Information on EC 3.4.21.118 - kallikrein 8

Word Map on EC 3.4.21.118
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.118
-
RECOMMENDED NAME
GeneOntology No.
kallikrein 8
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
171715-15-4
-
9001-01-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
C57BL/6 mice
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-Pro-Phe-Arg-4-nitroanilide + H2O
acetyl-Pro-Phe-Arg + 4-nitroaniline
show the reaction diagram
benzoyl-Phe-Val-Arg-4-methylcoumarin 7-amide + H2O
benzoyl-Phe-Val-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Gly-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
1.2% activity compared to tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
-
?
benzyloxycarbonyl-Gly-Gly-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Gly-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
ratio kcat/KM-value is 1000 M/s
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
ratio kcat/KM-value is 1000 M/s
-
-
?
benzyloxycarbonyl-L-Val-L-Val-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Val-L-Val-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Boc-Phe-Ser-Arg-4-methylcoumarin-7-amide + H2O
?
show the reaction diagram
Boc-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Boc-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Boc-Val-Pro-Arg-4-methylcoumarin-7-amide + H2O
?
show the reaction diagram
Boc-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
Boc-Val-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Boc-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
collagen type IV + H2O
?
show the reaction diagram
-
-
-
?
D-Val-Leu-Arg-4-nitroanilide + H2O
D-Val-Leu-Arg + 4-nitroaniline
show the reaction diagram
native and recombinant enzyme
-
?
D-Val-Leu-Lys-4-nitroanilide + H2O
D-Val-Leu-Lys + 4-nitroaniline
show the reaction diagram
native and recombinant enzyme
-
?
Fibrinogen + H2O
?
show the reaction diagram
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
GDDSTPSILPAPRGYPGQV + H2O
GDDSTPSILPAPR + GYPGQV
show the reaction diagram
-
the tethered ligand is GYPGQV
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
?
GPNSKGRSLIGRLDTPYGGC + H2O
GPNSKGR + SLIGRLDTPYGC
show the reaction diagram
-
the tethered ligand is SLIGRL
-
-
?
GTNRSSKGRSLIGKVDGTSHVTGKGVT + H2O
GTNRSSKGR + SLIGKVDGTSHVTGKGVT
show the reaction diagram
-
the tethered ligand is SLIGKV
-
-
?
high-molecular weight kininogen + H2O
?
show the reaction diagram
-
-
-
?
L-Pro-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Pro-L-Phe-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
best substrate
-
-
?
LL-37 antimicrobial peptide + H2O
?
show the reaction diagram
-
i.e. LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
pro-kallikrein 1 + H2O
kallikrein 1
show the reaction diagram
-
-
-
-
?
pro-kallikrein 11 + H2O
kallikrein 11
show the reaction diagram
-
-
-
-
?
Pro-Phe-Arg-4-methylcoumaryl-7-amide
Pro-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
10% activity compared to tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
-
?
promeprin beta + H2O
meprin beta
show the reaction diagram
-
KLK8 activates promeprin beta
-
-
?
proteinase-activated receptor 2 peptide precursor + H2O
?
show the reaction diagram
-
the enzyme can unmask a PAR2 receptor-activating sequence from a peptide precursor
-
-
?
Rattus norvegicus proteinase-activated receptor 2 + H2O
?
show the reaction diagram
-
no activity witht the human proteinase-activated receptor 2
-
-
?
single-chain tissue-type plasminogen activator + H2O
two-chain tissue-type plasminogen activator
show the reaction diagram
specific cleavage of Arg275-Ile276 bond
-
-
?
t-butyloxycarbonyl-L-Leu-L-Lys-L-Arg-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-L-Leu-L-Lys-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
t-butyloxycarbonyl-L-Phe-L-Ser-L-Arg-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-L-Phe-L-Ser-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
t-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-L-Val-L-Leu-L-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
t-butyloxycarbonyl-L-Val-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-L-Val-L-Pro-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
tert-butyloxycarbonyl-Ala-Gly-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Ala-Gly-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
recombinant, not native, enzyme
-
?
tert-butyloxycarbonyl-Asp(benzyloxy)-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Asp(benzyloxy)-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
wild-type and mutants
-
?
tert-butyloxycarbonyl-Asp-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Asp-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
recombinant, not native, enzyme
-
?
tert-butyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
11% activity compared to tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
-
?
tert-butyloxycarbonyl-Gln-Arg-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Gln-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
5.0% activity compared to tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
-
?
tert-butyloxycarbonyl-Gln-Gly-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Gln-Gly-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
1.4% activity compared to tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
-
?
tert-butyloxycarbonyl-Glu-Gly-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Glu-Gly-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
tert-butyloxycarbonyl-Glu-Lys-Lys-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Glu-Lys-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
tert-butyloxycarbonyl-Leu-Arg-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Leu-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
tert-butyloxycarbonyl-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Leu-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
4.9% activity compared to tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
-
?
tert-butyloxycarbonyl-Leu-Lys-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Leu-Lys-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
3.9% activity compared to tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
-
?
tert-butyloxycarbonyl-Leu-Thr-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Leu-Thr-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
4.2% activity compared to tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
-
?
tert-butyloxycarbonyl-pyroglutamyl-Gly-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-pyroglutamyl-Gly-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
recombinant and native enzyme
-
?
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
3.8% activity compared to tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
100% activity
-
-
?
tosyl-Gly-L-Pro-L-Lys-7-amido-4-methylcoumarin + H2O
tosyl-Gly-L-Pro-L-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
ratio kcat/KM-value is 670 M/s
-
-
?
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
1.0% activity compared to tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Fibronectin + H2O
?
show the reaction diagram
-
affects cell adhesion or cell migration by modulating the content and/or chemical characteristics of fibronectin in the extracellular matrix
-
-
?
LL-37 antimicrobial peptide + H2O
?
show the reaction diagram
-
i.e. LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
pro-kallikrein 1 + H2O
kallikrein 1
show the reaction diagram
-
-
-
-
?
pro-kallikrein 11 + H2O
kallikrein 11
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
1.7fold stimulation
additional information
-
KLK8 is not influenced by Na+ and K+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(4-amidinohenyl)methanesulfonyl 1-fluoride
61% inhibition at 1 mM
1-(3,5-difluorophenyl)-5-hydroxy-7-(4-hydroxy-3,5-dimethoxyphenyl)-6,7-dihydro-1H-pyrrolo[3,2-b] pyridine-3-carboxylic acid
-
i.e. ZINC61720639
2-[[5-(2-chlorophenyl)-4-imino-3-methyl-4,5-dihydro-1H-pyrazolo[3,4-d]pyrimidin-6-yl]sulfanyl]-N-(2,5-dimethoxyphenyl)acetamide
-
-
4,4'-[pentane-1,5-diylbis(oxy)]bis(3,5-dibromobenzenecarboximidamide)
-
-
4-amino-N3-[(2R)-1-(tert-butylamino)-1-oxopropan-2-yl]-N3-(3-chloro-4-fluorophenyl)-2H-pyrrole-3,5-dicarboxamide
-
-
alpha2-antiplasmin
-
-
-
antipain
Aprotinin
benzamidine
chymostatin
diisopropyl fluorophosphate
2 mM, 100% inhibition
diisopropylfluorophosphate
16% inhibition at 0.1 mM
human alpha1-antichymotrypsin
weak, 16% inhibition at 2 mM
-
human alpha1-antitrypsin
weak, 20% inhibition at 10 mM
-
leupeptin
murinoglobulin I
-
24% inhibition at enzyme-inhibitor ratio of 1:2; formation of a SDS-stable complex; i.e. MUG I
-
N-(7-amino-1-chloro-2-oxoheptan-3-yl)-4-methylbenzenesulfonamide
-
-
N-[[5-([2-[(4-bromo-2-fluorophenyl)amino]-2-oxoethyl]sulfanyl)-4-methyl-4H-1,2,4-triazol-3-yl]methyl]furan-2-carboxamide
-
-
Ni2+
50% inhibition at 0.011 mM
NP STOP
-
neuropsin-specific inhibitor. Single stimulus in S1 during application of NP STOP completely eliminates the late associativity between S0 and S1 synapses. When a strong (four) stimulus in S0 is followed by the application of NP STOP, the late associativity between S0 and S1 synapses is not eliminated
-
pefabloc
-
-
phenylmethylsulfonyl fluoride
-
-
Protein C inhibitor
-
-
-
serine protease inhibitor-3
-
formation of a SDS-stable complex, bimolecular kinetics; from pyramidal neurons; slowly and tightly binding inhibitor
-
serpinB6
-
shRNA
-
inhibition of endogenous KLK8 expression, reduces cancer cell invasiveness
-
trans-epoxysuccinyl-L-leucylamido(4-guanidinobutane)
i.e. E-64, 15% inhibition at 0.1 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12-O-tetradecanoylphorbol-13-acetate
-
upregulates Klk8 mRNA 5fold
kallikrein 5
-
-
-
lysyl endopeptidase
-
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4312
benzyloxycarbonyl-Gly-Gly-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
0.07
benzyloxycarbonyl-L-Val-L-Val-L-Arg-7-amido-4-methylcoumarin
37C, pH 8.0
0.23 - 0.28
D-Val-Leu-Arg-4-nitroanilide
0.07
L-Pro-L-Phe-L-Arg-7-amido-4-methylcoumarin
37C, pH 8.0
8.36
Pro-Phe-Arg-4-methylcoumaryl-7-amide
-
recombinant wild-type enzyme, pH 8.0, 25C
0.1533
Pro-Phe-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
0.1
t-butyloxycarbonyl-L-Leu-L-Lys-L-Arg-7-amido-4-methylcoumarin
37C, pH 8.0
0.07
t-butyloxycarbonyl-L-Phe-L-Ser-L-Arg-7-amido-4-methylcoumarin
37C, pH 8.0
0.1
t-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin
37C, pH 8.0
0.07
t-butyloxycarbonyl-L-Val-L-Pro-L-Arg-7-amido-4-methylcoumarin
37C, pH 8.0
0.32
tert-butyloxycarbonyl-Asp(benzyloxy)-Pro-Arg-4-methylcoumaryl-7-amide
-
recombinant wild-type enzyme, pH 8.0, 25C
0.34
tert-butyloxycarbonyl-Asp-Pro-Arg-4-methylcoumaryl-7-amide
recombinant enzyme, pH 8.0, 37C
0.1844
tert-butyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
0.2247
tert-butyloxycarbonyl-Gln-Arg-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
0.3699
tert-butyloxycarbonyl-Gln-Gly-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
0.1165
tert-butyloxycarbonyl-Leu-Arg-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
0.1407
tert-butyloxycarbonyl-Leu-Lys-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
0.22 - 0.54
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide
0.2983
tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
0.3326
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
0.27 - 0.3
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
0.0238
tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
0.6897
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.49
benzyloxycarbonyl-Gly-Gly-Arg-7-amido-4-methylcoumarin
Homo sapiens
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
140
benzyloxycarbonyl-L-Val-L-Val-L-Arg-7-amido-4-methylcoumarin
Homo sapiens
O60259
37C, pH 8.0
180
L-Pro-L-Phe-L-Arg-7-amido-4-methylcoumarin
Homo sapiens
O60259
37C, pH 8.0
193
Pro-Phe-Arg-4-methylcoumaryl-7-amide
Mus musculus
-
recombinant wild-type enzyme, pH 8.0, 25C
4.45
Pro-Phe-Arg-7-amido-4-methylcoumarin
Homo sapiens
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
65
t-butyloxycarbonyl-L-Leu-L-Lys-L-Arg-7-amido-4-methylcoumarin
Homo sapiens
O60259
37C, pH 8.0
40
t-butyloxycarbonyl-L-Phe-L-Ser-L-Arg-7-amido-4-methylcoumarin
Homo sapiens
O60259
37C, pH 8.0
48
t-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin
Homo sapiens
O60259
37C, pH 8.0
98
t-butyloxycarbonyl-L-Val-L-Pro-L-Arg-7-amido-4-methylcoumarin
Homo sapiens
O60259
37C, pH 8.0
31.3
tert-butyloxycarbonyl-Asp(benzyloxy)-Pro-Arg-4-methylcoumaryl-7-amide
Mus musculus
-
recombinant wild-type enzyme, pH 8.0, 25C
5.75
tert-butyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin
Homo sapiens
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
3.39
tert-butyloxycarbonyl-Gln-Arg-Arg-7-amido-4-methylcoumarin
Homo sapiens
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
1.43
tert-butyloxycarbonyl-Gln-Gly-Arg-7-amido-4-methylcoumarin
Homo sapiens
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
1.62
tert-butyloxycarbonyl-Leu-Arg-Arg-7-amido-4-methylcoumarin
Homo sapiens
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
1.56
tert-butyloxycarbonyl-Leu-Lys-Arg-7-amido-4-methylcoumarin
Homo sapiens
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
34.8
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide
Mus musculus
-
recombinant wild-type enzyme, pH 8.0, 25C
3.57
tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin
Homo sapiens
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
9.64
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
Homo sapiens
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
100
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
Mus musculus
-
recombinant wild-type enzyme, pH 8.0, 25C
6.76
tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
Homo sapiens
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
2.11
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
Homo sapiens
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.45
benzyloxycarbonyl-Gly-Gly-Arg-7-amido-4-methylcoumarin
Homo sapiens
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
9766
29.02
Pro-Phe-Arg-7-amido-4-methylcoumarin
Homo sapiens
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
5274
31.2
tert-butyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin
Homo sapiens
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
37354
15.1
tert-butyloxycarbonyl-Gln-Arg-Arg-7-amido-4-methylcoumarin
Homo sapiens
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
41920
3.85
tert-butyloxycarbonyl-Gln-Gly-Arg-7-amido-4-methylcoumarin
Homo sapiens
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
41921
13.91
tert-butyloxycarbonyl-Leu-Arg-Arg-7-amido-4-methylcoumarin
Homo sapiens
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
9767
11.12
tert-butyloxycarbonyl-Leu-Lys-Arg-7-amido-4-methylcoumarin
Homo sapiens
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
9918
11.96
tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin
Homo sapiens
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
11334
10.93
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
Homo sapiens
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
2521
283.4
tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
Homo sapiens
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
9920
3.05
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
Homo sapiens
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37C
2114
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0008
serine protease inhibitor-3
-
complex formation, pH 7.4, 37C
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.23
purified native enzyme, substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
6.26
purified recombinant enzyme, substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
8.2
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
no detectable activity below
7 - 9
-
-
7.4 - 10
more than 50% of maximum activity within this range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
expression in embryo brain samples
Manually annotated by BRENDA team
-
epithelial ovarian tumor
Manually annotated by BRENDA team
-
epidermis, keratinocytes
Manually annotated by BRENDA team
-
in the hippocampal CA1-CA3 subfields
Manually annotated by BRENDA team
-
oligodendrocytes only express Klk8 mRNA after injury to the central nervous system
Manually annotated by BRENDA team
-
epithelial ovarian tumor
Manually annotated by BRENDA team
-
low activity in nonpregnant uteri, increased activity in pregnant uteri, highest at midgestational period
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
KRP/hK8 is nuclear in glial cells of the brain, in myoepithelial cells of the submandibular gland and in the adenocarcinoma
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10000
-
x * 10000 + x * 18000, SDS-PAGE
18000
-
x * 10000 + x * 18000, SDS-PAGE
26000
1 * 26000, non-reducing SDS-PAGE
26600
recombinant enzyme, MALDI-TOF MS
28520
-
precursor, calculated from sequence of cDNA
29000
recombinant enzyme, gel filtration
30000
x * 30000, SDS-PAGE
31500
x * 31500, SDS-PAGE of active recombinant enzyme
32000
1 * 32000, reducing SDS-PAGE
35000
-
immunoblotting
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 26000, non-reducing SDS-PAGE; 1 * 32000, reducing SDS-PAGE
additional information
-
determination of loop structure and organization
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, recombinant enzyme, protein solution: 24.5 mg/ml, 5 mM HEPES, pH 7.4, 100 mM NaCl, 4C, precipitant with PEG, X-ray diffraction structure determination and analysis
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
KLK8 displays 2.5fold higher activity in 100 mM sodium phosphate buffer than in 50 mM Tris-HCl buffer
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Tween-20
-
KLK8 shows 1.25-fold higher activity when 0.01% Tween-20 is added as a carrier in the reaction mix
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 0.01 M acetic acid containing 250 mM NaCl, pH 4.76, 1 month, no loss of activity
-
-20C, active recombinant enzyme, stable for at least two months
-80C, 0.01 M acetic acid containing 250 mM NaCl, pH 4.76, 12 months, no loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1100fold from brain; recombinant from SF21 insect cells
recombinant from SF21 insect cells
-
recombinant from SF9 insect cells
-
Sepharose column chromatography and Source15S column chromatography and Superdex 200 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis
-
expressed in Pichia pastoris strain GS115
-
expression and secretion of wild-type and mutants from Neuro2a cells
-
gene KLK6, genetic organization and structure of the kallikrein gene family, clustered on chromosome 19q13.3-q13.4; gene KLK8, genetic organization and structure of the kallikrein gene family, clustered on chromosome 19q13.3-q13.4
into the expression cosmid cassette pAxCAwt as a transfer vector for adenovirus preparation, transfection into primary keratinocyte cultures from the skin of Klk8-/- mice
-
KLK8 splice variants K8-2 and K8-R amplified and inserted into the pLNCX retroviral vector, CL1-5 cells transfected with each KLK8 splice variant. Expression of hK8 in s.c. tumors in SCID mice by injection of SCID mice s.c. with CL1-5/K8-2 or CL1-5/K8-R cells
-
overexpression of proneuropsin in Spodoptera frugiperda insect cells via baculovirus infection
-
recombinant KLK 8 type II is expressed using the baculovirus insect cell system
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
KLK8 expression is increased 4fold in cell lines with overexpressing urinary type plasminogen activator and receptor versus cell lines with silencing of urinary type plasminogen activator and receptor
KLK8 protein expression increases during terminal keratinocyte differentiation
-
neuropsin is upregulated in the epidermis of sodium lauryl sulfate-treated mouse skin
-
oligodendrocytes only express Klk8 mRNA after injury to the central nervous system
-
skin inflammation increases KLK8/neuropsin expression in the stratum spinosum
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
enzyme expression in epithelial ovarian tumors correlates significantly with favorable patient survival. Use of enzyme as a prognostic marker in patients with ovarian cancer
C108S
-
oligonucleotide-directed mutagenesis, reduced Km, increased kcat, increased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
C145S
-
oligonucleotide-directed mutagenesis of disulfide bond SS3, reduced Km and kcat, increased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
C208S
-
oligonucleotide-directed mutagenesis of disulfide bond SS6, highly reduced Km and reduced kcat, increased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
C233S
-
oligonucleotide-directed mutagenesis, highly reduced Km and slightly reduced kcat, reduced activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
C246S
-
oligonucleotide-directed mutagenesis, reduced Km and kcat, decreased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
C39S
-
oligonucleotide-directed mutagenesis of disulfide bond SS1, increased Km, reduced kcat, reduced activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
C7S
-
oligonucleotide-directed mutagenesis, reduced Km and kcat, slightly decreased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
D206V
-
oligonucleotide-directed mutagenesis, reduced Km and highly reduced kcat, decreased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-7-amino-4-methylcoumarin
N110A
-
oligonucleotide-directed mutagenesis, reduced Km and kcat, slightly increased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
-
enzyme might contribute to the remodeling of extracellular components after decidualization
medicine
molecular biology
-
miRNAs play a role in the regulation of KLK expression: using a bioinformatics approach 96 strong KLK/miRNA interactions are identified. KLK10 is the most frequently targeted kallikrein, followed by KLK5 and KLK13. KLK1, KLK3, KLK8 and KLK12 do not have strongly predicted miRNA/KLK interactions
pharmacology
-
enzyme is a drug target in the treatment of epilepsy
additional information
-
the type II form (longer form) of neuropsin is only expressed in the central nervous system of human. Its origin is less than 5 million years ago. The occurrence of the type II form in human is caused by a human-specific mutation near the novel splicing site. It persists a molecular mechanism for the creation of novel proteins through alternative splicing in the central nervous system during human evolution. Potential importance of the creation of novel splicing forms in the central nervous system in the emergence of human cognition