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Information on EC 3.4.21.35 - tissue kallikrein
for references in articles please use BRENDA:EC3.4.21.35
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.21 Serine endopeptidases
3.4.21.35 tissue kallikrein
IUBMB Comments
Formed from tissue prokallikrein by activation with trypsin. In peptidase family S1 (trypsin family). A large number of tissue kallikrein-related sequences have been reported for rats and mice , though fewer seem to exist in other mammals. The few that have been isolated and tested on substrates include mouse γ-renin (EC 3.4.21.54), submandibular proteinase A [2,15], epidermal growth-factor-binding protein, nerve growth factor γ-subunit, rat tonin [3,4,9], submaxillary proteinases A and B , T-kininogenase , kallikreins k7 and k8 and human prostate-specific antigen (γ-seminoprotein, )
The enzyme appears in viruses and cellular organisms
- 3.4.21.35
- kallikreins
-
prostatectomy
-
gleason
- androgen
- rectal
- hyperplasia
-
transrectal
-
ultrasound
-
preoperative
- adenocarcinoma
-
prostate-specific
-
seminal
- lymph
-
followup
- metastases
-
radiotherapy
-
postoperative
-
needle
- urological
-
staging
-
pelvic
- bradykinin
-
lncap
-
transurethral
-
beam
-
retropubic
-
kallikrein-kinin
- kininogens
-
ultrasonography
-
sextant
-
suspicious
-
brachytherapy
-
nadir
-
extraprostatic
-
urologist
- aprotinin
-
immunosensors
-
actuarial
-
ultrasound-guided
-
multiparametric
- incontinence
-
lymphadenectomy
-
transperineal
-
antiandrogens
- hk2
-
organ-confined
-
extracapsular
- biotechnology
- medicine
- drug development
- finasteride
-
kininase
-
mcrpc
Reaction Schemes
showPreferential 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
Synonyms
prostate specific antigen, tissue kallikrein, glandular kallikrein, renal kallikrein, trypsin-like serine protease, prokallikrein, klk15, salivary kallikrein, glandular kallikrein 2, urinary kallidinogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bradykininogenase
-
-
-
-
callicrein
-
-
-
-
depot-Padutin
-
-
-
-
dilminal D
-
-
-
-
EC 3.4.21.8
-
-
formerly
-
EC 3.4.4.21
-
-
formerly, part transferred
-
GK1
glandular kallikrein
glumorin
-
-
-
-
hK11
K1
kallidinogenase
kallikrein
kallikrein 1
kidney/pancreas/salivary gland kallikrein
-
-
-
-
kininogenase
-
-
-
-
kininogenin
-
-
-
-
KLK
KLK-S3
-
-
-
-
KLK1
KLK11
KLK4
KLK5
KLK6
KLK7
onokrein P.
-
-
-
-
P1 kallikrein
-
-
-
-
padreatin
-
-
-
-
padutin
-
-
-
-
pancreatic kallikrein
-
-
-
-
PPK
-
-
-
-
Prk
PS kallikrein
-
-
-
-
renal tissue kallikrein
-
-
-
-
RSGK-50
-
-
-
-
RUK
-
-
-
-
S01.160
-
-
-
-
S1 kallikrein
-
-
-
-
S2 kallikrein
-
-
-
-
S3 kallikrein
-
-
-
-
salivary kallikrein
-
-
-
-
SEV
-
-
-
-
submandibular enzymatic vasoconstrictor
-
-
-
-
T-kininogenase
-
-
-
-
tissue kallikrein
tissue kallikrein 1
tissue kallikrein 4
urinary kallidinogenase
urinary kallikrein
urokallikrein
-
-
-
-
additional information
-
KLK1, KLK4, and KLK11 are serine proteases with trypsin-like activity, while KLK9 has chymotrypsin-like activity
glandular kallikrein
-
-
-
-
kallidinogenase
-
-
-
-
kallikrein
-
-
-
-
kallikrein 1
-
-
-
-
KLK1
-
-
Prk
-
-
-
-
urinary kallikrein
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
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
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
substrate binding pocket contains an Asp residue
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
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
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
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
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
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
389069-73-2
-
9001-01-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-aminobenzoyl-MISLMKRPPGFSPFRSS(PO3H2)RI-NH2 + H2O
2-aminobenzoyl-MISLM + KRPPGFSPFRSS(PO3H2)RI-NH2
-
Substrates: -
Products: -
Products: -
?
2-aminobenzoyl-MISLMKRPPGFSPFRSSRI-NH2 + H2O
2-aminobenzoyl-MISLM + KRPPGFSPFRSSRI-NH2
-
Substrates: -
Products: -
Products: -
?
Abz-GFSPFRSLRI-Q-EDDnp + H2O
Abz-GFSPFR + SLRI-Q-EDDnp
Substrates: -
Products: -
Products: -
?
Abz-GFSPFRSSRI-Q-EDDnp + H2O
Abz-GFSPFR + SSRI-Q-EDDnp
Substrates: -
Products: -
Products: -
?
Abz-KLYSQED-Dnp + H2O
?
Substrates: artificial fluorogenic substrate
Products: -
Products: -
?
Abz-MISLMKLP-Q-EDDnp + H2O
Abz-MISLM + KLP-Q-EDDnp
Substrates: -
Products: -
Products: -
?
Abz-MISLMKRP-Q-EDDnp + H2O
Abz-MISLM + KRP-Q-EDDnp
Substrates: -
Products: -
Products: -
?
Abz-MISLMKRPPGFSPFRSSRI-NH2 + H2O
Abz-MISLM + KRPPGFSPF + RSSRI-NH2
-
Substrates: -
Products: -
Products: -
?
Ac-GKAFRR-L12ADT + H2O
?
-
Substrates: peptide coupled to cytotoxin thapsigarin, L12ADT, as an enzyme-activated prodrug. Enzyme cleaves at R-residue adjacent to L12ADT
Products: -
Products: -
?
Ac-KHLY-7-amino-4-carbamoylmethylcoumarin + H2O
Ac-KHLY + 7-amino-4-carbamoylmethylcoumarin
Substrates: -
Products: -
Products: -
?
acetyl-2-aminohexanoic acid-Arg methyl ester + H2O
acetyl-2-aminohexanoic acid-Arg + methanol
-
Substrates: -
Products: -
Products: -
?
acetyl-Ala-Arg methyl ester + H2O
acetyl-Ala-Arg + methanol
-
Substrates: -
Products: -
Products: -
?
acetyl-Ala-Leu-Arg-p-nitroanilide + H2O
acetyl-Ala-Leu-Arg + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-Ala-Phe-Arg methyl ester + H2O
acetyl-Ala-Phe-Arg + methanol
-
Substrates: -
Products: -
Products: -
?
acetyl-Ala-Phe-Arg-Ala + H2O
acetyl-Ala-Phe-Arg + L-alanine
-
Substrates: -
Products: -
Products: -
?
acetyl-Ala-Phe-Arg-Ala-NH2 + H2O
acetyl-Ala-Phe-Arg + Ala-NH2
-
Substrates: -
Products: -
Products: -
?
acetyl-Ala-Phe-Arg-p-nitroanilide + H2O
acetyl-Ala-Phe-Arg + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-Ala-Thr-Arg-p-nitroanilide + H2O
acetyl-Ala-Thr-Arg + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-Arg-p-nitroanilide + H2O
acetyl-Arg + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-D-Ala-Arg methyl ester + H2O
acetyl-D-Ala-Arg + methanol
-
Substrates: -
Products: -
Products: -
?
acetyl-D-Phe-Arg methyl ester + H2O
acetyl-D-Phe-Arg + methanol
-
Substrates: -
Products: -
Products: -
?
acetyl-Glu-Leu-Arg-p-nitroanilide + H2O
acetyl-Glu-Leu-Arg + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-Glu-Lys-Arg-p-nitroanilide + H2O
acetyl-Glu-Lys-Arg + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-Glu-Phe-Arg-p-nitroanilide + H2O
acetyl-Glu-Phe-Arg + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-Glu-Thr-Arg-p-nitroanilide + H2O
acetyl-Glu-Thr-Arg + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-Gly-Arg methyl ester + H2O
acetyl-Gly-Arg + methanol
-
Substrates: -
Products: -
Products: -
?
acetyl-Gly-Arg-Ser-Val-Gln + H2O
acetyl-Gly-Arg + Ser-Val-Gln
-
Substrates: -
Products: -
Products: -
?
acetyl-Ile-Arg methyl ester + H2O
acetyl-Ile-Arg + methanol
-
Substrates: -
Products: -
Products: -
?
acetyl-Leu-Arg methyl ester + H2O
acetyl-Leu-Arg + methanol
-
Substrates: -
Products: -
Products: -
?
acetyl-Met-Arg methyl ester + H2O
acetyl-Met-Arg + methanol
-
Substrates: -
Products: -
Products: -
?
acetyl-Phe-Arg ethyl ester + H2O
acetyl-Phe-Arg + ethanol
-
Substrates: -
Products: -
Products: -
?
acetyl-Phe-Arg-p-nitroanilide + H2O
acetyl-Phe-Arg + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-Phe-Arg-Ser-NH2 + H2O
acetyl-Phe-Arg + Ser-NH2
-
Substrates: -
Products: -
Products: -
?
acetyl-Phe-Arg-Ser-Val-Gln + H2O
acetyl-Phe-Arg + Ser-Val-Gln
-
Substrates: -
Products: -
Products: -
?
acetyl-Phe-Arg-Ser-Val-NH2 + H2O
acetyl-Phe-Arg + Ser-Val-NH2
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Arg methyl ester + H2O
acetyl-Pro-Arg + methanol
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Phe-Arg methyl ester + H2O
acetyl-Pro-Phe-Arg + methanol
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Phe-Arg-Ala + H2O
acetyl-Pro-Phe-Arg + L-alanine
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Phe-Arg-Ala-NH2 + H2O
acetyl-Pro-Phe-Arg + Ala-NH2
-
Substrates: -
Products: -
Products: -
?
acetyl-Pro-Phe-Arg-p-nitroanilide + H2O
acetyl-Pro-Phe-Arg + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-Trp-2-aminohexanoic acid methyl ester + H2O
?
-
Substrates: -
Products: -
Products: -
?
acetyl-Trp-Arg methyl ester + H2O
acetyl-Trp-Arg + methanol
-
Substrates: -
Products: -
Products: -
?
acetyl-Tyr-Arg methyl ester + H2O
acetyl-Tyr-Arg + methanol
-
Substrates: -
Products: -
Products: -
?
acetyl-Val-Arg methyl ester + H2O
acetyl-Val-Arg + methanol
-
Substrates: -
Products: -
Products: -
?
Ala-Ala-Arg-7-amido-4-methylcoumarin + H2O
Ala-Ala-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
angiotensin I + H2O
?
-
Substrates: reaction with prostate enzyme, very low reaction with submandibular enzyme
Products: -
Products: -
?
angiotensinogen + H2O
?
-
Substrates: reaction with prostate enzyme, no reaction with submandibular enzyme
Products: -
Products: -
?
benzoyl-Phe-Val-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-Phe-Val-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
benzoyl-Pro-Phe-Arg-p-nitroanilide + H2O
benzoyl-Pro-Phe-Arg + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Arg-Ala-NH2 + H2O
benzyloxycarbonyl-Arg + Ala-NH2
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Arg-p-nitroanilide + H2O
benzyloxycarbonyl-Arg + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
Benzyloxycarbonyl-Lys methyl ester + H2O
Benzyloxycarbonyl-Lys + methanol
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
-
Substrates: about 30% of the activity with Pro-Phe-Arg-4-methylcoumarin 7-amide
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Pro-Gly-Arg methyl ester + H2O
benzyloxycarbonyl-Pro-Gly-Arg + methanol
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Pro-Phe-Arg methyl ester + H2O
benzyloxycarbonyl-Pro-Phe-Arg + methanol
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Tyr-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Tyr + 4-nitrophenol
-
Substrates: -
Products: -
Products: -
?
Boc-VPR-7-amino-4-methylcoumarin + H2O
Boc-VPR + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
-
Substrates: weak activity
Products: -
Products: -
?
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
-
Substrates: weak activity
Products: -
Products: -
?
D-Pro-Phe-Phe-7-amido4-methylcoumarin + H2O
D-Pro-Phe-Phe + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
D-Val-Leu-Arg-7-amido-4-methylcoumarin + H2O
D-Val-Leu-Arg + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
D-Val-Leu-Arg-7-amido-4-trifluoromethylcoumarin + H2O
D-Val-Leu-Arg + 7-amino-4-trifluoromethylcoumarin
-
Substrates: -
Products: -
Products: -
?
epithelial sodium channel + H2O
activated epithelial sodium channel + ?
-
Substrates: -
Products: -
Products: -
?
Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
Gln-Ala-Arg + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
Gly-Pro-Arg + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
H-D-Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
H-D-Pro-Phe-Arg + 7-amino-4-methylcoumarin
-
Substrates: i.e. S-2302
Products: -
Products: -
?
insulin-like growth factor binding protein + H2O
?
-
Substrates: -
Products: -
Products: -
?
insulin-like growth factor binding proteins
insulin-like growth factor binding protein fragments
kinin B2 receptor + H2O
?
-
Substrates: tissue kallikrein directly activates kinin B2 receptor in the absence of kininogen
Products: -
Products: -
?
L-Pro-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Pro-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Leu-Leu-Arg-7-amido-4-methylcoumarin + H2O
Leu-Leu-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
low molecular weight kininogen + H2O
kallidin + kinin
-
Substrates: -
Products: -
Products: -
?
low-molecular-weight kininogen + H2O
GMISLM + KRPPGFSPFR + SSRIG
Substrates: -
Products: KRPPGFSPFR is kallidin
Products: KRPPGFSPFR is kallidin
?
N-alpha-acetyl-Phe-Arg ethyl ester + H2O
N-alpha-acetyl-Phe-Arg + ethanol
-
Substrates: -
Products: -
Products: -
?
N-alpha-benzoyl-L-citrulline methyl ester + H2O
N-alpha-benzoyl-L-citrulline + methanol
-
Substrates: -
Products: -
Products: -
?
N-alpha-benzoyl-L-Orn methyl ester + H2O
N-alpha-benzoyl-L-Orn + methanol
-
Substrates: -
Products: -
Products: -
?
N-alpha-tosyl-L-arginine methyl ester + H2O
N-alpha-tosyl-L-arginine + methanol
-
Substrates: -
Products: -
Products: -
?
N-methoxysuccinyl-Arg-Pro-Tyr-4-nitroanilide + H2O
N-methoxysuccinyl-Arg-Pro-Tyr + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-AIKFFIRE-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-AIKFF + IRE-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-AIKFFQRE-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-AIKFF + QRE-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-AIKFFSAE-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-AIKFF + SAE-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-AIKFFSKE-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-AIKFF + SKE-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-AIKFFSPE-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-AIKFF + SPE-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-AIKFFSRE-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-AIKFF + SRE-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-AIKFFSRQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-AIKFF + SRQ-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: substrate sequence is derived from the kallistatin reactive centre loop sequence
Products: -
Products: -
?
o-aminobenzoyl-AIKFFSSE-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-AIKFF + SSE-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-AIKFFTRE-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-AIKFF + TRE-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-FRSSR-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-FR + SSR-N-(2,4-dinitrophenyl)ethylene diamine
o-aminobenzoyl-FRSVQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-FR + SVQ-N-(2,4-dinitrophenyl)ethylene diamine
o-aminobenzoyl-GFSPF-4-(aminocyclohexyl)alanine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
-
Substrates: 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
Products: -
Products: -
?
o-aminobenzoyl-GFSPF-4-(aminomethyl)-N-isopropylphenylalanine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
-
Substrates: 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
Products: -
Products: -
?
o-aminobenzoyl-GFSPF-4-(aminomethyl)phenylalanine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
-
Substrates: 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
Products: -
Products: -
?
o-aminobenzoyl-GFSPF-4-piperidinylalanine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
-
Substrates: 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
Products: -
Products: -
?
o-aminobenzoyl-GFSPF-Nim-(dimethyl)histidine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
-
Substrates: 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
Products: -
Products: -
?
o-aminobenzoyl-GFSPFRAPRVQ-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-GFSPFR + APRVQ-ethylenediamine 2,4-dinitrophenol + o-aminobenzoyl-GFSPF + RAPRVQ-ethylenediamine 2,4-dinitrophenol
o-aminobenzoyl-GFSPFRSSRIGEIKEEQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-GFSPFR + SSRIGEIKEEQ-N-(2,4-dinitrophenyl)ethylene diamine
o-aminobenzoyl-GFSPFRSSRQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-GFSPFR + SSRQ-N-(2,4-dinitrophenyl)ethylene diamine
o-aminobenzoyl-GFSPFRSVQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-GFSPFR + SVQ-N-(2,4-dinitrophenyl)ethylene diamine
o-aminobenzoyl-GFSPFRSVQVMKYEGSQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-GFSPFR + SVQVMKYEGSQ-N-(2,4-dinitrophenyl)ethylene diamine
o-aminobenzoyl-GFSPFRSVTVQ-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-GFSPFR + SVTVQ-ethylenediamine 2,4-dinitrophenol
o-aminobenzoyl-LMKRP-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-LM + KRP-N-(2,4-dinitrophenyl)ethylene diamine
o-aminobenzoyl-LPRTMFIQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
-
Substrates: shortened, quenched fluorescent substrate, synthesized based on Bauhinia ungulata factor Xa inhibitor reactive sequence site
Products: -
Products: -
?
o-aminobenzoyl-LPRTMQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
-
Substrates: shortened, quenched fluorescent substrate, synthesized based on Bauhinia ungulata factor Xa inhibitor reactive sequence site
Products: -
Products: -
?
o-aminobenzoyl-MTEMARRPPGFSPFRSVTVQ-NH2 + H2O
o-aminobenzoyl-MTEMAR + RPPGFSPFR + SVTVQ-NH2
o-aminobenzoyl-MTEMARRPQ-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-MTEMAR + RPQ-ethylenediamine 2,4-dinitrophenol
o-aminobenzoyl-MTSVIRRPPGFSPFRAPRV-NH2 + H2O
des[Arg9] bradykinin + ?
-
Substrates: preferential hydrolysis of Phe-Arg compared with Arg-Ala bond, preferential release of des[Arg9] bradykinin
Products: -
Products: -
?
o-aminobenzoyl-MTSVIRRPQ-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-MTSVIR + RPQ-ethylenediamine 2,4-dinitrophenol
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
-
Substrates: 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
Products: -
Products: -
?
o-aminobenzoyl-Phe-Arg-Arg--ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-Phe-Arg + Arg-ethylenediamine 2,4-dinitrophenol
-
Substrates: slow hydrolysis
Products: -
Products: -
?
o-aminobenzoyl-Phe-Arg-Arg-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-Phe-Arg + Arg-ethylenediamine 2,4-dinitrophenol
o-aminobenzoyl-Phe-Arg-Lys-GFSPFRSVTVQ-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-Phe-Arg + Lys-ethylenediamine 2,4-dinitrophenol
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
-
Substrates: 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
Products: -
Products: -
?
o-aminobenzoyl-QPLGMISLMKRP-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-QPLGMISLM + KRP-N-(2,4-dinitrophenyl)ethylene diamine
o-aminobenzoyl-QPLGQTSLMKRP-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-QPLGQTSLM + KRP-N-(2,4-dinitrophenyl)ethylene diamine
o-aminobenzoyl-TSVIRRPQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
-
Substrates: -
Products: -
Products: -
?
Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
Phe-Ser-Arg + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
precursor of atrial natriuretic factor + H2O
natriuretic factor
Substrates: -
Products: -
Products: -
?
pro-insulin + H2O
insulin + insulin signal peptide
Substrates: -
Products: -
Products: -
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: reaction catalyzed by mK13
Products: -
Products: -
?
Pro-Phe-Arg-Arg-7-amido-4-methylcoumarin + H2O
Pro-Phe-Arg-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
prolactin + H2O
lactin + ?
-
Substrates: three cleavage sites between Arg174-Arg175, Lys185-Phe186 and Arg188-Cys189
Products: -
Products: -
?
QAR-7-amido-4-methylcoumarin + H2O
QAR + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
semenogelin I + H2O
semenogelin I fragments
-
Substrates: -
Products: -
Products: -
?
semenogelin II + H2O
semenogelin II fragments
-
Substrates: -
Products: -
Products: -
?
succinyl-Val-Pro-Phe-thiobenzyl ester + H2O
succinyl-Val-Pro-Phe + phenylmethanethiol
-
Substrates: -
Products: -
Products: -
?
tert-butyloxycarbonyl-Gln-Ala-Arg-4-methylcoumarin 7-amide + H2O
?
-
Substrates: about 15% of the activity with Pro-Phe-Arg-4-methylcoumarin 7-amide
Products: -
Products: -
?
tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
?
-
Substrates: about 50% of the activity with Pro-Phe-Arg-4-methylcoumarin 7-amide
Products: -
Products: -
?
tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
?
-
Substrates: about 20% of the activity with Pro-Phe-Arg-4-methylcoumarin 7-amide
Products: -
Products: -
?
tosyl-Gly-Pro-Arg-p-nitroanilide + H2O
tosyl-Gly-Pro-Arg + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
Val-Leu-Arg-4-nitroanilide + H2O
Val-Leu-Arg + 4-nitroaniline
-
Substrates: tracheobronchial epithelial cells grown at the air/liquid interface
Products: -
Products: -
?
Val-Pro-Arg-Arg-7-amido-4-methylcoumarin + H2O
Val-Pro-Arg-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
vascular endothelial growth factor 164 + H2O
?
-
Substrates: -
Products: -
Products: -
?
VPR-7-amido-4-methylcoumarin + H2O
VPR + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
zymogen of prostate-specific antigen + H2O
prostate-specific antigen + APLILSR
-
Substrates: -
Products: -
Products: -
?
zymogen of urokinase-type plasminogen activator + H2O
urokinase-type plasminogen activator
-
Substrates: activation of inactive zymogen to mature active enzyme
Products: -
Products: -
?
acetyl-Phe-Arg methyl ester + H2O
acetyl-Phe-Arg + methanol
-
Substrates: -
Products: -
Products: -
?
acetyl-Phe-Arg methyl ester + H2O
acetyl-Phe-Arg + methanol
-
Substrates: -
Products: -
Products: -
?
Ala-Arg-Arg-7-amido-4-methylcoumarin + H2O
Ala-Arg-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Ala-Arg-Arg-7-amido-4-methylcoumarin + H2O
Ala-Arg-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Arg methyl ester + H2O
benzyloxycarbonyl-Arg + methanol
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Arg methyl ester + H2O
benzyloxycarbonyl-Arg + methanol
-
Substrates: -
Products: -
Products: -
?
D-Pro-Phe-Arg-4-methylcoumarin-7-amide + H2O
?
-
Substrates: -
Products: -
Products: -
?
D-Pro-Phe-Phe-4-methylcoumarin-7-amide + H2O
?
-
Substrates: -
Products: -
Products: -
?
D-Val-Leu-Arg-4-nitroanilide + H2O
D-Val-Leu-Arg + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
D-Val-Leu-Arg-4-nitroanilide + H2O
D-Val-Leu-Arg + 4-nitroaniline
-
Substrates: also known as S2266, a chromogenic substrate for tissue kallikrein
Products: -
Products: -
?
D-Val-Leu-Arg-4-nitroanilide + H2O
D-Val-Leu-Arg + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
D-Val-Leu-Arg-4-nitroanilide + H2O
D-Val-Leu-Arg + 4-nitroaniline
-
Substrates: S-2266, selective tissue kallikrein substrate
Products: -
Products: -
?
D-Val-Leu-Arg-4-nitroanilide + H2O
D-Val-Leu-Arg + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
D-Val-Leu-Arg-p-nitroanilide + H2O
D-Val-Leu-Arg + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
D-Val-Leu-Arg-p-nitroanilide + H2O
D-Val-Leu-Arg + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
D-Val-Leu-Arg-p-nitroanilide + H2O
D-Val-Leu-Arg + p-nitroaniline
-
Substrates: weak activity
Products: -
Products: -
?
D-Val-Leu-Arg-p-nitroanilide + H2O
D-Val-Leu-Arg + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
D-Val-Leu-Arg-p-nitroanilide + H2O
D-Val-Leu-Arg + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
D-Val-Leu-Arg-p-nitroanilide + H2O
D-Val-Leu-Arg + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
D-Val-Leu-Arg-p-nitroanilide + H2O
D-Val-Leu-Arg + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
D-Val-Leu-Lys-4-nitroanilide + H2O
D-Val-Leu-Lys + 4-nitroaniline
-
Substrates: weak activity
Products: -
Products: -
?
D-Val-Leu-Lys-4-nitroanilide + H2O
D-Val-Leu-Lys + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
D-Val-Leu-Lys-4-nitroanilide + H2O
D-Val-Leu-Lys + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
DL-Val-Leu-Arg-p-nitroanilide + H2O
DL-Val-Leu-Arg + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
DL-Val-Leu-Arg-p-nitroanilide + H2O
DL-Val-Leu-Arg + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
insulin-like growth factor binding proteins
?
-
Substrates: enhancement of IGF bioavailability, role in tumor progression
Products: -
Products: -
?
insulin-like growth factor binding proteins
?
-
Substrates: degradation of IGFBP 2-5
Products: -
Products: -
?
insulin-like growth factor binding proteins
?
-
Substrates: i.e. IGFBP
Products: -
Products: -
?
insulin-like growth factor binding proteins
insulin-like growth factor binding protein fragments
-
Substrates: i.e. IGFBP
Products: identification of products
Products: identification of products
?
insulin-like growth factor binding proteins
insulin-like growth factor binding protein fragments
-
Substrates: degradation of IGFBP 2-5
Products: identification of products
Products: identification of products
?
kininogen + H2O
bradykinin + kinin
-
Substrates: high-molecular weight kininogen
Products: -
Products: -
?
kininogen + H2O
bradykinin + kinin
-
Substrates: 3 additional claevage sites at Arg427, Arg437, and Arg457
Products: -
Products: -
?
kininogen + H2O
bradykinin + kinin heavy chain + kinin light chain
-
Substrates: important role in bradykinin release in seminal fluid
Products: -
Products: -
?
kininogen + H2O
bradykinin + kinin heavy chain + kinin light chain
-
Substrates: high-molecular weight kininogen
Products: -
Products: -
?
kininogen + H2O
bradykinin + kinin heavy chain + kinin light chain
-
Substrates: 3 additional cleavage sites at Arg427, Arg437, and Arg457
Products: -
Products: -
?
kininogen + H2O
bradykinin + kinin heavy chain + kinin light chain
-
Substrates: cleavage of rat kininogen at Arg-Arg and Arg-Ser
Products: -
Products: -
?
kininogen + H2O
kallidin + kinin heavy chain + kinin light chain
Substrates: -
Products: -
Products: -
?
kininogen + H2O
kallidin + kinin heavy chain + kinin light chain
Substrates: best substrate
Products: -
Products: -
?
kininogen + H2O
kallidin + kinin heavy chain + kinin light chain
Substrates: enzyme is involved in inflammation, sepsis, pancreatitis, bone metabolism, heart disease, renal disease, and cancer through release of kallidin, i.e. Lys-bradykinin
Products: -
Products: -
?
kininogen + H2O
kinin + ?
-
Substrates: -
Products: -
Products: -
?
kininogen + H2O
kinin + ?
-
Substrates: high molecular weight kininogen from human and rat
Products: -
Products: -
?
kininogen + H2O
kinin + ?
-
Substrates: high-molecular weight kininogen
Products: -
Products: -
?
kininogen + H2O
kinin + ?
-
Substrates: acts preferentially in low molecular weight kininogen
Products: -
Products: -
?
kininogen + H2O
kinin + ?
-
Substrates: high molecular weight kininogen from human and rat
Products: -
Products: -
?
kininogen + H2O
kinin + ?
-
Substrates: rat low molecular weight kininogen and bovine low molecular weight kininogen, T-kininogen
Products: -
Products: -
?
kininogen + H2O
kinin + ?
-
Substrates: wild-type and recombinant enzyme
Products: -
Products: -
?
low-molecular-weight kininogen + H2O
kallidin + kinin
-
Substrates: -
Products: -
Products: -
?
low-molecular-weight kininogen + H2O
kallidin + kinin
-
Substrates: -
Products: -
Products: -
?
low-molecular-weight kininogen + H2O
kallidin + kinin
Substrates: -
Products: kallidin is Lys-bradykinin
Products: kallidin is Lys-bradykinin
?
low-molecular-weight kininogen + H2O
kallidin + kinin
-
Substrates: -
Products: kallidin is Lys-bradykinin
Products: kallidin is Lys-bradykinin
?
low-molecular-weight kininogen + H2O
kallidin + kinin
Substrates: -
Products: kallidin is Lys-bradykinin
Products: kallidin is Lys-bradykinin
?
low-molecular-weight kininogen + H2O
kallidin + kinin
-
Substrates: human
Products: -
Products: -
?
low-molecular-weight kininogen + H2O
kallidin + kinin
Substrates: cleavage sequence and sites
Products: kallidin is Lys-bradykinin
Products: kallidin is Lys-bradykinin
?
low-molecular-weight kininogen + H2O
kallidin + kinin
-
Substrates: -
Products: -
Products: -
?
low-molecular-weight kininogen + H2O
kallidin + kinin
Substrates: -
Products: -
Products: -
?
low-molecular-weight kininogen + H2O
kallidin + kinin
-
Substrates: -
Products: -
Products: -
?
low-molecular-weight kininogen + H2O
kallidin + kinin
-
Substrates: bovine or human
Products: -
Products: -
?
low-molecular-weight kininogen + H2O
kallidin + kinin
-
Substrates: -
Products: -
Products: -
?
low-molecular-weight kininogen + H2O
kallidin + kinin
-
Substrates: -
Products: -
Products: -
?
N-alpha-acetyl-Tyr ethyl ester + H2O
N-alpha-acetyl-Tyr + ethanol
-
Substrates: -
Products: -
Products: -
?
N-alpha-acetyl-Tyr ethyl ester + H2O
N-alpha-acetyl-Tyr + ethanol
-
Substrates: -
Products: -
Products: -
?
N-alpha-benzoyl-L-Arg ethyl ester + H2O
N-alpha-benzoyl-L-Arg + ethanol
-
Substrates: -
Products: -
Products: -
?
N-alpha-benzoyl-L-Arg ethyl ester + H2O
N-alpha-benzoyl-L-Arg + ethanol
-
Substrates: -
Products: -
Products: -
?
N-alpha-benzoyl-L-Arg methyl ester + H2O
N-alpha-benzoyl-L-Arg + methanol
-
Substrates: -
Products: -
Products: -
?
N-alpha-benzoyl-L-Arg methyl ester + H2O
N-alpha-benzoyl-L-Arg + methanol
-
Substrates: -
Products: -
Products: -
?
N-alpha-benzoyl-L-Lys methyl ester + H2O
N-alpha-benzoyl-L-Lys + methanol
-
Substrates: -
Products: -
Products: -
?
N-alpha-benzoyl-L-Lys methyl ester + H2O
N-alpha-benzoyl-L-Lys + methanol
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-FRAPR-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-FRAPR-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-FRLVR-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-FRLVR-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-FRSSR-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-FR + SSR-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: sequence spanning the scissile Arg-Ser bond in human kininogen
Products: -
Products: -
?
o-aminobenzoyl-FRSSR-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-FR + SSR-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: sequence spanning the scissile Arg-Ser bond in human kininogen
Products: -
Products: -
?
o-aminobenzoyl-FRSVQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-FR + SVQ-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: sequence spanning the scissile Arg-Ser bond in bovine kininogen
Products: -
Products: -
?
o-aminobenzoyl-FRSVQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-FR + SVQ-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: sequence spanning the scissile Arg-Ser bond in bovine kininogen
Products: -
Products: -
?
o-aminobenzoyl-GFSPFRAPRVQ-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-GFSPFR + APRVQ-ethylenediamine 2,4-dinitrophenol + o-aminobenzoyl-GFSPF + RAPRVQ-ethylenediamine 2,4-dinitrophenol
-
Substrates: preferentially hydrolyzed at Phe-Arg bond compared with Phe-Arg
Products: -
Products: -
?
o-aminobenzoyl-GFSPFRAPRVQ-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-GFSPFR + APRVQ-ethylenediamine 2,4-dinitrophenol + o-aminobenzoyl-GFSPF + RAPRVQ-ethylenediamine 2,4-dinitrophenol
-
Substrates: preferentially hydrolyzed at Phe-Arg bond compared with Phe-Arg
Products: -
Products: -
?
o-aminobenzoyl-GFSPFRAPRVQ-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-GFSPFR + APRVQ-ethylenediamine 2,4-dinitrophenol + o-aminobenzoyl-GFSPF + RAPRVQ-ethylenediamine 2,4-dinitrophenol
-
Substrates: preferentially hydrolyzed at Phe-Arg bond compared with Phe-Arg
Products: -
Products: -
?
o-aminobenzoyl-GFSPFRSSRIGEIKEEQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-GFSPFR + SSRIGEIKEEQ-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: sequence spanning the scissile Arg-Ser bond in human kininogen
Products: -
Products: -
?
o-aminobenzoyl-GFSPFRSSRIGEIKEEQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-GFSPFR + SSRIGEIKEEQ-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: sequence spanning the scissile Arg-Ser bond in human kininogen
Products: -
Products: -
?
o-aminobenzoyl-GFSPFRSSRQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-GFSPFR + SSRQ-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: sequence spanning the scissile Arg-Ser bond in human kininogen
Products: -
Products: -
?
o-aminobenzoyl-GFSPFRSSRQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-GFSPFR + SSRQ-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: sequence spanning the scissile Arg-Ser bond in human kininogen
Products: -
Products: -
?
o-aminobenzoyl-GFSPFRSVQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-GFSPFR + SVQ-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: sequence spanning the scissile Arg-Ser bond in bovine kininogen
Products: -
Products: -
?
o-aminobenzoyl-GFSPFRSVQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-GFSPFR + SVQ-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: sequence spanning the scissile Arg-Ser bond in bovine kininogen
Products: -
Products: -
?
o-aminobenzoyl-GFSPFRSVQVMKYEGSQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-GFSPFR + SVQVMKYEGSQ-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: sequence spanning the scissile Arg-Ser bond in bovine kininogen
Products: -
Products: -
?
o-aminobenzoyl-GFSPFRSVQVMKYEGSQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-GFSPFR + SVQVMKYEGSQ-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: sequence spanning the scissile Arg-Ser bond in bovine kininogen
Products: -
Products: -
?
o-aminobenzoyl-GFSPFRSVTVQ-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-GFSPFR + SVTVQ-ethylenediamine 2,4-dinitrophenol
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-GFSPFRSVTVQ-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-GFSPFR + SVTVQ-ethylenediamine 2,4-dinitrophenol
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-GFSPFRSVTVQ-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-GFSPFR + SVTVQ-ethylenediamine 2,4-dinitrophenol
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-LMKRP-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-LM + KRP-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: low activity
Products: -
Products: -
?
o-aminobenzoyl-LMKRP-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-LM + KRP-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: sequence spanning the scissile Met-Lys bond in human and bovine kininogen
Products: -
Products: -
?
o-aminobenzoyl-LMKRP-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-LM + KRP-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-LMKRP-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-LM + KRP-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: low activity
Products: -
Products: -
?
o-aminobenzoyl-MTEMARRPPGFSPFRSVTVQ-NH2 + H2O
o-aminobenzoyl-MTEMAR + RPPGFSPFR + SVTVQ-NH2
-
Substrates: -
Products: RPPGFSPFR is bradykinin
Products: RPPGFSPFR is bradykinin
?
o-aminobenzoyl-MTEMARRPPGFSPFRSVTVQ-NH2 + H2O
o-aminobenzoyl-MTEMAR + RPPGFSPFR + SVTVQ-NH2
-
Substrates: -
Products: RPPGFSPFR is bradykinin
Products: RPPGFSPFR is bradykinin
?
o-aminobenzoyl-MTEMARRPPGFSPFRSVTVQ-NH2 + H2O
o-aminobenzoyl-MTEMAR + RPPGFSPFR + SVTVQ-NH2
-
Substrates: -
Products: RPPGFSPFR is bradykinin
Products: RPPGFSPFR is bradykinin
?
o-aminobenzoyl-MTEMARRPQ-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-MTEMAR + RPQ-ethylenediamine 2,4-dinitrophenol
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-MTEMARRPQ-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-MTEMAR + RPQ-ethylenediamine 2,4-dinitrophenol
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-MTEMARRPQ-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-MTEMAR + RPQ-ethylenediamine 2,4-dinitrophenol
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-MTSVIRRPPGFSPFRAPRV-NH2 + H2O
o-aminobenzoyl-MTSVIR + RPPGFSPFR + APRV-NH2
-
Substrates: -
Products: RPPGFSPFR is bradykinin
Products: RPPGFSPFR is bradykinin
?
o-aminobenzoyl-MTSVIRRPPGFSPFRAPRV-NH2 + H2O
o-aminobenzoyl-MTSVIR + RPPGFSPFR + APRV-NH2
-
Substrates: -
Products: RPPGFSPFR is bradykinin
Products: RPPGFSPFR is bradykinin
?
o-aminobenzoyl-MTSVIRRPQ-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-MTSVIR + RPQ-ethylenediamine 2,4-dinitrophenol
-
Substrates: slow hydrolysis
Products: -
Products: -
?
o-aminobenzoyl-MTSVIRRPQ-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-MTSVIR + RPQ-ethylenediamine 2,4-dinitrophenol
-
Substrates: slow hydrolysis
Products: -
Products: -
?
o-aminobenzoyl-MTSVIRRPQ-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-MTSVIR + RPQ-ethylenediamine 2,4-dinitrophenol
-
Substrates: slow hydrolysis
Products: -
Products: -
?
o-aminobenzoyl-Phe-Arg-Arg-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-Phe-Arg + Arg-ethylenediamine 2,4-dinitrophenol
-
Substrates: slow hydrolysis
Products: -
Products: -
?
o-aminobenzoyl-Phe-Arg-Arg-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-Phe-Arg + Arg-ethylenediamine 2,4-dinitrophenol
-
Substrates: slow hydrolysis
Products: -
Products: -
?
o-aminobenzoyl-Phe-Arg-Lys-GFSPFRSVTVQ-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-Phe-Arg + Lys-ethylenediamine 2,4-dinitrophenol
-
Substrates: slow hydrolysis
Products: -
Products: -
?
o-aminobenzoyl-Phe-Arg-Lys-GFSPFRSVTVQ-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-Phe-Arg + Lys-ethylenediamine 2,4-dinitrophenol
-
Substrates: slow hydrolysis
Products: -
Products: -
?
o-aminobenzoyl-Phe-Arg-Lys-GFSPFRSVTVQ-ethylenediamine 2,4-dinitrophenol + H2O
o-aminobenzoyl-Phe-Arg + Lys-ethylenediamine 2,4-dinitrophenol
-
Substrates: slow hydrolysis
Products: -
Products: -
?
o-aminobenzoyl-QPLGMISLMKRP-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-QPLGMISLM + KRP-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: sequence spanning the scissile Met-Lys bond in human kininogen
Products: -
Products: -
?
o-aminobenzoyl-QPLGMISLMKRP-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-QPLGMISLM + KRP-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: sequence spanning the scissile Met-Lys bond in human kininogen
Products: -
Products: -
?
o-aminobenzoyl-QPLGQTSLMKRP-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-QPLGQTSLM + KRP-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: sequence spanning the scissile Met-Lys bond in bovine kininogen
Products: -
Products: -
?
o-aminobenzoyl-QPLGQTSLMKRP-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-QPLGQTSLM + KRP-N-(2,4-dinitrophenyl)ethylene diamine
-
Substrates: sequence spanning the scissile Met-Lys bond in bovine kininogen
Products: -
Products: -
?
o-aminobenzoyl-SVIRRVQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-SVIRRVQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-VMIAALPRTMFIQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
-
Substrates: low activity
Products: -
Products: -
?
o-aminobenzoyl-VMIAALPRTMFIQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
-
Substrates: quenched fluorescent substrate, synthesized based on Bauhinia ungulata factor Xa inhibitor reactive sequence site
Products: -
Products: -
?
o-aminobenzoyl-VMIAALPRTMQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
-
Substrates: low activity
Products: -
Products: -
?
o-aminobenzoyl-VMIAALPRTMQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
?
-
Substrates: quenched fluorescent substrate, synthesized based on Bauhinia ungulata factor Xa inhibitor reactive sequence site
Products: -
Products: -
?
polypeptide + H2O
peptides
-
647361, 647483, 647485, 647486, 647487, 647488, 647497, 647498, 647500, 647501, 647502, 647503, 647506, 647508, 647509, 647510, 647512, 647513, 647514
Substrates: -
Products: -
Products: -
?
polypeptide + H2O
peptides
-
Substrates: S1' and S2' subsites of the enzyme play a determinant role in the recognition and hydrolysis of substrates
Products: -
Products: -
?
polypeptide + H2O
peptides
-
Substrates: serine at position P1' and arginine at position P2' result in high activity
Products: -
Products: -
?
polypeptide + H2O
peptides
-
Substrates: -
Products: -
Products: -
?
polypeptide + H2O
peptides
-
Substrates: serine at position P1' and arginine at position P2' results in high activity
Products: -
Products: -
?
polypeptide + H2O
peptides
Substrates: implicated in processing of growth factrors and peptide hormones
Products: -
Products: -
?
polypeptide + H2O
peptides
-
Substrates: -
Products: -
Products: -
?
polypeptide + H2O
peptides
-
Substrates: -
Products: -
Products: -
?
Pro-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
-
Substrates: -
Products: -
Products: -
?
Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
single-chain tissue-type plasminogen activator + H2O
?
-
Substrates: 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
Products: -
Products: -
?
single-chain tissue-type plasminogen activator + H2O
?
-
Substrates: -
Products: -
Products: -
?
Tosyl-Arg methyl ester + H2O
Tosyl-Arg + methanol
-
Substrates: -
Products: -
Products: -
?
Tosyl-Arg methyl ester + H2O
Tosyl-Arg + methanol
-
Substrates: -
Products: -
Products: -
?
Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
Val-Pro-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
Val-Pro-Arg + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity study
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity study
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: K1, sustrate specificty of S1 subsite, accepts both Arg and Phe
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificty study by phage display
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: likely the physiological activator of the zymogen form of prostate-specific antigen in the prostate
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in prostate cancer development
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in blood pressure regulation and inflammation processes
Products: -
Products: -
?
additional information
?
-
-
Substrates: tissue kallikrein 4 regulates the structure and functions of the tumor-associated urokinase-type plasminogen activator receptor
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme cleaves synthetic peptides after arginine but not lysine residues. It does not cleave chymotrypsin
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: KLK1 can release des-(Arg9)-Lys-bradykinin (KRPPGFSPF) directly from human kininogen, if S391 is phosphorylated
Products: -
Products: -
?
additional information
?
-
-
Substrates: KLK1 shows substrate specificity with Tyr and Arg preferred at P1 and Ser at P1'
Products: -
Products: -
?
additional information
?
-
Substrates: KLK1 shows substrate specificity with Tyr and Arg preferred at P1 and Ser at P1'
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme cleaves preferentially after arginine
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme cleaves preferentially after arginine
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity study
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
epithelial sodium channel + H2O
activated epithelial sodium channel + ?
-
Substrates: -
Products: -
Products: -
?
kininogen + H2O
bradykinin + kinin heavy chain + kinin light chain
-
Substrates: important role in bradykinin release in seminal fluid
Products: -
Products: -
?
low-molecular-weight kininogen + H2O
GMISLM + KRPPGFSPFR + SSRIG
Substrates: -
Products: KRPPGFSPFR is kallidin
Products: KRPPGFSPFR is kallidin
?
prolactin + H2O
lactin + ?
-
Substrates: three cleavage sites between Arg174-Arg175, Lys185-Phe186 and Arg188-Cys189
Products: -
Products: -
?
single-chain tissue-type plasminogen activator + H2O
?
-
Substrates: 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
Products: -
Products: -
?
vascular endothelial growth factor 164 + H2O
?
-
Substrates: -
Products: -
Products: -
?
insulin-like growth factor binding proteins
?
-
Substrates: enhancement of IGF bioavailability, role in tumor progression
Products: -
Products: -
?
insulin-like growth factor binding proteins
?
-
Substrates: degradation of IGFBP 2-5
Products: -
Products: -
?
insulin-like growth factor binding proteins
?
-
Substrates: i.e. IGFBP
Products: -
Products: -
?
kininogen + H2O
kallidin + kinin heavy chain + kinin light chain
Substrates: -
Products: -
Products: -
?
kininogen + H2O
kallidin + kinin heavy chain + kinin light chain
Substrates: best substrate
Products: -
Products: -
?
kininogen + H2O
kallidin + kinin heavy chain + kinin light chain
Substrates: enzyme is involved in inflammation, sepsis, pancreatitis, bone metabolism, heart disease, renal disease, and cancer through release of kallidin, i.e. Lys-bradykinin
Products: -
Products: -
?
low-molecular-weight kininogen + H2O
kallidin + kinin
-
Substrates: -
Products: -
Products: -
?
low-molecular-weight kininogen + H2O
kallidin + kinin
Substrates: -
Products: -
Products: -
?
low-molecular-weight kininogen + H2O
kallidin + kinin
-
Substrates: -
Products: -
Products: -
?
polypeptide + H2O
peptides
-
647361, 647483, 647485, 647486, 647487, 647488, 647497, 647498, 647500, 647501, 647502, 647503, 647506, 647508, 647509, 647510, 647512, 647513, 647514
Substrates: -
Products: -
Products: -
?
polypeptide + H2O
peptides
-
Substrates: S1' and S2' subsites of the enzyme play a determinant role in the recognition and hydrolysis of substrates
Products: -
Products: -
?
polypeptide + H2O
peptides
-
Substrates: -
Products: -
Products: -
?
polypeptide + H2O
peptides
-
Substrates: serine at position P1' and arginine at position P2' results in high activity
Products: -
Products: -
?
polypeptide + H2O
peptides
Substrates: implicated in processing of growth factrors and peptide hormones
Products: -
Products: -
?
polypeptide + H2O
peptides
-
Substrates: -
Products: -
Products: -
?
polypeptide + H2O
peptides
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: likely the physiological activator of the zymogen form of prostate-specific antigen in the prostate
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in prostate cancer development
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in blood pressure regulation and inflammation processes
Products: -
Products: -
?
additional information
?
-
-
Substrates: tissue kallikrein 4 regulates the structure and functions of the tumor-associated urokinase-type plasminogen activator receptor
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Na+
additional information
additional information
Mg2+ has no significant effect on the enzyme activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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-Lys-Phe-Phe-Pro-Leu-Glu-NH2
-
leader compound for design of specific inhibitors of K1; weak inhibition
Bauhinia bauhinioides Kunitz-type serine protease inhibitor
BbKI or BbTI-II, recombinant protein expressed in Escherichia coli Rosetta 2 (DE3) as His6-MBP-TEV-BbKI construct, the MBP tag is cleaved off. An 18 kDa protein originally isolated from the seeds of Bauhinia bauhinioides. The protein is a potent inhibitor of the trypsin-like plasma kallikrein, but also a potent inhibitor of human tissue kallikrein 4 (KLK4) and the chymotrypsin-like human tissue kallikrein 7 (KLK7). Modeling of structures of BbKI complexed with the catalytic domain of human plasma kallikrein, and with KLK4 and KLK7, structure comparisons and interaction analysis, overview. Competitive inhibition; BbKI or BbTI-II, recombinant protein expressed in Escherichia coli Rosetta 2 (DE3) as His6-MBP-TEV-BbKI construct, the MBP tag is cleaved off. An 18 kDa protein originally isolated from the seeds of Bauhinia bauhinioides. The protein is a potent inhibitor of the trypsin-like plasma kallikrein, but also a potent inhibitor of human tissue kallikrein 4 (KLK4) and the chymotrypsin-like human tissue kallikrein 7 (KLK7). Modeling of structures of BbKI complexed with the catalytic domain of human plasma kallikrein, and with KLK4 and KLK7, structure comparisons and interaction analysis, overview. Competitive inhibition
-
Bauhinia bauhinioides Kunitz-type serine protease inhibitor mutant L55R
recombinant protein expressed in Escherichia coli Rosetta 2 (DE3) as His6-MBP-TEV-BbKI construct, the MBP tag is cleaved off. Modeling of structures of BbKI mutant complexed with the catalytic domain of human plasma kallikrein, and with KLK4 and KLK7, structure comparisons and interaction analysis, overview; recombinant protein expressed in Escherichia coli Rosetta 2 (DE3) as His6-MBP-TEV-BbKI construct, the MBP tag is cleaved off. Modeling of structures of BbKI mutant complexed with the catalytic domain of human plasma kallikrein, and with KLK4 and KLK7, structure comparisons and interaction analysis, overview
-
Bauhinia bauhinioides trypsin inhibitor II
-
N-terminal sequence of the protein is SVVVDTNGQPVSNGADAYYLV; i.e. BbTI-II
-
diisopropylfluorophosphate
-
2.0 mM, complete inhibition of hydrolysis of Pro-Phe-Arg-4-methylcoumarin-7-amide
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-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
pepstatin
-
0.01 mM, 10% inhibition of hydrolysis of Pro-Phe-Arg-4-methylcoumarin-7-amide
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
-
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.
-
tissue kallikrein-binding protein
-
rapidly forms a covalent complex with tissue kallikrein
-
alpha1-antitrypsin
-
slowly binds to tissue kallikrein and suppresses its activity
-
antipain
-
0.1 mM, 90% inhibition of hydrolysis of Pro-Phe-Arg-4-methylcoumarin-7-amide
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 37°C for 1 h
Aprotinin
-
blocks increase of DU145 cell migration and invasion by tissue kallikrein
benzamidine
-
1 mM, 80% inhibition of hydrolysis of Pro-Phe-Arg-4-methylcoumarin-7-amide
chymostatin
-
0.01 mM, 5% inhibition of hydrolysis of Pro-Phe-Arg-4-methylcoumarin-7-amide
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
-
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
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
SERPINA4 of the serine protease inhibitor (serpin) superfamily, a kallikrein binding protein that causes specific inhibition of tissue kallikrein 1 (KLK1). Serpins share a conserved mouse-trap mechanism in inhibiting their target proteases. The protease binds and attacks the scissile bond in the reactive center loop of the native serpin. Heparin blocks the inhibition of KLK1 by kallistatin through electrostatic repulsion. The heparin binding site of kallistatin is located on a surface with positive electrostatic potential near a unique protruded 310 helix between helix H and strand 2 of beta-sheet C. Heparin binding on this site prevents KLK1 from docking onto kallistatin due to the electrostatic repulsion between heparin and the negatively charged surface of KLK1, thus blocking the inhibition of KLK1 by kallistatin. Replacement of the acidic exosite 1 residues of KLK1 with basic amino acids as in thrombin results in accelerated inhibition. Analysis of the heparin binding site of kallistatin. Heparin binds across the center of the heparin binding area of kallistatin while KLK1 surface loops form exosite interactions with the rim of this area involving residues such as K307, R308, K312, and K313
-
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
Protein C inhibitor
cleaves the inhibitor at Arg354-Ser355 without inactivating it; covalent complex formation with K2
-
Soybean trypsin inhibitor
-
kallikrein B is inhibited, kallikrein A not
-
additional information
-
no inhibition by Bauhinia bauhinioides trypsin inhibitor I
-
additional information
-
cardiac glycosides can dramatically suppress the transcription of KLKs
-
additional information
crystallization of purified recombinant wild-type kallistatin free or in complex with heparin by sitting-drop vapor-diffusion method, mixing of 200 nl of 10 mg/ml protein in 10 mM Tris-HCl, pH 7.4, and 0.1 M NaCl with 200 nl of precipitant solution containing 40% tert-butanol, and equilibration against 0.08 ml reservoir solution. A cryosolution consisting of 10% glycerol and 10% ethylene glycol is directly added to the drop and the crystals are quickly picked up using a micro-loop and flash-cooled in liquid nitrogen, X-ray diffraction structure determination and analysis at 1.8-1.9 A resolution, molecular replacement method using reactive loop cleaved PCI structure (PDB ID 3DY0) as search model
-
additional information
DNA of nine selected scFvs is isolated from the phages in a phage display, and the unique sequences are recloned into the pCSE2.6-hIgG1-Fc-XP vector for production as the IgG-like antibody format scFv-Fc. For the production of the functional antibodies, the pCSE2.6-hIgG1-Fc-XP vectors containing the unique sequences are transfected into HEK293-6E cells. The antibody products are purified using protein A
-
additional information
-
not inhibited by interleukin-1beta-converting enzyme inhibitors
-
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 bauhinioides trypsin inhibitor I
-
additional information
-
no inhibition by Bauhinia ungulata factor Xa inhibitor, and Bauhinia variegata trypsin inhibitor
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
aldosterone
-
increased aldosterone levels lead to enhanced kallikrein activity
chymase
-
stimulation, in correlation with secretory leukoprotease inhibitor stimulation, in stimulated serous cells
-
hyaluronidase
-
increases K2 enzyme activity by digesting the K2-bound hyaluronic acid
-
Thermolysin
-
thermolysin activates prokallikrein cleaving off the N-terminal Ile1-Val2
-
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
-
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
-
additional information
-
administration of glibenclamide or N,N'-dicyclohexyl-4-morholinecarboxamide increases urinary kallikrein secretion
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0015
Abz-FRSSR-Q-EDDnp
pH and temperature not specified in the publication
0.00036
Abz-GFSPFRSLRI-Q-EDDnp
pH and temperature not specified in the publication
0.0002
Abz-GFSPFRSSRI-Q-EDDnp
pH and temperature not specified in the publication
0.009
Abz-MISLMKLP-Q-EDDnp
pH and temperature not specified in the publication
0.0007
Abz-MISLMKRP-Q-EDDnp
pH and temperature not specified in the publication
0.00027
o-aminobenzoyl-AIKFFIRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.00013
o-aminobenzoyl-AIKFFQRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.0018
o-aminobenzoyl-AIKFFSAE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.00021
o-aminobenzoyl-AIKFFSKE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.0013
o-aminobenzoyl-AIKFFSPE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.00036
o-aminobenzoyl-AIKFFSRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.00094
o-aminobenzoyl-AIKFFSSE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.00023
o-aminobenzoyl-AIKFFTRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.0007
o-aminobenzoyl-GFSPF-4-(aminocyclohexyl)alanine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.0038
o-aminobenzoyl-GFSPF-4-(aminomethyl)-N-isopropylphenylalanine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.0003
o-aminobenzoyl-GFSPF-4-(aminomethyl)phenylalanine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.00064
o-aminobenzoyl-GFSPF-4-piperidinylalanine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.001
o-aminobenzoyl-GFSPF-Nim-(dimethyl)histidine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.0027
o-aminobenzoyl-LPRTMFIQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 8.0, 37°C
0.0036
o-aminobenzoyl-Phe-4-(aminomethyl)phenylalanine-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.00024 - 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, 37°C
0.00023
o-aminobenzoyl-VMIAALPRTMFIQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 8.0, 37°C
0.0005
o-aminobenzoyl-VMIAALPRTMQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 8.0, 37°C
0.12
DL-Val-Leu-Arg-p-nitroanilide
-
recombinant enzyme from liver, pH 8.0, 22°C
0.154
DL-Val-Leu-Arg-p-nitroanilide
-
recombinant enzyme from salivary gland, pH 8.0, 22°C
0.158
DL-Val-Leu-Arg-p-nitroanilide
-
recombinant enzyme from pancreas, pH 8.0, 22°C
0.0002
o-aminobenzoyl-FRSSR-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30°C
0.0009
o-aminobenzoyl-FRSVQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30°C
0.0067
o-aminobenzoyl-GFSPFRSSRIGEIKEEQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30°C
0.0104
o-aminobenzoyl-GFSPFRSSRIGEIKEEQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30°C
0.0004
o-aminobenzoyl-GFSPFRSSRQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30°C
0.00076
o-aminobenzoyl-GFSPFRSSRQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30°C
0.00035
o-aminobenzoyl-GFSPFRSVQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30°C
0.0014
o-aminobenzoyl-GFSPFRSVQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30°C
0.00041
o-aminobenzoyl-GFSPFRSVQVMKYEGSQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30°C
0.00051
o-aminobenzoyl-GFSPFRSVQVMKYEGSQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30°C
0.0023
o-aminobenzoyl-LMKRP-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30°C
0.00024
o-aminobenzoyl-Phe-Arg-Lys-GFSPFRSVTVQ-ethylenediamine 2,4-dinitrophenol
-
-
0.00077
o-aminobenzoyl-Phe-Arg-Lys-GFSPFRSVTVQ-ethylenediamine 2,4-dinitrophenol
-
-
0.0039
o-aminobenzoyl-QPLGMISLMKRP-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30°C
0.0042
o-aminobenzoyl-QPLGMISLMKRP-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30°C
0.0003
o-aminobenzoyl-QPLGQTSLMKRP-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30°C
0.0455
o-aminobenzoyl-QPLGQTSLMKRP-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30°C
0.084
Pro-Phe-Arg-4-methylcoumarin 7-amide
-
naturally occuring urinary enzyme, pH 8.0, 22°C
0.099
Pro-Phe-Arg-4-methylcoumarin 7-amide
-
recombinant enzyme from liver, pH 8.0, 22°C
0.112
Pro-Phe-Arg-4-methylcoumarin 7-amide
-
recombinant enzyme from pancreas, pH 8.0, 22°C
0.114
Pro-Phe-Arg-4-methylcoumarin 7-amide
-
recombinant enzyme from salivary gland, pH 8.0, 22°C
0.516
succinyl-Val-Pro-Phe-thiobenzyl ester
-
naturally occuring urinary enzyme, pH 8.0, 22°C
0.668
succinyl-Val-Pro-Phe-thiobenzyl ester
-
recombinant enzyme from liver, pH 8.0, 22°C
0.764
succinyl-Val-Pro-Phe-thiobenzyl ester
-
recombinant enzyme from salivary gland, pH 8.0, 22°C
0.842
succinyl-Val-Pro-Phe-thiobenzyl ester
-
recombinant enzyme from pancreas, pH 8.0, 22°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.6
Abz-FRSSR-Q-EDDnp
pH and temperature not specified in the publication
4.6
Abz-GFSPFRSLRI-Q-EDDnp
pH and temperature not specified in the publication
17.7
Abz-GFSPFRSSRI-Q-EDDnp
pH and temperature not specified in the publication
0.02
Abz-MISLMKLP-Q-EDDnp
pH and temperature not specified in the publication
0.33
Abz-MISLMKRP-Q-EDDnp
pH and temperature not specified in the publication
0.05
o-aminobenzoyl-AIKFFIRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.02
o-aminobenzoyl-AIKFFQRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.54
o-aminobenzoyl-AIKFFSAE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.21
o-aminobenzoyl-AIKFFSKE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.05
o-aminobenzoyl-AIKFFSPE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
3.33
o-aminobenzoyl-AIKFFSRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.3
o-aminobenzoyl-AIKFFSSE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.04
o-aminobenzoyl-AIKFFTRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.51
o-aminobenzoyl-GFSPF-4-(aminocyclohexyl)alanine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.81
o-aminobenzoyl-GFSPF-4-(aminomethyl)-N-isopropylphenylalanine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
1.8
o-aminobenzoyl-GFSPF-4-(aminomethyl)phenylalanine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.61
o-aminobenzoyl-GFSPF-4-piperidinylalanine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
2.1
o-aminobenzoyl-GFSPF-Nim-(dimethyl)histidine-SSRPQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
1
o-aminobenzoyl-Phe-4-(aminomethyl)phenylalanine-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
1.2
o-aminobenzoyl-Phe-Nim-(dimethyl)histidine-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.0005
o-aminobenzoyl-VMIAALPRTMFIQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 8.0, 37°C
0.004
o-aminobenzoyl-VMIAALPRTMQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 8.0, 37°C
1.16
DL-Val-Leu-Arg-p-nitroanilide
-
recombinant pancreatic enzyme, pH 8.0, 22°C
3
o-aminobenzoyl-GFSPFRSSRIGEIKEEQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30°C
3.1
o-aminobenzoyl-GFSPFRSSRIGEIKEEQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30°C
7.5
o-aminobenzoyl-GFSPFRSSRQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30°C
0.94
o-aminobenzoyl-GFSPFRSVQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30°C
1.5
o-aminobenzoyl-GFSPFRSVQVMKYEGSQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30°C
40.1
o-aminobenzoyl-GFSPFRSVQVMKYEGSQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30°C
18.4
o-aminobenzoyl-Phe-Arg-Lys-GFSPFRSVTVQ-ethylenediamine 2,4-dinitrophenol
-
-
21.8
o-aminobenzoyl-Phe-Arg-Lys-GFSPFRSVTVQ-ethylenediamine 2,4-dinitrophenol
-
-
0.4
o-aminobenzoyl-QPLGMISLMKRP-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30°C
7.1
o-aminobenzoyl-QPLGMISLMKRP-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30°C
0.6
o-aminobenzoyl-QPLGQTSLMKRP-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30°C
1.1
o-aminobenzoyl-QPLGQTSLMKRP-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 30°C
5.3
Pro-Phe-Arg-4-methylcoumarin 7-amide
-
recombinant enzyme from liver, pH 8.0, 22°C
6.1
Pro-Phe-Arg-4-methylcoumarin 7-amide
-
naturally occuring urinary enzyme, pH 8.0, 22°C
7.3
Pro-Phe-Arg-4-methylcoumarin 7-amide
-
recombinant salivary enzyme, pH 8.0, 22°C
7.4
Pro-Phe-Arg-4-methylcoumarin 7-amide
-
recombinant pancreatic enzyme, pH 8.0, 22°C
2
succinyl-Val-Pro-Phe-thiobenzyl ester
-
recombinant enzyme from liver and naturally occuring urinary enzyme, pH 8.0, 22°C
27
succinyl-Val-Pro-Phe-thiobenzyl ester
-
recombinant pancreatic enzyme, pH 8.0, 22°C
29
succinyl-Val-Pro-Phe-thiobenzyl ester
-
recombinant salivary enzyme, pH 8.0, 22°C
additional information
o-aminobenzoyl-MTSVIRRPQ-ethylenediamine 2,4-dinitrophenol
-
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1067
Abz-FRSSR-Q-EDDnp
pH and temperature not specified in the publication
12780
Abz-GFSPFRSLRI-Q-EDDnp
pH and temperature not specified in the publication
88500
Abz-GFSPFRSSRI-Q-EDDnp
pH and temperature not specified in the publication
2
Abz-MISLMKLP-Q-EDDnp
pH and temperature not specified in the publication
471
Abz-MISLMKRP-Q-EDDnp
pH and temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
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, 37°C
0.000000036 - 0.0000022
Bauhinia bauhinioides Kunitz-type serine protease inhibitor mutant L55R
-
0.00000013
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
-
0.00033
o-aminobenzoyl-AIKFFARE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.0004
o-aminobenzoyl-AIKFFERE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.00015
o-aminobenzoyl-AIKFFKRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.00032
o-aminobenzoyl-AIKFFLRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.00035
o-aminobenzoyl-AIKFFNRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.00009
o-aminobenzoyl-AIKFFPRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.00021
o-aminobenzoyl-AIKFFRRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.00051
o-aminobenzoyl-AIKFFSEE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.001
o-aminobenzoyl-AIKFFSIE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.00019
o-aminobenzoyl-AIKFFSLE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.00073
o-aminobenzoyl-AIKFFSNE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.0006
o-aminobenzoyl-AIKFFSQE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.00032
o-aminobenzoyl-AIKFFSTE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.0017
o-aminobenzoyl-AIKFFSVE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.00022
o-aminobenzoyl-AIKFFVRE-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.000022
o-aminobenzoyl-D-Lys-L-Phe-L-Arg-D-Arg-L-Gln-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.000029
o-aminobenzoyl-D-Lys-L-Phe-L-Phe-D-Arg-L-Gln-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.00005
o-aminobenzoyl-F-4-(aminomethyl)cyclohexylalanine-SRQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pH 9.0, 37°C
0.000000045
Bauhinia bauhinioides Kunitz-type serine protease inhibitor
pH 8.0, temperature not specified in the publication
-
0.00000018
Bauhinia bauhinioides Kunitz-type serine protease inhibitor
pH 8.0, temperature not specified in the publication
-
0.000000036
Bauhinia bauhinioides Kunitz-type serine protease inhibitor mutant L55R
pH 8.0, temperature not specified in the publication
-
0.0000022
Bauhinia bauhinioides Kunitz-type serine protease inhibitor mutant L55R
pH 8.0, temperature not specified in the publication
-
additional information
additional information
kallistatin inhibition kinetics, overview
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
96.5
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
8.2
8.5
9
-
tosyl-Arg methyl ester hydrolase activity and kininogenase activity of wild-type and recombinant enzyme
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9.5
-
pH 6.5: about 30% of maximal activity, pH 9.5: about 40% of maximal activity
7 - 10
about 35% activity at pH 7.0, about 90% activity at pH 8.0, about 55% activity at pH 9.0, about 35% activity at pH 10.0
8 - 10
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
647332, 647361, 647483, 647485, 647486, 647487, 647488, 647489, 647497, 647498, 647500, 647501, 647502, 647503, 647506, 647508, 647509, 647510, 647512, 647513, 647514, 647519, 647522, 647523, 647531, 647536, 647537, 647542, 664270, 665230, 667476, 667876
-
-
brenda
-
668489, 669226, 669627, 669651, 669753, 670218, 670649, 677844, 678468, 678522, 678523, 679016, 679071, 679520, 681754, 682071, 695948, 696026, 696531, 696533, 696534, 696535, 697148, 697377, 698169, 698292, 698297, 698327, 699317, 700407, 700918, 707005, 707431, 707619, 707627, 708436, 709251, 709621, 710059, 710169, 717095, 717166, 717446, 717501, 717572, 731256, 731367, 731632, 731671, 731894, 732735, 732782, 732932
-
-
brenda
patients with pemphigus foliaceus (autoimmune blistering disease) and control
-
-
brenda
-
667476, 668967, 669519, 670739, 671024, 679490, 681581, 695496, 696531, 697725, 699620, 707431, 707619, 717526, 718318, 731281
-
-
brenda
-
647331, 647361, 647480, 647482, 647494, 647495, 647496, 647504, 647505, 647530, 667476, 682915, 696536, 698203, 698208, 707619, 707627, 708396, 708418, 717193, 717664, 731110, 731959, 732367
-
-
brenda
gene KLK1, pancreatic glandular kallikrein 1 precursor
SwissProt
brenda
different forms of beta-kallikrein, i.e. Cbeta-kallikrein, Abeta-kallikrein, and Tbeta-kallikrein, are built from alpha-kallikrein via chymotrypsin digestion
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
secretory epithelial cells tf trachea, thyroid gland, mammary gland, salivary gland, jejunum, ileum, epididymis, seminal vesicle and urethra
brenda
-
activity in plasma of patients with pemphigus foliaceus is significantly increased compared with controls
brenda
activity is higher during the middle of the menstrual cycle, possible up-regulation by estrogens
brenda
-
almost every kallikrein is expressed in the salivary gland
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
secretion
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
human tissue kallikreins (KLKs) constitute a family of 15 serine proteases that are distributed in various tissues and implicated in several pathological disorders
malfunction
metabolism
physiological function
malfunction
-
genetically ablating tissue kallikrein in mice results in dilated decompensated cardiomyopathy
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
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
-
molecular knockdown of endogenous KLK1 expression attenuates advanced glycation end-products-induced interleukin-8 and intercellular adhesion molecule-1 productions in vitro
malfunction
-
partial or total deficiency in tissue kallikrein induces resistance to the infarct size reducing effect of cyclosporin A in cardiac ischemia in mice
malfunction
enzyme inhibition accelerates the initial virus-induced apoptotic depletion of alveolar macrophages
metabolism
heparin controls the specificity of KLK1 inhibitor kallistatin, such that kinin generation by KLK1 within the microcirculation will be locally protected by the binding of kallistatin to the heparin-like glycosaminoglycans of the endothelium
metabolism
-
tissue kallikrein (TK), a subgroup of serine proteinases, is an important component of the kallikrein-kinin system. Exogenous TK attenuated cerebral vasospasm in a rabbit model of subarachnoid hemorrhage
physiological function
-
purified tissue kallikrein promotes DU145 prostate cancer cell migration in a similar manner than rat tissue kallikrein
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
-
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
-
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
-
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
-
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
-
tissue kallikrein is a unique kalliuretic factor that protects against hyperkalemia after a dietary potassium load
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
-
up-regulation of KLK1 in tubular epithelial cells may mediate pro-inflammatory pathway and protease-activated receptor activation during diabetic nephropathy
physiological function
-
tissue kallikrein induces SH-SY5Y cell proliferation via epidermal growth factor receptor and extracellular signal-regulated kinase1/2 pathway
physiological function
-
tissue kallikrein is required for the cardioprotective effect of cyclosporin A in myocardial ischemia in the mouse. The enzyme is required for the mitochondrial action of cyclosporin A and may interact with cyclophilin D
physiological function
-
tissue kallikrein reduces cell injury induced by oxygen and glucose deprivation/reoxygenation through activating and increasing the protein expression of Homer1b/c protein
physiological function
-
tissue kallikrein promotes vessel growth by increasing the number of peripheral endothelial progenitor cells and enhancing their functional properties through the kinin B2 receptor-Akt signaling pathway. The enzyme reduces hypoxia-induced apoptosis of peripheral endothelial progenitor cells and increases cardiac function after myocardial infarction
physiological function
-
tissue kallikrein treatment significantly reduces monocyte chemoattractant protein-1, intercellular adhesion molecule-1, and interleukin-6 levels in retinal pigment epithelium-choroid complexes. Tissue kallikrein exhibits antiangiogenic properties by cleaving vascular endothelial growth factor 164 in a laser-induced choroidal neovascularization model
physiological function
-
exogenous tissue kallikrein attenuates the cerebral ischemia/reperfusion induced rat hippocampal CA1 neurons injury through activating the beta-arrestin-2 assembled B2R-Raf-MEK1/2 signaling module
physiological function
the enzyme regulates alveolar macrophage apoptosis early in influenza virus infection
physiological function
-
the enzyme ameliorates cerebral vasospasm and inhibits apoptosis in the basilar artery in a rabbit model of subarachnoid hemorrhage. The enzyme increases levels of nitric oxide which has a vasodilatory effect, but does not affect levels of endothelin-1, which has a vasoconstrictive effect
physiological function
-
the enzyme protects SH-SY5Y neuronal cells against oxygen and glucose deprivation-induced injury through bradykinin B2 receptor-dependent regulation of autophagy induction. The enzyme decreases cell death caused by oxygen and glucose deprivation
physiological function
kinin generation by KLK1 within the microcirculation
physiological function
tissue kallikrein KLK7 is an unusual serine protease that presents both trypsin-like and chymotrypsin-like specificity and appears to be upregulated in pathologies that are related to skin desquamation processes, such as atopic dermatitis, psoriasis, and Netherton syndrome
physiological function
-
the kallikrein-kinin system (KKS) has been considered as an inflammatory response system, which influences the biological systems and possesses multiple pleiotropic functions. KKS have key roles in vascular permeability and inflammation as well as thrombosis and blood coagulation. Tissue kallikrein (TK), a subgroup of serine proteinases, is an important component of the KKS, which processes low molecular weight kininogen to release kinin peptide, in turn activating bradykinin B1 and B2 receptors and triggering a host of biological effects. Tissue kallikrein (TK) plays an important role in the kallikrein-kinin system. It plays a protective role in traumatic brain injury (TBI). TK can regulate blood pressure, contract and relax smooth muscle, stimulate vascular cell growth, improve vascular permeability, inactivate inflammatory cascades, maintain electrolyte balance, and ameliorate pain. Determination and analysis of the relationship between serum TK levels and trauma severity in addition to clinical outcome in TBI, overview. TK levels are significantly lower in patients than in controls
Show AA Sequence and Transmembrane Helices (518 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11000
-
x * 11000 + x * 16000, kallikrein A, SDS-PAGE after reduction with 2-mercaptoethanol
14000
16000
18000
32000
34000
-
x * 34000 or x * 37000, the two molecular species represent differentially glycosylated forms
36000
37000
-
x * 34000 or x * 37000, the two molecular species represent differentially glycosylated forms
38000
39000
40000
additional information
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
16000
-
x * 4000 + x * 16000, kallikrein B, SDS-PAGE after reduction with 2-mercaptoethanol
16000
-
x * 11000 + x * 16000, kallikrein A, SDS-PAGE after reduction with 2-mercaptoethanol
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
?
-
x * 4000 + x * 16000, kallikrein B, SDS-PAGE after reduction with 2-mercaptoethanol
?
-
x * 11000 + x * 16000, kallikrein A, SDS-PAGE after reduction with 2-mercaptoethanol
?
-
x * 34000 or x * 37000, the two molecular species represent differentially glycosylated forms
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
side-chain modification
glycoprotein
the enzyme has two glycosylated sites within the active protease domain
proteolytic modification
-
thermolysin activates prokallikrein cleaving off the N-terminal Ile1-Val2
proteolytic modification
-
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
-
urinary and renal kallikrein exist in both active and proenzyme form
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
side-chain modification
-
multiple forms are due at least in part to varying carbohydrates
side-chain modification
-
the glycoprotein consists of 283 amino acid residues and 19-21 sugar residues
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
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme expressed in a deglycosylated form at high levels in Pichia pastoris, structure analysis
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
construction of KLK1 enzyme variant KLK1-99Lm lacking nine residues from its 99 loop
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing results in at least three-fold increase of specific activity
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.1 N NaCl, 0.01 M sodium phosphate buffer, pH 7.0, stable for months
-
20°C, purified urinary enzyme, 0.02% w/v NaN3, neutral pH, stable for more than 14 days
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by affinity column chromatography
from urine
the recombinant wild-type and mutant enzymes dissolved from inclusion bodies after expression in Escherichia coli strain BL21(DE3) is further purified by dialysis against 20 mM Tris-HCl, pH 7.4, 0.5 M NaCl, and 20 mM imidazole and affinity chromatography on a HiTrap FF column. KLK1 is activated by protease SENP2 releasing the SUMO3 tag from the fusion protein, and further purification on a Hitrap SP HP column and elution by a NaCl gradient (0.05-1 M), ultrafiltration and dialysis against 10 mM Tris-HCl, pH 7.4, 0.1 M NaCl
to homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
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
-
expression of recombinant human prokallikrein and kallikrein in engineered Chinese hamster ovary cells
-
gene KLK1, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) in inclusion bodies
genetic organization and structure of the kallikrein gene family, clustered on chromosome 19q13.3-q13.4
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
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
blood plasma tissue kallikrein levels are significantly lower in stroke patients, especially those with ischemic stroke
-
dietary potassium loading stimulates directly the secretion of tissue kallikrein independently of aldosterone
-
enzyme levels in lung tissue and in bronchoalveolar lavage fluid increase substantially during infection with influenza H3N2 virus
excretion of tissue kallikrein is stimulated following 5 days of a high-K+ or low-Na+ diet in rats
-
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
-
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
-
lower human kallikrein protein levels are observed in proangiogenic cells from type 2 diabetic patients
-
patients with coronary artery disease and acute coronary syndrome have significantly elevated KLK1 levels
-
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
-
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
-
there is an increase of glandular kallikrein in skin, mucus, kidney, gills, and leukocytes of Vibrio ordalii- and Piscirickettsia salmonis-infected fish
-
tissue kallikrein (KLK1) expression is up-regulated in human diabetic kidney tissue and induced by high glucose in human proximal tubular epithelial cells
-
tubular expression of KLK1 in diabetic kidney biopsies. High-glucose stimulates expression of KLK1
-
urinary kallikrein excretion is significantly reduced in patients with mild renal disease, and to a further extent in patients with severe renal failure
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) inclusion bodies by rapid dilution of dissolved inclusion bodies into refolding buffer containing 50 mM Tris-HCl, pH 8.0, 0.6 M arginine, 20 mM CaCl2, 10% v/v glycerol, 10 mM reduced glutathione, and 1 mM oxidized glutathione for 16 h at 4 C with a final protein concentration less than 0.3 mg/ml
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APPLICATION
ORGANISM
UNIPROT
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
diagnostics
drug development
medicine
diagnostics
-
tissue kallikrein (TK), a subgroup of serine proteinases, is a potential serum biomarker to predict delayed cerebral ischemia in aneurysmal subarachnoid hemorrhage (aSAH) for assessment of hemorrhagic severity and prediction of DCI following aSAH. TK levels are substantially lower in aSAH patients than in controls, overview. TK concentration is independently associated with an unfavorable outcome for stroke or head trauma patients
diagnostics
-
serum tissue kallikrein (TK) can represent a potential predictor of clinical outcome in traumatic brain injury (TBI) patients. Determination and analysis of the relationship between serum TK levels and trauma severity in addition to clinical outcome in TBI, overview. TK levels are significantly lower in patients than in controls
diagnostics
-
analysis of the association between a serum tissue kallikrein (TK) level and a 90-day outcome in 75 acute ischemic stroke (AIS) patients, who received acute reperfusion therapy, revelas that a higher baseline TK is independently associated with a favorable functional outcome (mRS 0-2), 95% confidence interval (CI), and low mortality rate at 90 days. Serum TK can be a promising predictor of clinical outcome in those AIS patients
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
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
KLK7 represents a potential target for new therapeutic procedures for diseases related to skin desquamation processes, it is a target for development of therapeutic protease inhibitors for diseases related to uncontrolled kallikrein activity
medicine
-
enzyme complexed with prostate protease inhibitor-6 may be a naturally occuring marker of tissue damage and necrosis associated with neoplasia
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
-
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
-
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
-
kallikrein may serve as new drug target for the prevention and treatment of heart failure, renal disease and stroke in humans
medicine
-
tissue kallikreins, particularly KLK6, are considered potential candidates for epithelial antimetastatic therapy
medicine
-
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
-
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
-
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
-
rhinovirus-induced human tissue kallikrein activation may contribute to airway inflammation and asthmatic exacerbations
medicine
-
expression of tissue kallikrein exerts antihypertrophic and antifibrotic actions in the heart
medicine
-
urinary kallikrein excretion is positively correlated to renal function, serum and urinary inflammatory mediator monocyte chemoattractant protein-1 in chronic kidney disease patients
medicine
-
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
-
kallidinogenase may be efficacious for simple retinopathy including hyperpermeability in subjects with diabetes
medicine
-
tissue kallikrein therapy is a promising regimen in the treatment of acute ischemic stroke in humans
medicine
-
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
-
tissue kallikrein administration can remarkably alleviate hypoxia/reoxygenation-induced neuronal injury by reduction of lactate dehydrogenase release and promotion of neuron viability
medicine
-
KLK10 expression and stage are independent predictors of unfavorable DFS and overall survival in colorectal cancer
medicine
-
high KLK1 levels are an independent predictor for coronary artery disease
EXTERNAL LINKS (specific for EC-Number 3.4.21.35)
Transporter Classification Database (TCDB): 8.A.131.1.5
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Release 2026.1 (March 2026)
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