation and promotes cell migration of cultured endothelial cells, expression of human tissue kallikrein in rat heart reduces infarct size after myocardial infarction, tissue kallikrein inhibits GSK-3beta activity and stimulates vascular endothelial growth factor and vascular endothelial growth factor receptor-2 expression in cultured endothelial cells
-
-
-
additional information
?
-
-
KLK1 can release des-(Arg9)-Lys-bradykinin (KRPPGFSPF) directly from human kininogen, if S391 is phosphorylated
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
insulin-like growth factor binding proteins
?
show the reaction diagram
-
i.e. IGFBP, degradation of IGFBP 2-5, enhancement of IGF bioavailability, role in tumor progression
-
-
?
kininogen + H2O
kinin + ?
show the reaction diagram
-
-
-
-
?
kininogen + H2O
bradykinin + kinin heavy chain + kinin light chain
show the reaction diagram
-
important role in bradykinin release in seminal fluid
-
?
kininogen + H2O
bradykinin + ?
show the reaction diagram
-
-
-
-
?
kininogen + H2O
kallidin + kinin heavy chain + kinin light chain
show the reaction diagram
-
-
-
-
?
kininogen + H2O
kallidin + kinin heavy chain + kinin light chain
show the reaction diagram
-, P06870
best substrate
-
-
?
kininogen + H2O
kallidin + kinin heavy chain + kinin light chain
show the reaction diagram
-, P06870
enzyme is involved in inflammation, sepsis, pancreatitis, bone metabolism, heart disease, renal disease, and cancer through release of kallidin, i.e. Lys-bradykinin
-
-
?
kininogen + H2O
kinin + bradykinin
show the reaction diagram
-
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-, P06870
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
P06870
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
S1' and S2' subsites of the enzyme play a determinant role in the recognition and hydrolysis of substrates, serine at position P1' and arginine at position P2' results in high activity
-
?
polypeptide + H2O
peptides
show the reaction diagram
-, P06870
implicated in processing of growth factrors and peptide hormones
-
?
single-chain tissue-type plasminogen activator + H2O
?
show the reaction diagram
-
glandular kallikrein 24 may play a role in degradation of extracellular matrix proteins in the interstitial area surrounding the Leydig cells of the adult mouse testis, due not only to its own activity, but also to that of plasmin produced by the single-chain tissue-type plasminogen activator-converting activity of glandular kallikrein 24
-
-
?
vascular endothelial growth factor-165 + H2O
?
show the reaction diagram
-
-
-
-
?
low-molecular-weight kininogen + H2O
kallidin + kinin
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme is implicated in the pathology of various inflammatory disorders, the enzyme is an attractive target for therapeutic intervention in diseases such as asthma, pancreatitis and rheumatoid arthritis
-
-
-
additional information
?
-
-
likely the physiological activator of the zymogen form of prostate-specific antigen in the prostate
-
-
-
additional information
?
-
-
involved in prostate cancer development
-
-
-
additional information
?
-
-
involved in blood pressure regulation and inflammation processes
-
-
-
additional information
?
-
-
decrease in activity of tissue kallikrein results from a genetic mutation in humans and is associated with a newly discovered form of arterial dysfunction characterized by an inward remodeling of the brachial artery, which is not adapted to a chronic increase in wall shear stress
-
-
-
additional information
?
-
-
kallikrein 24 may play a role in the degradation of extracellular matrix proteins in the interstitial area surrounding the Leydig cells of the adult mouse testis
-
-
-
additional information
?
-
-
tissue kallikrein 4 regulates the structure and functions of the tumor-associated urokinase-type plasminogen activator receptor
-
-
-
additional information
?
-
-
tissue kallikrein plays an important role in the airways by processing the pro-form of the epidermal growth factor to mature epidermal growth factor in airway submucosal gland cells. The activity of tissue kallikrein is regulated by hyaluronan. Tissue kallikrein is inhibited in the presence of native hyaluronan in the airway and in the submucosal gland duct. Hyaluronan depolymerization is expected to cause activation of tissue kallikrein, release of epidermal growth factor and signaling of epidermal growth factor receptor and to lead to hypertrophy of tracheal submucosal gland cells and hyperplasia as well as mucus hypersecretion with subsequent airflow obstruction
-
-
-
additional information
?
-
-
tissue kallikreins may be causally involved in carcinogenesis, particularly in tumor metastasis and invasion, and thus, may represent attractive drug targets to consider for therapeutic intervention
-
-
-
additional information
?
-
-
tissue kallikrein stimulates capillary tube formation and promotes cell migration of cultured endothelial cells, expression of human tissue kallikrein in rat heart reduces infarct size after myocardial infarction, tissue kallikrein inhibits GSK-3beta activity and stimulates vascular endothelial growth factor and vascular endothelial growth factor receptor-2 expression in cultured endothelial cells
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
Na+, K+, Li+, Rb+ or Ca2+ required for activation
K+
-
Na+, K+, Li+, Rb+ or Ca2+ required for activation
Li+
-
Na+, K+, Li+, Rb+ or Ca2+ required for activation
Na+
-
Na+, K+, Li+, Rb+ or Ca2+ required for activation
Na+
-
required for kininogenase activity
Rb+
-
Na+, K+, Li+, Rb+ or Ca2+ required for activation
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(4-amidino-phenyl)-methane-sulfonyl fluoride
Q9UBX7
2.5 mM, complete inhibition
(tris[2-carboxyethyl] phosphine) and dihydro-lipoic acid
-
13% residual activity at 3 mM
4-(2-aminoethyl)benzenesulfonyl fluoride
-
is an active-site-directed covalent inhibitor
acetyl-D-Lys-L-Phe-L-Arg-D-Arg-L-Gln-N-(2,4-dinitrophenyl)ethylene diamine
-
-
acetyl-D-Lys-L-Phe-L-Arg-D-Arg-L-Gln-NH2
-
-
acetyl-D-Lys-L-Phe-L-Arg-D-Arg-NH2
-
-
acetyl-D-Lys-L-Phe-L-Arg-L-Leu-L-Glu-NH2
-
-
acetyl-Lys-Phe-Phe-Pro-Leu-Glu-NH2
-
leader compound for design of specific inhibitors of K1; weak inhibition
Al3+
-
linear mixed inhibition
Alpha1-antitrypsin
-
-
-
Alpha1-antitrypsin
-
slowly binds to tissue kallikrein and suppresses its activity
-
antipain
-
wild-type and recombinant enzyme
antipain
-
weak
antipain
-
0.1 mM, 90% inhibition of hydrolysis of Pro-Phe-Arg-4-methylcoumarin-7-amide
Aprotinin
-
strong
Aprotinin
-
wild-type and recombinant enzyme
Aprotinin
Q9UBX7
up to 40% inhibition
Aprotinin
-
0.1 mM, 55% inhibition of hydrolysis of Pro-Phe-Arg-4-methylcoumarin-7-amide
Aprotinin
-
tissue kallikrein is inactivated by incubation with 5fold molar excess of aprotinin at 37C for 1 h
Aprotinin
-
blocks increase of DU145 cell migration and invasion by tissue kallikrein
Aprotinin
-
delays skin wound healing
Aprotinin
-
attenuates high-glucose stimulated expression of KLK1
Bauhinia bauhinioides trypsin inhibitor II
-
i.e. BbTI-II; N-terminal sequence of the protein is SVVVDTNGQPVSNGADAYYLV
-
Benzamidine
-
1 mM, 80% inhibition of hydrolysis of Pro-Phe-Arg-4-methylcoumarin-7-amide
beta-mercaptoethanol
-
65% residual activity at 15 mM
Ca2+
-
linear competitive
chymostatin
-
0.01 mM, 5% inhibition of hydrolysis of Pro-Phe-Arg-4-methylcoumarin-7-amide
cinnamoyl imidazole
-
-
convallatoxin
-
-
D-Pro-Phe-Arg-chloromethane
-
is an active-site-directed covalent inhibitor
digitoxigenin
-
-
digitoxin
-
-
dihydrolipoate
-
35% residual activity at 3 mM
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
at a slow rate
diisopropylfluorophosphate
-
2.0 mM, complete inhibition of hydrolysis of Pro-Phe-Arg-4-methylcoumarin-7-amide
dithiothreitol
-
complete inhibition at 3 mM
DX-2300
-
DX-2300 is a fully human antibody that inhibits KLK1 via a competitive inhibition mechanism. Completely inhibits KLK1-like activity in urine and saliva, inhibits KLK1-like activity by 70% in bronchoalveolar lavage fluid. Inability of DX-2300 to bind either KLK1 covalently modified with 4-(2-aminoethyl)benzenesulfonyl fluoride or D-Pro-Phe-Arg-chloromethane, thus DX-2300 binds at or near the active site of the enzyme. DX-2300 blocks oxidative-stress-induced epidermal-growth-factor receptor activation and downstream mucus cell proliferation and hypersecretion, which is mediated by KLK1. DX-2300 is a potent and specific inhibitor of KLK1 that is efficacious in in vitro and in vivo models of airway disease
-
DX-2300
-
completely inhibits KLK1-like activity in urine. In an allergic sheep model of asthma, inhalation of either 1 or 5 mg of DX-2300 inhibits high-molecular mass kininogen-induced bronchoconstriction by 49 and 68%, respectively
-
EGFR inhibitor
-
blocks tissue kallikrein's skin wound healing effect
-
Egg white
-
-
-
epidermal growth factor receptor inhibitor
-
-
-
glutathione
-
16% residual activity at 15 mM
hK11-specific monoclonal antibody
Q9UBX7
up to 40% inhibition
-
Human plasma
-
-
-
human urine
-
-
-
hyaluronic acid
-
binds to the enzyme in vivo
icatibant
-
blocks decrease of isoproterenol-induced cardiac hypertrophy and fibrosis by overexpressed tissue kallikrein in transgenic rats
icatibant
-
minimally affects increase of DU145 cell migration and invasion by tissue kallikrein
icatibant
-
blocks tissue kallikrein's skin wound healing effect
indolacryloyl imidazole
-
-
-
K+
-
linear competitive
kallikrein antibody
-
-
-
kallikrein antibody
-
-
-
kallistatin
-
complex formation, highly specific; kinetics; serine protease inhibitor, i.e. serpin, with unique P1 Phe; wild-type human kallistatin and mutants with amino acid substitutions at each P1, P2, or P3 residue, inhibitory potentials, overview
-
kallistatin
-
complex formation, highly specific; inhibitor protein mutants with amino acid substitutions of basic residues at a heparin binding site, which is essential for inhibition of kallikrein; positively charged loop on the surface of kallistatin enhances inhibition of tissue kallikrein by acting as a secondary binding site for kallikrein, model, chimeric mutants; serine protease inhibitor, i.e. serpin, with unique P1 Phe
-
kallistatin
-
-
-
Leupeptin
-
wild-type and recombinant enzyme
Leupeptin
-
weak
Leupeptin
-
0.1 mM, about 75% inhibition of hydrolysis of Pro-Phe-Arg-4-methylcoumarin-7-amide; 0.2 mM, 85% inhibition of hydrolysis of Pro-Phe-Arg-4-methylcoumarin-7-amide
Na+
-
inhibits amidase activity
Na+
-
linear competitive
Nalpha-p-tosyl-L-lysine chloromethyl ketone
-
0.1 mM, 10% inhibition of hydrolysis of Pro-Phe-Arg-4-methylcoumarin-7-amide
Nalpha-p-tosyl-L-phenylalanine chloromethyl ketone
-
0.1 mM, 5% inhibition of hydrolysis of Pro-Phe-Arg-4-methylcoumarin-7-amide
o-aminobenzoyl-AIKFFARE-N-(2,4-dinitrophenyl)ethylene diamine
-
compound gets poorly hydrolyzed as substrate and is a competitive inhibitor
o-aminobenzoyl-AIKFFERE-N-(2,4-dinitrophenyl)ethylene diamine
-
compound gets poorly hydrolyzed as substrate and is a competitive inhibitor
o-aminobenzoyl-AIKFFKRE-N-(2,4-dinitrophenyl)ethylene diamine
-
compound gets poorly hydrolyzed as substrate and is a competitive inhibitor
o-aminobenzoyl-AIKFFLRE-N-(2,4-dinitrophenyl)ethylene diamine
-
compound gets poorly hydrolyzed as substrate and is a competitive inhibitor
o-aminobenzoyl-AIKFFNRE-N-(2,4-dinitrophenyl)ethylene diamine
-
compound gets poorly hydrolyzed as substrate and is a competitive inhibitor
o-aminobenzoyl-AIKFFPRE-N-(2,4-dinitrophenyl)ethylene diamine
-
-
o-aminobenzoyl-AIKFFRRE-N-(2,4-dinitrophenyl)ethylene diamine
-
compound gets poorly hydrolyzed as substrate and is a competitive inhibitor
o-aminobenzoyl-AIKFFSEE-N-(2,4-dinitrophenyl)ethylene diamine
-
compound gets poorly hydrolyzed as substrate and is a competitive inhibitor
o-aminobenzoyl-AIKFFSIE-N-(2,4-dinitrophenyl)ethylene diamine
-
compound gets poorly hydrolyzed as substrate and is a competitive inhibitor
o-aminobenzoyl-AIKFFSLE-N-(2,4-dinitrophenyl)ethylene diamine
-
compound gets poorly hydrolyzed as substrate and is a competitive inhibitor
o-aminobenzoyl-AIKFFSNE-N-(2,4-dinitrophenyl)ethylene diamine
-
compound gets poorly hydrolyzed as substrate and is a competitive inhibitor
o-aminobenzoyl-AIKFFSQE-N-(2,4-dinitrophenyl)ethylene diamine
-
compound gets poorly hydrolyzed as substrate and is a competitive inhibitor
o-aminobenzoyl-AIKFFSTE-N-(2,4-dinitrophenyl)ethylene diamine
-
compound gets poorly hydrolyzed as substrate and is a competitive inhibitor
o-aminobenzoyl-AIKFFSVE-N-(2,4-dinitrophenyl)ethylene diamine
-
compound gets poorly hydrolyzed as substrate and is a competitive inhibitor
o-aminobenzoyl-AIKFFVRE-N-(2,4-dinitrophenyl)ethylene diamine
-
compound gets poorly hydrolyzed as substrate and is a competitive inhibitor
o-aminobenzoyl-D-Lys-L-Phe-L-Arg-D-Arg-L-Gln-N-(2,4-dinitrophenyl)ethylene diamine
-
-
o-aminobenzoyl-D-Lys-L-Phe-L-Arg-L-Pro-L-Arg-L-Gln N-(2,4-dinitrophenyl)ethylene diamine
-
-
o-aminobenzoyl-D-Lys-L-Phe-L-Phe-D-Arg-L-Gln-N-(2,4-dinitrophenyl)ethylene diamine
-
-
o-aminobenzoyl-D-Lys-L-Phe-L-Phe-L-Pro-L-Arg-L-Gln N-(2,4-dinitrophenyl)ethylene diamine
-
-
o-aminobenzoyl-D-Lys-L-Phe-L-Phe-L-Pro-L-Leu-L-Glu N-(2,4-dinitrophenyl)ethylene diamine
-
-
o-aminobenzoyl-F-4-(aminomethyl)cyclohexylalanine-SRQ-N-(2,4-dinitrophenyl)ethylene diamine
-
K1, highly specific
o-aminobenzoyl-TSVIRRPQ-ethylenediamine
-
-
p-nitrophenyl p'-guanidinobenzoate
-
-
pancratic inhibitor
-
-
-
Pepstatin
-
0.01 mM, 10% inhibition of hydrolysis of Pro-Phe-Arg-4-methylcoumarin-7-amide
peruvoside
-
-
Phe-Phe-Arg-CH2Cl
-
-
phenylmethylsulfonyl fluoride
-
-
protease inhibitor-6
-
from prostate, increased expression in prostate carcinoma; intracellular serine protease inhibitor with both antitrypsin and antichymotrypsin activity; rapid complex formation with the enzyme, involved in neoplastic progression
-
Protein C inhibitor
-
cleaves the inhibitor at Arg354-Ser355 without inactivating it; covalent complex formation with K2
-
Protein C inhibitor
-
-
-
Protein C inhibitor
-
covalent complex formation with K2
-
recombinant alpha1-antichymotrypsin
-
generation of selective inhibitors based on substrates selected from a pentapeptide phage-display library and transplanted to the reactive-site loop of alpha1-antichymotrypsin. Engineered alpha1-antichymotrypsins with peptides RGR-SE and ER-VSP are inhibitory and specific to enzyme.
-
Soybean trypsin inhibitor
-
weak
-
Soybean trypsin inhibitor
-
at high concentrations
-
Soybean trypsin inhibitor
-
no inhibition
-
Soybean trypsin inhibitor
-
kallikrein B is inhibited, kallikrein A not
-
Soybean trypsin inhibitor
-
-
-
Soybean trypsin inhibitor
-
no inhibition
-
tissue kallikrein-binding protein
-
rapidly forms a covalent complex with tissue kallikrein
-
tosyl-L-Lys-chloromethylketone
-
-
Zn2+
-
allosteric inhibition
additional information
-
no inhibition by Bauhinia bauhinioides trypsin inhibitor I
-
additional information
-
Zn2+-dependent small-molecule competitive inhibitor
-
additional information
-
not affected by heparin
-
additional information
-
not inhibited by interleukin-1beta-converting enzyme inhibitors
-
additional information
-
ascorbate is devoid of inactivating potential
-
additional information
-
cardiac glycosides can dramatically suppress the transcription of KLKs
-
additional information
-
DX-2300 is a fully human antibody, it does not inhibit the KLK1-like activity in mouse urine
-
additional information
-
kinin has little effect on increase of DU145 cell migration and invasion by tissue kallikrein. Tissue kallikrein-induced cell migration and invasion are abolished by inhibition of PAR1 using a pharmacological inhibitor or RNA interference. The effect of tissue kallikrein on cell migration and invasion are also blocked by inhibitors of protein kinase C, c-Src, matrix metalloproteinase, EGFR and extracellular signal-regulated kinase
-
additional information
-
neutralizing tissue kallikrein antibody delays skin wound healing
-
additional information
-
no inhibition by Bauhinia ungulata factor Xa inhibitor, and Bauhinia variegata trypsin inhibitor
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
aldosterone
-
increased aldosterone levels lead to enhanced kallikrein activity
Bovine serum albumin
-
1 mg/ml, activates
-
Brij-58
-
0.1%, activates
chymase
-
stimulation, in correlation with secretory leukoprotease inhibitor stimulation, in stimulated serous cells
-
deoxycholate
-
0.1%, activates
hyaluronidase
-
increases K2 enzyme activity by digesting the K2-bound hyaluronic acid
-
Lima-bean trypsin inhibitor
-
stimulates
-
Lima-bean trypsin inhibitor
-
0.017 mg/ml, activates
-
ovomucoid trypsin inhibitor
-
stimulates
-
ovomucoid trypsin inhibitor
-
0.017 mg/ml, activates
-
Soybean trypsin inhibitor
-
at low concentrations
-
Thermolysin
-
thermolysin activates prokallikrein cleaving off the N-terminal Ile1-Val2
-
Triton X-100
-
0.1%, activates
Lubrol Px
-
0.1%, activates
additional information
-
not affected by heparin
-
additional information
-
KLKs are secreted as pro-KLK zymogens upon removal of their pre-peptide signal, cleavage of the pro-peptide induces a conformational change in the active site and substrate pocket, resulting in extracellular activation of the mature enzyme
-
additional information
-
administration of glibenclamide or N,N'-dicyclohexyl-4-morholinecarboxamide increases urinary kallikrein secretion
-
additional information
-
experimental rhinovirus infection in allergic asthmatic subjects is accompanied by increased lower airway human tissue kallikrein activation
-
additional information
-
exposure of tracheobronchial epithelial cells to reactive oxygen species results in a significant increase in the amount of active KLK1
-
additional information
-
release of tissue kallikrein into the distal tubules of kidney can be stimulated by low sodium levels, high potassium levels and antidiuretic hormone
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.08
-
acetyl-2-aminohexanoic acid-Arg methyl ester
-
-
-
0.6
-
acetyl-Ala-Arg methyl ester
-
pH 9.0, 25C
-
1.14
-
acetyl-Ala-Arg methyl ester
-
pH 8.0, 25C
-
8.6
-
acetyl-Ala-Arg-Ala-NH2
-
pH 8.0, 25C
-
0.222
-
acetyl-Ala-Leu-Arg-p-nitroanilide
-
pH 8.5, 37C
-
0.035
-
acetyl-Ala-Phe-Arg methyl ester
-
pH 8.0, 25C
-
0.17
-
acetyl-Ala-Phe-Arg-Ala
-
pH 8.0, 25C
-
0.11
-
acetyl-Ala-Phe-Arg-p-nitroanilide
-
pH 8.0, 25C
0.571
-
acetyl-Ala-Thr-Arg-p-nitroanilide
-
pH 8.5, 37C
4.1
-
acetyl-Arg methyl ester
-
pH 8.0, 25C
16
-
acetyl-Arg p-nitroanilide
-
pH 8.0, 25C
14
-
acetyl-Arg-Ala-NH2
-
pH 8.0, 25C
2.5
-
acetyl-D-Ala-Arg methyl ester
-
pH 9.0, 25C
0.95
-
acetyl-D-Phe-Arg methyl ester
-
pH 9.0, 25C
0.849
-
acetyl-Glu-Leu-Arg-p-nitroanilide
-
pH 8.5, 37C
0.291
-
acetyl-Glu-Lys-Arg-p-nitroanilide
-
pH 8.5, 37C
0.765
-
acetyl-Glu-Phe-Arg-p-nitroanilide
-
pH 8.5, 37C
0.929
-
acetyl-Glu-Thr-Arg-p-nitroanilide
-
pH 8.5, 37C
0.77
-
acetyl-Gly-Arg methyl ester
-
pH 9.0, 25C
26
-
acetyl-Gly-Arg-Ser-Val-Gln
-
pH 9.0, 25C
0.199
-
acetyl-Ile-Arg methyl ester
-
pH 9.0, 25C
0.0249
-
acetyl-Leu-Arg methyl ester
-
pH 9.0, 25C
0.182
-
acetyl-Met-Arg methyl ester
-
pH 9.0, 25C
0.14
-
acetyl-Phe-Arg ethyl ester
-
-
0.0244
-
acetyl-Phe-Arg methyl ester
-
pH 9.0, 25C
0.0311
-
acetyl-Phe-Arg methyl ester
-
pH 8.0, 25C
0.27
-
acetyl-Phe-Arg-Ala-NH2
-
pH 8.0, 25C
0.15
-
acetyl-Phe-Arg-p-nitroanilide
-
pH 8.0, 25C
0.21
-
acetyl-Phe-Arg-Ser-NH2
-
pH 9.0, 25C
0.31
-
acetyl-Phe-Arg-Ser-Val-Gln
-
pH 9.0, 25C
0.04
-
acetyl-Phe-Arg-Ser-Val-NH2
-
pH 9.0, 25C
0.153
-
acetyl-Pro-Arg methyl ester
-
pH 9.0, 25C
0.089
-
acetyl-Pro-Phe-Arg methyl ester
-
pH 8.0, 25C
0.21
-
acetyl-Pro-Phe-Arg-Ala
-
pH 8.0, 25C
0.087
-
acetyl-Pro-Phe-Arg-p-nitroanilide
-
pH 8.0, 25C
0.027
-
acetyl-Trp-Arg methyl ester
-
pH 9.0, 25C
0.132
-
acetyl-Tyr-Arg methyl ester
-
pH 9.0, 25C
0.283
-
acetyl-Val-Arg methyl ester
-
pH 9.0, 25C
0.02
-
Ala-Arg-Arg-4-methylcoumarin 7-amide
-
-
0.02
-
Ala-Arg-Arg-7-amino-4-methylcoumarin
-
pH 7.5, 37C
0.45
-
benzoyl-Pro-Phe-Arg-p-nitroanilide
-
pH 8.0, 37C
0.243
-
benzyloxycarbonyl-Arg methyl ester
-
pH 8.0, 25C
1.25
-
benzyloxycarbonyl-Arg-Ala-NH2
-
pH 8.0, 25C
0.327
-
benzyloxycarbonyl-Arg-p-nitroanilide
-
pH 8.0, 25C
0.209
-
benzyloxycarbonyl-Pro-Gly-Arg methyl ester
-
-
0.0114
-
benzyloxycarbonyl-Pro-Phe-Arg methyl ester
-
pH 9.0, 25C
61.1
-
citrated bovine plasma
-
pH 7.8, 37C
-
50.8
-
citrated dog plasma
-
pH 7.8, 37C
-
0.00018
-
D-Pro-Phe-Arg-4-methylcoumarin-7-amide
-
37C, pH 8.5
0.0015
-
D-Pro-Phe-Arg-4-methylcoumarin-7-amide
-
37C, pH 8.5
0.0031
-
D-Pro-Phe-Arg-4-methylcoumarin-7-amide
-
37C, pH 8.5
0.001
-
D-Pro-Phe-Phe-4-methylcoumarin-7-amide
-
37C, pH 8.5
0.0027
-
D-Pro-Phe-Phe-4-methylcoumarin-7-amide
-
37C, pH 8.5
0.07
-
D-Pro-Phe-Phe-4-methylcoumarin-7-amide
-
37C, pH 8.5
0.0183
-
D-Val-Leu-Arg-p-nitroanilide
-
pH 8.5, 37C
0.06
-
D-Val-Leu-Arg-p-nitroanilide
-
-
28.4
-
D-Val-Leu-Arg-p-nitroanilide
-
pH 7.8, 37C
0.528
-
D-Val-Leu-Lys-p-nitroanilide
-
pH 8.0, 37C
0.868
-
D-Val-Leu-Lys-p-nitroanilide
-
pH 8.5, 37C
0.12
-
DL-Val-Leu-Arg-p-nitroanilide
-
recombinant enzyme from liver, pH 8.0, 22C
0.14
-
DL-Val-Leu-Arg-p-nitroanilide
-
natural urinary enzyme, pH 8.0, 22C
0.154
-
DL-Val-Leu-Arg-p-nitroanilide
-
recombinant enzyme from salivary gland, pH 8.0, 22C
0.158
-
DL-Val-Leu-Arg-p-nitroanilide
-
recombinant enzyme from pancreas, pH 8.0, 22C
1.83
-
DL-Val-Leu-Arg-p-nitroanilide
-
pH 8.0, 37C
58.8
-
DL-Val-Leu-Arg-p-nitroanilide
-
natural urinary enzyme, pH 8.0, 22C
0.064
-
FSPFRSVQ
-
pH 9.0, 25C
0.27
-
Gln-Ala-Arg-7-amido-4-methylcoumarin
Q9UBX7
37C, pH 7.5
1.18
-
Gly-Pro-Arg-7-amido-4-methylcoumarin
Q9UBX7
37C, pH 7.5
17.6
-
human high molecular weight kininogen
-
pH 7.8, 37C
-
12.7
-
human low molecular weight kininogen
-
pH 7.8, 37C
-
0.383
-
N-alpha-acetyl-Arg-p-nitroanilide
-
pH 8.5, 37C
50
-
N-alpha-acetyl-Tyr ethyl ester
-
pH 8.0, 40C
0.104
-
N-alpha-benzoyl-L-Arg ethyl ester
-
pH 8.0, 40C
0.125
-
N-alpha-benzoyl-L-Arg methyl ester
-
pH 8.0, 40C
0.08
-
N-alpha-benzoyl-L-arginine ethyl ester
-
Cbeta-kallikrein, pH 8.0, 25C
0.109
-
N-alpha-benzoyl-L-arginine ethyl ester
-
Abeta-kallikrein, pH 8.0, 25C
0.234
-
N-alpha-benzoyl-L-arginine ethyl ester
-
alpha-kallikrein, pH 8.0, 25C
0.333
-
N-alpha-benzoyl-L-arginine ethyl ester
-
Tbeta-kallikrein, pH 8.0, 25C
12.3
-
N-alpha-benzoyl-L-citrulline methyl ester
-
pH 8.0, 40C
2
-
N-alpha-benzoyl-L-Lys methyl ester
-
pH 8.0, 40C
2.44
-
N-alpha-benzoyl-L-Orn methyl ester
-
pH 8.0, 40C
0.031
-
N-alpha-toluenesulfonyl-L-Arg methyl ester
-
pH 8.0, 40C
0.022
-
N-alpha-tosyl-L-arginine methyl ester
-
Cbeta-kallikrein, pH 8.0, 25C
0.039
-
N-alpha-tosyl-L-arginine methyl ester
-
alpha-kallikrein, pH 8.0, 25C
0.048
-
N-alpha-tosyl-L-arginine methyl ester
-
Abeta-kallikrein, pH 8.0, 25C
0.117
-
N-alpha-tosyl-L-arginine methyl ester
-
Tbeta-kallikrein, pH 8.0, 25C
0.00027
-
o-aminobenzoyl-AIKFFIRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.00013
-
o-aminobenzoyl-AIKFFQRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.0018
-
o-aminobenzoyl-AIKFFSAE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.00021
-
o-aminobenzoyl-AIKFFSKE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.0013
-
o-aminobenzoyl-AIKFFSPE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.00036
-
o-aminobenzoyl-AIKFFSRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.00094
-
o-aminobenzoyl-AIKFFSSE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.00023
-
o-aminobenzoyl-AIKFFTRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.0002
-
o-aminobenzoyl-FRSSR-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
0.0006
-
o-aminobenzoyl-FRSSR-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
0.0009
-
o-aminobenzoyl-FRSVQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
0.0073
-
o-aminobenzoyl-FRSVQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
0.0007
-
o-aminobenzoyl-GFSPF-4-(aminocyclohexyl)alanine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.0038
-
o-aminobenzoyl-GFSPF-4-(aminomethyl)-N-isopropylphenylalanine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.0003
-
o-aminobenzoyl-GFSPF-4-(aminomethyl)phenylalanine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.00064
-
o-aminobenzoyl-GFSPF-4-piperidinylalanine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.001
-
o-aminobenzoyl-GFSPF-Nim-(dimethyl)histidine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.00096
-
o-aminobenzoyl-GFSPFRAPRVQ-ethylenediamine 2,4-dinitrophenol
-
-
0.00147
-
o-aminobenzoyl-GFSPFRAPRVQ-ethylenediamine 2,4-dinitrophenol
-
-
0.0067
-
o-aminobenzoyl-GFSPFRSSRIGEIKEEQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
0.0104
-
o-aminobenzoyl-GFSPFRSSRIGEIKEEQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
0.0004
-
o-aminobenzoyl-GFSPFRSSRQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
0.00076
-
o-aminobenzoyl-GFSPFRSSRQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
0.00035
-
o-aminobenzoyl-GFSPFRSVQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
0.0014
-
o-aminobenzoyl-GFSPFRSVQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
0.00041
-
o-aminobenzoyl-GFSPFRSVQVMKYEGSQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
0.00051
-
o-aminobenzoyl-GFSPFRSVQVMKYEGSQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
0.00017
-
o-aminobenzoyl-GFSPFRSVTVQ-ethylenediamine 2,4-dinitrophenol
-
-
0.0021
-
o-aminobenzoyl-GFSPFRSVTVQ-ethylenediamine 2,4-dinitrophenol
-
-
0.00251
-
o-aminobenzoyl-GFSPFRSVTVQ-ethylenediamine 2,4-dinitrophenol
-
-
0.0023
-
o-aminobenzoyl-LMKRP-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
0.0047
-
o-aminobenzoyl-LMKRP-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
0.0027
-
o-aminobenzoyl-LPRTMFIQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 8.0, 37C
0.0007
-
o-aminobenzoyl-LPRTMQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 8.0, 37C
0.003
-
o-aminobenzoyl-MTEMARRPQ-ethylenediamine 2,4-dinitrophenol
-
-
0.00616
-
o-aminobenzoyl-MTEMARRPQ-ethylenediamine 2,4-dinitrophenol
-
-
0.00735
-
o-aminobenzoyl-MTEMARRPQ-ethylenediamine 2,4-dinitrophenol
-
-
0.00223
-
o-aminobenzoyl-MTSVIRRPQ-ethylenediamine 2,4-dinitrophenol
-
-
0.0024
-
o-aminobenzoyl-MTSVIRRPQ-ethylenediamine 2,4-dinitrophenol
-
-
0.0036
-
o-aminobenzoyl-Phe-4-(aminomethyl)phenylalanine-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.0002
-
o-aminobenzoyl-Phe-Arg-Arg-ethylenediamine 2,4-dinitrophenol
-
-
0.00033
-
o-aminobenzoyl-Phe-Arg-Arg-ethylenediamine 2,4-dinitrophenol
-
-
0.00024
-
o-aminobenzoyl-Phe-Arg-Lys-GFSPFRSVTVQ-ethylenediamine 2,4-dinitrophenol
-
-
0.00077
-
o-aminobenzoyl-Phe-Arg-Lys-GFSPFRSVTVQ-ethylenediamine 2,4-dinitrophenol
-
-
0.0007
-
o-aminobenzoyl-Phe-Nim-(dimethyl)histidine-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.0039
-
o-aminobenzoyl-QPLGMISLMKRP-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
0.0042
-
o-aminobenzoyl-QPLGMISLMKRP-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
0.0003
-
o-aminobenzoyl-QPLGQTSLMKRP-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
0.0455
-
o-aminobenzoyl-QPLGQTSLMKRP-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
0.005
-
o-aminobenzoyl-TSVIRRVQ-ethylenediamine
-
-
0.00023
-
o-aminobenzoyl-VMIAALPRTMFIQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 8.0, 37C
0.0005
-
o-aminobenzoyl-VMIAALPRTMQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 8.0, 37C
0.057
-
PFRSVQ
-
pH 9.0, 25C
2.2
-
Phe-Arg-Ser-Val-Gln
-
pH 9.0, 25C
0.44
-
Phe-Ser-Arg-7-amido-4-methylcoumarin
Q9UBX7
37C, pH 7.5
0.07
-
Pro-Phe-Arg-4-methylcoumarin 7-amide
-
pH 9.0, 37C
0.084
-
Pro-Phe-Arg-4-methylcoumarin 7-amide
-
naturally occuring urinary enzyme, pH 8.0, 22C
0.099
-
Pro-Phe-Arg-4-methylcoumarin 7-amide
-
recombinant enzyme from liver, pH 8.0, 22C
0.112
-
Pro-Phe-Arg-4-methylcoumarin 7-amide
-
recombinant enzyme from pancreas, pH 8.0, 22C
0.114
-
Pro-Phe-Arg-4-methylcoumarin 7-amide
-
recombinant enzyme from salivary gland, pH 8.0, 22C
0.53
-
Pro-Phe-Arg-7-amido-4-methylcoumarin
Q9UBX7
37C, pH 7.5
0.04
-
Pro-Phe-Arg-Arg-7-amino-4-methylcoumarin
-
pH 7.5, 37C
0.066
-
RPPGFSPFRSVQ
-
pH 9.0, 25C
-
0.516
-
succinyl-Val-Pro-Phe-thiobenzyl ester
-
naturally occuring urinary enzyme, pH 8.0, 22C
-
0.668
-
succinyl-Val-Pro-Phe-thiobenzyl ester
-
recombinant enzyme from liver, pH 8.0, 22C
-
0.764
-
succinyl-Val-Pro-Phe-thiobenzyl ester
-
recombinant enzyme from salivary gland, pH 8.0, 22C
-
0.842
-
succinyl-Val-Pro-Phe-thiobenzyl ester
-
recombinant enzyme from pancreas, pH 8.0, 22C
-
0.103
-
tosyl-Gly-Pro-Arg-p-nitroanilide
-
pH 8.0, 37C
0.28
-
Val-Pro-Arg-7-amido-4-methylcoumarin
Q9UBX7
37C, pH 7.5
0.048
-
Val-Pro-Arg-Arg-7-amino-4-methylcoumarin
-
pH 7.5, 37C
0.067
-
Z-L-Phe-L-Arg-7-amido-4-methylcoumarin
-
pH 7.5, 25C
0.071
-
Leu-Leu-Arg-7-amido-4-methylcoumarin
-
pH 7.5, 37C
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1180
-
acetyl-2-aminohexanoic acid-Arg methyl ester
-
pH 9.0, 25C
-
682
-
acetyl-Ala-Arg methyl ester
-
pH 9.0, 25C
-
0.0542
-
acetyl-Ala-Arg-Ala-NH2
-
pH 8.0, 25C
-
6.74
-
acetyl-Ala-Leu-Arg-p-nitroanilide
-
pH 8.5, 37C
-
0.87
-
acetyl-Ala-Phe-Arg-Ala
-
pH 8.0, 25C
-
1.71
-
acetyl-Ala-Phe-Arg-p-nitroanilide
-
pH 8.0, 25C
0.72
-
acetyl-Ala-Thr-Arg-p-nitroanilide
-
pH 8.5, 37C
0.02
-
acetyl-Arg-Ala-NH2
-
pH 8.0, 25C
0.05
-
acetyl-Arg-p-nitroanilide
-
pH 8.0, 25C
4.6
-
acetyl-D-Ala-Arg methyl ester
-
pH 9.0, 25C
49
-
acetyl-D-Phe-Arg methyl ester
-
pH 9.0, 25C
9.2
-
acetyl-Glu-Leu-Arg-p-nitroanilide
-
pH 8.5, 37C
0.029
-
acetyl-Glu-Lys-Arg-p-nitroanilide
-
pH 8.5, 37C
6.62
-
acetyl-Glu-Phe-Arg-p-nitroanilide
-
pH 8.5, 37C
0.38
-
acetyl-Glu-Thr-Arg-p-nitroanilide
-
pH 8.5, 37C
385
-
acetyl-Gly-Arg methyl ester
-
pH 9.0, 25C
0.77
-
acetyl-Gly-Arg-Ser-Val-Gln
-
pH 9.0, 25C
727
-
acetyl-Ile-Arg methyl ester
-
pH 9.0, 25C
634
-
acetyl-Leu-Arg methyl ester
-
pH 9.0, 25C
1380
-
acetyl-Met-Arg methyl ester
-
pH 9.0, 25C
915
-
acetyl-Phe-Arg methyl ester
-
pH 9.0, 25C
0.81
-
acetyl-Phe-Arg-Ala-NH2
-
pH 8.0, 25C
1.69
-
acetyl-Phe-Arg-p-nitroanilide
-
pH 8.0, 25C
2.1
-
acetyl-Phe-Arg-Ser-NH2
-
pH 9.0, 25C
6.8
-
acetyl-Phe-Arg-Ser-Val-Gln
-
pH 9.0, 25C
11.6
-
acetyl-Phe-Arg-Ser-Val-NH2
-
pH 9.0, 25C
806
-
acetyl-Pro-Arg methyl ester
-
pH 9.0, 25C
0.24
-
acetyl-Pro-Phe-Arg-Ala
-
pH 8.0, 25C
0.78
-
acetyl-Pro-Phe-Arg-p-nitroanilide
-
pH 8.0, 25C
438
-
acetyl-Trp-Arg methyl ester
-
pH 9.0, 25C
680
-
acetyl-Tyr-Arg methyl ester
-
pH 9.0, 25C
964
-
acetyl-Val-Arg methyl ester
-
pH 9.0, 25C
0.12
-
Ala-Arg-Arg-7-amino-4-methylcoumarin
-
pH 7.5, 37C
0.113
-
benzyloxycarbonyl-Arg-Ala-NH2
-
pH 8.0, 25C
0.014
-
benzyloxycarbonyl-Arg-p-nitroanilide
-
pH 8.0, 25C
259
-
benzyloxycarbonyl-Pro-Gly-Arg methyl ester
-
pH 9.0, 25C
537
-
benzyloxycarbonyl-Pro-Phe-Arg methyl ester
-
pH 9.0, 25C
3.18
-
D-Pro-Phe-Arg-4-methylcoumarin-7-amide
-
37C, pH 8.5
3.2
-
D-Pro-Phe-Arg-4-methylcoumarin-7-amide
-
37C, pH 8.5
3.6
-
D-Pro-Phe-Arg-4-methylcoumarin-7-amide
-
37C, pH 8.5
95.3
-
D-Pro-Phe-Arg-4-methylcoumarin-7-amide
-
37C, pH 8.5
0.05
-
D-Pro-Phe-Phe-4-methylcoumarin-7-amide
-
37C, pH 8.5
0.085
-
D-Pro-Phe-Phe-4-methylcoumarin-7-amide
-
37C, pH 8.5
12.5
-
D-Pro-Phe-Phe-4-methylcoumarin-7-amide
-
37C, pH 8.5
6.6
-
D-Val-Leu-Arg-p-nitroanilide
-
pH 8.5, 37C
4.1
-
D-Val-Leu-Lys-p-nitroanilide
-
pH 8.5, 37C
0.8
-
DL-Val-Leu-Arg-p-nitroanilide
-
recombinant enzyme from liver, pH 8.0, 22C
1.07
-
DL-Val-Leu-Arg-p-nitroanilide
-
recombinant salivary enzyme, pH 8.0, 22C
1.16
-
DL-Val-Leu-Arg-p-nitroanilide
-
recombinant pancreatic enzyme, pH 8.0, 22C
6.4
-
FSPFRSVQ
-
pH 9.0, 25C
0.0038
-
Gln-Ala-Arg-7-amido-4-methylcoumarin
Q9UBX7
37C, pH 7.5
0.0035
-
Gly-Pro-Arg-7-amido-4-methylcoumarin
Q9UBX7
37C, pH 7.5
0.154
-
N-alpha-acetyl-Arg-p-nitroanilide
-
pH 8.5, 37C
11.2
-
N-alpha-acetyl-Tyr ethyl ester
-
pH 8.0, 25C
123
-
N-alpha-benzoyl-L-Arg ethyl ester
-
pH 8.0, 25C
154
-
N-alpha-benzoyl-L-Arg methyl ester
-
pH 8.0, 25C
53.8
-
N-alpha-benzoyl-L-arginine ethyl ester
-
Tbeta-kallikrein, pH 8.0, 25C
62.5
-
N-alpha-benzoyl-L-arginine ethyl ester
-
alpha-kallikrein, pH 8.0, 25C
81.6
-
N-alpha-benzoyl-L-arginine ethyl ester
-
Abeta-kallikrein, pH 8.0, 25C
100
-
N-alpha-benzoyl-L-arginine ethyl ester
-
Cbeta-kallikrein, pH 8.0, 25C
86.4
-
N-alpha-benzoyl-L-citrulline methyl ester
-
pH 8.0, 25C
15.5
-
N-alpha-benzoyl-L-Lys methyl ester
-
pH 8.0, 25C
1.8
-
N-alpha-benzoyl-L-Orn methyl ester
-
pH 8.0, 25C
2.7
-
N-alpha-toluenesulfonyl-L-Arg methyl ester
-
pH 8.0, 25C
2.35
-
N-alpha-tosyl-L-arginine methyl ester
-
Cbeta-kallikrein, pH 8.0, 25C
2.75
-
N-alpha-tosyl-L-arginine methyl ester
-
Abeta-kallikrein, pH 8.0, 25C
3.13
-
N-alpha-tosyl-L-arginine methyl ester
-
alpha-kallikrein, pH 8.0, 25C
9.38
-
N-alpha-tosyl-L-arginine methyl ester
-
Tbeta-kallikrein, pH 8.0, 25C
0.05
-
o-aminobenzoyl-AIKFFIRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.02
-
o-aminobenzoyl-AIKFFQRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.54
-
o-aminobenzoyl-AIKFFSAE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.21
-
o-aminobenzoyl-AIKFFSKE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.05
-
o-aminobenzoyl-AIKFFSPE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
3.33
-
o-aminobenzoyl-AIKFFSRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.3
-
o-aminobenzoyl-AIKFFSSE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.04
-
o-aminobenzoyl-AIKFFTRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
1.4
-
o-aminobenzoyl-FRSSR-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
7
-
o-aminobenzoyl-FRSSR-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
0.9
-
o-aminobenzoyl-FRSVQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
1.6
-
o-aminobenzoyl-FRSVQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
0.51
-
o-aminobenzoyl-GFSPF-4-(aminocyclohexyl)alanine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.81
-
o-aminobenzoyl-GFSPF-4-(aminomethyl)-N-isopropylphenylalanine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
1.8
-
o-aminobenzoyl-GFSPF-4-(aminomethyl)phenylalanine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.61
-
o-aminobenzoyl-GFSPF-4-piperidinylalanine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
2.1
-
o-aminobenzoyl-GFSPF-Nim-(dimethyl)histidine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
6.6
-
o-aminobenzoyl-GFSPFRAPRVQ-ethylenediamine 2,4-dinitrophenol
-
-
12
-
o-aminobenzoyl-GFSPFRAPRVQ-ethylenediamine 2,4-dinitrophenol
-
-
3
-
o-aminobenzoyl-GFSPFRSSRIGEIKEEQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
3.1
-
o-aminobenzoyl-GFSPFRSSRIGEIKEEQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
1
-
o-aminobenzoyl-GFSPFRSSRQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
7.5
-
o-aminobenzoyl-GFSPFRSSRQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
0.94
-
o-aminobenzoyl-GFSPFRSVQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
4
-
o-aminobenzoyl-GFSPFRSVQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
1.5
-
o-aminobenzoyl-GFSPFRSVQVMKYEGSQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
40.1
-
o-aminobenzoyl-GFSPFRSVQVMKYEGSQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
3.1
-
o-aminobenzoyl-GFSPFRSVTVQ-ethylenediamine 2,4-dinitrophenol
-
-
7
-
o-aminobenzoyl-GFSPFRSVTVQ-ethylenediamine 2,4-dinitrophenol
-
-
14.7
-
o-aminobenzoyl-GFSPFRSVTVQ-ethylenediamine 2,4-dinitrophenol
-
-
0.04
-
o-aminobenzoyl-LMKRP-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
0.076
-
o-aminobenzoyl-LMKRP-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
0.032
-
o-aminobenzoyl-LPRTMFIQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 8.0, 37C
0.014
-
o-aminobenzoyl-LPRTMQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 8.0, 37C
0.73
-
o-aminobenzoyl-MTEMARRPQ-ethylenediamine 2,4-dinitrophenol
-
-
0.8
-
o-aminobenzoyl-MTEMARRPQ-ethylenediamine 2,4-dinitrophenol
-
-
3.27
-
o-aminobenzoyl-MTSVIRRPQ-ethylenediamine 2,4-dinitrophenol
-
-
5.86
-
o-aminobenzoyl-MTSVIRRPQ-ethylenediamine 2,4-dinitrophenol
-
-
1
-
o-aminobenzoyl-Phe-4-(aminomethyl)phenylalanine-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
12.7
-
o-aminobenzoyl-Phe-Arg-Arg-ethylenediamine 2,4-dinitrophenol
-
-
18.7
-
o-aminobenzoyl-Phe-Arg-Arg-ethylenediamine 2,4-dinitrophenol
-
-
18.4
-
o-aminobenzoyl-Phe-Arg-Lys-GFSPFRSVTVQ-ethylenediamine 2,4-dinitrophenol
-
-
21.8
-
o-aminobenzoyl-Phe-Arg-Lys-GFSPFRSVTVQ-ethylenediamine 2,4-dinitrophenol
-
-
1.2
-
o-aminobenzoyl-Phe-Nim-(dimethyl)histidine-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.4
-
o-aminobenzoyl-QPLGMISLMKRP-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
7.1
-
o-aminobenzoyl-QPLGMISLMKRP-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
0.6
-
o-aminobenzoyl-QPLGQTSLMKRP-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
1.1
-
o-aminobenzoyl-QPLGQTSLMKRP-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30C
0.0005
-
o-aminobenzoyl-VMIAALPRTMFIQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 8.0, 37C
0.004
-
o-aminobenzoyl-VMIAALPRTMQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 8.0, 37C
5.7
-
PFRSVQ
-
pH 9.0, 25C
2.8
-
Phe-Arg-Ser-Val-Gln
-
pH 9.0, 25C
0.0065
-
Phe-Ser-Arg-7-amido-4-methylcoumarin
Q9UBX7
37C, pH 7.5
5.3
-
Pro-Phe-Arg-4-methylcoumarin 7-amide
-
recombinant enzyme from liver, pH 8.0, 22C
6.1
-
Pro-Phe-Arg-4-methylcoumarin 7-amide
-
naturally occuring urinary enzyme, pH 8.0, 22C
7.3
-
Pro-Phe-Arg-4-methylcoumarin 7-amide
-
recombinant salivary enzyme, pH 8.0, 22C
7.4
-
Pro-Phe-Arg-4-methylcoumarin 7-amide
-
recombinant pancreatic enzyme, pH 8.0, 22C
12.5
-
Pro-Phe-Arg-4-methylcoumarin 7-amide
-
pH 9.0, 37C
0.031
-
Pro-Phe-Arg-7-amido-4-methylcoumarin
Q9UBX7
37C, pH 7.5
0.917
-
Pro-Phe-Arg-Arg-7-amino-4-methylcoumarin
-
pH 7.5, 37C
5.7
-
RPPGFSPFRSVQ
-
pH 9.0, 25C
-
2
-
succinyl-Val-Pro-Phe-thiobenzyl ester
-
recombinant enzyme from liver and naturally occuring urinary enzyme, pH 8.0, 22C
-
27
-
succinyl-Val-Pro-Phe-thiobenzyl ester
-
recombinant pancreatic enzyme, pH 8.0, 22C
-
29
-
succinyl-Val-Pro-Phe-thiobenzyl ester
-
recombinant salivary enzyme, pH 8.0, 22C
-
0.0075
-
Val-Pro-Arg-7-amido-4-methylcoumarin
Q9UBX7
37C, pH 7.5
0.0267
-
Val-Pro-Arg-Arg-7-amino-4-methylcoumarin
-
pH 7.5, 37C
0.04
-
Leu-Leu-Arg-7-amido-4-methylcoumarin
-
pH 7.5, 37C
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
1.49
-
o-aminobenzoyl-MTEMARRPQ-ethylenediamine 2,4-dinitrophenol
-
-
additional information
-
o-aminobenzoyl-MTSVIRRPQ-ethylenediamine 2,4-dinitrophenol
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.000424
-
acetyl-D-Lys-L-Phe-L-Arg-D-Arg-L-Gln-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.000494
-
acetyl-D-Lys-L-Phe-L-Arg-D-Arg-L-Gln-NH2
-
pH 9.0, 37C
0.0044
-
acetyl-D-Lys-L-Phe-L-Arg-D-Arg-NH2
-
pH 9.0, 37C
2.9e-05
-
acetyl-D-Lys-L-Phe-L-Arg-L-Leu-L-Glu-NH2
-
pH 9.0, 37C
2e-06
-
Bauhinia bauhinioides trypsin inhibitor II
-
pH 8.0, 37C
-
7e-08
-
diisopropyl fluorophosphate
-
pH 7.2, 25C
0.00033
-
o-aminobenzoyl-AIKFFARE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.0004
-
o-aminobenzoyl-AIKFFERE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.00015
-
o-aminobenzoyl-AIKFFKRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.00032
-
o-aminobenzoyl-AIKFFLRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.00035
-
o-aminobenzoyl-AIKFFNRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
9e-05
-
o-aminobenzoyl-AIKFFPRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.00021
-
o-aminobenzoyl-AIKFFRRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.00051
-
o-aminobenzoyl-AIKFFSEE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.001
-
o-aminobenzoyl-AIKFFSIE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.00019
-
o-aminobenzoyl-AIKFFSLE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.00073
-
o-aminobenzoyl-AIKFFSNE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.0006
-
o-aminobenzoyl-AIKFFSQE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.00032
-
o-aminobenzoyl-AIKFFSTE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.0017
-
o-aminobenzoyl-AIKFFSVE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.00022
-
o-aminobenzoyl-AIKFFVRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
2.2e-05
-
o-aminobenzoyl-D-Lys-L-Phe-L-Arg-D-Arg-L-Gln-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
2.9e-05
-
o-aminobenzoyl-D-Lys-L-Phe-L-Phe-D-Arg-L-Gln-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
5e-05
-
o-aminobenzoyl-F-4-(aminomethyl)cyclohexylalanine-SRQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37C
0.0042
-
o-aminobenzoyl-TSVIRRPQ-ethylenediamine
-
pH 9.0, 37C
2.5e-08
-
Protein C inhibitor
-
pH 7.5, 37C
-
0.0033
-
Zn2+-dependent small-molecule competitive inhibitor
-
-
-
1.3e-07
-
DX-2300
-
in 20 mM Tris/HCl buffer, pH 7.5, 150 mM NaCl, 1 mM EDTA, 0.1% poly(ethylene glycol)-8000 and 0.1% Triton X-100
-
additional information
-
additional information
-
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00013
-
convallatoxin
-
KLK6
0.00015
-
convallatoxin
-
KLK5
0.00021
-
digitoxigenin
-
KLK5
0.00038
-
digitoxigenin
-
KLK6
4.2e-05
-
digitoxin
-
KLK5
5e-05
-
digitoxin
-
KLK6
9e-05
-
digoxin
-
KLK5
0.0001
-
digoxin
-
KLK6
6.5e-05
-
Ouabain
-
KLK6
0.00012
-
Ouabain
-
KLK5
6e-06
-
peruvoside
-
KLK6
8e-06
-
peruvoside
-
KLK5
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
47
-
-
purified enzyme
96.5
-
-
purified enzyme
96.5
-
-
-
315
-
-
purified kallikrein A
323
-
-
purified kallikrein B
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.4
-
-
assay at
7.5
-
-
assay at
7.5
-
Q9UBX7
hydrolysis of Pro-Phe-Arg-7-amido-4-methylcoumarin
7.8
-
-
assay at
8
10
-
cleavage of D-Val-Leu-Arg-p-nitroanilide
8
-
-
assay at
8
-
-
assay at
8
-
-
assay at
8
-
-
assay at
8
-
-
assay at
8
-
-
assay at
8
-
-
assay at
8.2
-
-
assay at
8.2
-
-
assay at
8.5
-
-
assay at
8.5
-
-
kinin releasing activity, prostate
9
-
-
esterase activity
9
-
-
tosyl-Arg methyl esterase activity
9
-
-
assay at
9
-
-
tosyl-Arg methyl ester hydrolase activity and kininogenase activity of wild-type and recombinant enzyme
9
-
-
assay at
9
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
9.5
-
pH 6.5: about 30% of maximal activity, pH 9.5: about 40% of maximal activity
8
10
-
pH 8.0: about 35% of maximal activity, pH 10.0: about 70% of maximal activity
8
10
-
pH 8.0: about 60% of maximal activity, pH 10.0: about 55% of maximal activity, kinin releasing activity, prostate
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
assay at
25
-
-
assay at
25
-
-
assay at
30
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
activity in plasma of patients with pemphigus foliaceus is significantly increased compared with controls
Manually annotated by BRENDA team
-
lower content
Manually annotated by BRENDA team
-
primary, tracheal submucosal gland
Manually annotated by BRENDA team
-
activity is higher during the middle of the menstrual cycle, possible up-regulation by estrogens
Manually annotated by BRENDA team
-
secretory epithelial cell
Manually annotated by BRENDA team
-
secretory epithelial cells tf trachea, thyroid gland, mammary gland, salivary gland, jejunum, ileum, epididymis, seminal vesicle and urethra
Manually annotated by BRENDA team
-
anterior; prolactin-secreting adenomas
Manually annotated by BRENDA team
-
secretory epithelial cell
Manually annotated by BRENDA team
-
; low content
Manually annotated by BRENDA team
-
small and large
Manually annotated by BRENDA team
-
secretory epithelial cell
Manually annotated by BRENDA team
-
granular keratinocyte
Manually annotated by BRENDA team
-
in the collecting segment of the distal tubule
Manually annotated by BRENDA team
-
proximal tubular epithelial cell
Manually annotated by BRENDA team
-
secretory epithelial cell
Manually annotated by BRENDA team
-
tracheal, primary cell culture
Manually annotated by BRENDA team
-
lower content
Manually annotated by BRENDA team
-
KLK4 and KLK11
Manually annotated by BRENDA team
-
increased expression
Manually annotated by BRENDA team
-
prostate-specific
Manually annotated by BRENDA team
-
secretory epithelial cell
Manually annotated by BRENDA team
-
almost every kallikrein is expressed in the salivary gland
Manually annotated by BRENDA team
-
secretory epithelial cell
Manually annotated by BRENDA team
-
KLK9, KLK11
Manually annotated by BRENDA team
-
lower content
Manually annotated by BRENDA team
-
expressed exclusively in the Leydig cells of adult mice
Manually annotated by BRENDA team
-
secretory epithelial cell
Manually annotated by BRENDA team
-
submucosal gland, primary cell culture
Manually annotated by BRENDA team
-
secretory epithelial cell
Manually annotated by BRENDA team
-
secretory epithelial cell
Manually annotated by BRENDA team
-
low content
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25200
-
-
equilibrium sedimentation
31000
35000
-
gel filtration
33000
-
-
kallikrein B, gel filtration
33500
-
-
light scattering
35900
-
-
prokallikrein A, gel filtration
36000
-
-
kallikrein A, gel filtration
37400
-
-
prokallikrein B, gel filtration
38000
-
-
gel filtration
39000
-
-
glycosylated monomer, SDS-PAGE
40000
-
-
gel filtration
40500
-
-
short column equilibrium sedimentation
53000
-
-
prokallikrein and kallikrein, gel filtration
72000
-
-
unglycosylated dimer, SDS-PAGE
additional information
-
Q9UBX7
about 40% of human tissue kallikrein 11 (40000 Da) is enzymatically active, whereas the rest is inactivated by internal cleavage after Arg156 which generates two peptides of 20000 Da, connected by internal disulfide bonds
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 38000, kallikrein k1, SDS-PAGE
?
-
x * 38000, SDS-PAGE under reducing conditions
?
-
x * 43000, urinary enzyme, SDS-PAGE
?
-
x * 34000 or x * 37000, the two molecular species represent differentially glycosylated forms
?
-
x * 11000 + x * 16000, kallikrein A, SDS-PAGE after reduction with 2-mercaptoethanol; x * 27000, kallikrein B, SDS-PAGE; x * 33000, kallikrein A, SDS-PAGE; x * 4000 + x * 16000, kallikrein B, SDS-PAGE after reduction with 2-mercaptoethanol
?
-
x * 29000, SDS-PAGE under reducing conditions
?
-
x * 14000 + x * 18000, SDS-PAGE under reducing conditions
?
-
x * 14000 + x * 18000, SDS-PAGE under reducing conditions; x * 28000, SDS-PAGE in absence of a reducing agent; x * 32000, K2, SDS-PAGE
?
-
x * 32000, K2, SDS-PAGE
?
Q9UBX7
x * 40000, SDS-PAGE
?
-
x * 35000, SDS-PAGE
?
-
x * 39000, SDS-PAGE
homodimer
-
2 * 36000, unglycosylated dimer, SDS-PAGE
monomer
-
1 * 46000, active kallikrein, SDS-PAGE; 1 * 48000, prokallikrein, SDS-PAGE
monomer
-
1 * 36500, prokallikrein A, SDS-PAGE; 1* 38400, prokallikrein B, SDS-PAGE
monomer
-
1 * 38000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
-
glycoprotein
-
-
proteolytic modification
-
thermolysin activates prokallikrein cleaving off the N-terminal Ile1-Val2; zymogen: prokallikrein can by activated by two types of enzymes, serine proteases which cleave at the C-terminus of basic amino acids and by a metalloproteinase that cleaves at the N-terminus of hydrophobic amino acids
proteolytic modification
-
preprokallikrein consists of 262 amino acid residues
proteolytic modification
-
zymogen: prokallikrein
side-chain modification
-
-
side-chain modification
-
glycoprotein
side-chain modification
-
both kallikrein and prokallikrein display multiple molecular forms with differences in both molecular sizes and charges. The structural differences are found to be due to glycosylation, with the high-molecular-weight species glycosylated at three Asn-linked sites and the low-molecular-weight species at two of the three Asn-linked sites. The multiply charged kallikrein isoforms are derived from different numbers of sialic acids attached at the detected Asn-linked carbohydrates
proteolytic modification
-
activation by trypsin; zymogen: prokallikrein
proteolytic modification
-
activation by trypsin; urinary and renal kallikrein exist in both active and proenzyme form
side-chain modification
-
multiple forms are due at least in part to varying carbohydrates
side-chain modification
-
kallikrein A contains 5.6% carbohydrate by weight, kallikrein B contains 11.5% carbohydrate per weight. Carbohydrate is located on both chains of kallikrein B
side-chain modification
-
the glycoprotein consists of 283 amino acid residues and 19-21 sugar residues
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
enzyme expressed in a deglycosylated form at high levels in Pichia pastoris, structure analysis
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
-
-
immediate irreversible inactivation
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
pH 7.0-9.5, 5 h, stable. Little loss of activity after 5 h at pH 4.4
55
-
-
18 h, 70% of the activity is retained
100
-
-
5 min, 60% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
freezing and thawing results in at least three-fold increase of specific activity
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, stable for more than 3 months
-
-30C, purified urinary enzyme, stable for 1 year
-
20C, purified urinary enzyme, 0.02% w/v NaN3, neutral pH, stable for more than 14 days
-
4C, purified urinary enzyme, 0.02% w/v NaN3, stable for more than 6 months
-
4C, stable for 1 month
-
-20C, 0.1 N NaCl, 0.01 M sodium phosphate buffer, pH 7.0, stable for months
-
4C, stable for weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
1460fold; large scale
-
397fold; large scale
-
by affinity column chromatography
-
enzyme expressed in a deglycosylated form at high levels in Pichia pastoris
-
from urine; to homogeneity
-
glandular kallikrein, 5000fold, to homogeneity
-
prokallikrein, 183fold
-
recombinant
-
recombinant from Pichia pastoris
-
to homogeneity
-
Zn2+-nitrilotriacetic acid agarose column chromatography
-
DEAE-cellulose column chromatography
-
partial
-
427fold from submandibular gland; from urine
-
by affinity column chromatography
-
prokallikrein A and B; to homogeneity
-
recombinant enzyme
-
partially purified by DEAE-cellulose column chromatography
-
kallikrein A and B
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
860-bp fragment of tissue kallikrein containing an open reading frame subcloned into pXXUF1 downstream of CMV. recombinant adeno-associated virus encoding tissue kallikrein delivered to spontaneously hypertensive rats and cultured HEK-293 cells
-
cDNA of the tissue kallikrein gene is subcloned into the chicken oviduct-specific expression vector pOV3. The resultant recombinant vector pOV3K is injected into laying hens via wing vein after mixing with polyethyleneimine. The chicken oviduct-specific transient expression system can produce relatively high level and authentic recombinant enzyme with a potential for further development for therapeutic use
-
DNA sequence determination, expression of prokallikrein in Pichia pastoris
-
expressed in diabetic Rattus norvegicus
-
expressed in Mus musculus and Danio rerio
-
expressed in Mus musculus and Rattus norvegicus
-
expressed in Rattus norvegicus and Mus musculus myocardium
-
expressed in Rattus norvegicus heart
-
expressed in the egg white of laying hens
-
expression in Escherichia coli
-
expression of recombinant human prokallikrein and kallikrein in engineered Chinese hamster ovary cells
-
genetic organization and structure of the kallikrein gene family, clustered on chromosome 19q13.3-q13.4
P06870
overexpressed in transgenic mice or rats
-
production of pro-form of tissue kallikrein 9 in Escherichia coli cells. Production of tissue kallikrein 9 in CHO cells
-
recombinant adeno-associated virus-mediated human tissue kallikrein expression is induced in a rodent model of chronic renal failure
-
expression in Escherichia coli and in yeast
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
urinary kallikrein excretion is significantly reduced in patients with mild renal disease, and to a further extent in patients with severe renal failure
-
aprotinin attenuates high-glucose stimulated expression of KLK1
-
in an endothelial-cervical carcinoma conditioned-medium model, HeLa metabolites cause a dramatic decrease in endothelial cellular tissue kallikrein and a concomitant proliferation of endothelial cells
-
blood plasma tissue kallikrein levels are significantly lower in stroke patients, especially those with ischemic stroke
-
lower human kallikrein protein levels are observed in proangiogenic cells from type 2 diabetic patients
-
tubular expression of KLK1 in diabetic kidney biopsies. High-glucose stimulates expression of KLK1
-
presence of tissue kallikrein in HeLa cells and in angiogenic HUVECs. In the submandibular gland control tissue, positive tissue kallikrein staining within the ductal epithelial gland. On conditioned media a dose-dependent increase of tissue kallikrein. In challenged endothelial cells with metabolites from cervical cancer cells, the reduction in cellular tissue kallikrein is associated with a concomitant increase in tissue kallikrein within the media
-
dietary potassium loading stimulates directly the secretion of tissue kallikrein independently of aldosterone
-
prednisolone treatment for 9 days to adjuvant arthritic rats results in reduction in the mean synovial tissue kallikrein level as compared to the non-treated arthritic rats
-
indomethacin-treated rats show elevated mean paw tissue kallikrein level as compared with the non-treated arthritic rats. Prednisolone treatment for 9 days to adjuvant arthritic rats results in appreciable raise in the mean paw tissue level as compared to the non-treated arthritic rats. Indomethacin-treated rats also show elevated mean paw tissue kallikrein level as compared to the non-treated arthritic rats
-
there is an increase of glandular kallikrein in skin, mucus, kidney, gills, and leukocytes of Vibrio ordalii- and Piscirickettsia salmonis-infected fish
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
R53H
-
inactive
Y228A
-
enlarges the S1 pocket
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
biotechnology
-
the chicken oviduct-specific transient expression system can produce relatively high level of authentic recombinant enzyme with a potential for further development for therapeutic use
drug development
-
recombinant adeno-associated virus-mediated tissue kallikrein gene delivery has multiple therapeutic possibilities for treating hypertension, not only by decreasing blood pressure, but also by directly inhibiting end-organ damage
drug development
-
tissue kallikrein represents a promising therapeutic strategy for ischemic stroke
drug development
-
pre-treatment with tissue kallikrein inhibitors and/or anti-angiogenic therapies may prove to benefit future cervical cancer patients
medicine
-
enzyme complexed with prostate protease inhibitor-6 may be a naturally occuring marker of tissue damage and necrosis associated with neoplasia; enzyme is a diagnostic marker for prostate cancer
medicine
-
diagnostic marker for ovarian cancer; enzyme is a diagnostic marker for prostate cancer
medicine
-
For men with localized prostate cancer and moderate elevation of prostate-specific antigen in serum, addition of free prostate-specific antigen and enzyme data increase predictive accuracy
medicine
-
tissue kallikreins may be causally involved in carcinogenesis, particularly in tumor metastasis and invasion, and thus, may represent attractive drug targets to consider for therapeutic intervention. Certain kallikreins are markers of favorable prognosis for cancer patients
medicine
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kallikrein may serve as new drug target for the prevention and treatment of heart failure, renal disease and stroke in humans
medicine
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protective effects against cardiac hypertrophy
medicine
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tissue kallikreins, particularly KLK6, are considered potential candidates for epithelial antimetastatic therapy
medicine
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KLK1 plays a critical role in arterial function, KLK1 is also involved in the control of ionic transport in the renal tubule, there are cardio- and nephroprotective effects of KLK1 and kinins in acute cardiac ischemia, post-ischemic heart failure, and diabetes
medicine
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rhinovirus-induced human tissue kallikrein activation may contribute to airway inflammation and asthmatic exacerbations
medicine
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expression of tissue kallikrein exerts antihypertrophic and antifibrotic actions in the heart
medicine
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urinary kallikrein excretion is positively correlated to renal function, serum and urinary inflammatory mediator monocyte chemoattractant protein-1 in chronic kidney disease patients
medicine
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tissue kallikrein therapy is a promising regimen in the treatment of acute ischemic stroke in humans
medicine
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plasma tissue kallikrein levels are negatively associated with the risk of first-ever stroke and stroke recurrence and positively associated with event-free survival during 5 years of follow-up
medicine
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the enzyme-activated prodrug Ac-GKAFRR-L12ADT, i.e. Ac-GKAFRR-thapsigarin, is stable in vivo. The maximally tolerated dose is 6 mg/kg, which produces a serum concentration of about 0.036 mM and has a half-life of 40 min
medicine
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in the context of chronic unilateral reduction in renal blood flow, tissue kallikrein does not influence the trophicity of kidneys, the synthesis and secretion of rennin, blood pressure increase and cardiac remodelling due to rennin angiotensin system activation
medicine
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tissue kallikrein exerts a protective role in heart failure in mice, tissue kallikrein-deficient subjects may be at increased risk of mortality in heart failure
medicine
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kallikrein improves cardiac function and reduces infarct size in kininogen-deficient rats, icatibant and N-alpha-nitro-L-arginine-methyl-ester block kallikrein's cardioprotective effects
medicine
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kallidinogenase may be efficacious for simple retinopathy including hyperpermeability in subjects with diabetes
medicine
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tissue kallikrein administration can remarkably alleviate hypoxia/reoxygenation-induced neuronal injury by reduction of lactate dehydrogenase release and promotion of neuron viability