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Information on EC 3.4.21.118 - kallikrein 8 and Organism(s) Mus musculus and UniProt Accession P07628
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3.4.21.118 kallikrein 8Specify your search results
Word Map
- 3.4.21.118
- kallikreins
- klk8
- melanopsin
-
desquamation
-
photopigment
-
iprgcs
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non-visual
-
peropsin
- medicine
- biotechnology
- molecular biology
- pharmacology
- analysis
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys
Synonyms
neuropsin, kallikrein-related peptidase, kallikrein-8, kallikrein 8, tadg-14, kallikrein-related peptidase 8, tadg14, rgk-8, type ii neuropsin, brain serine protease 1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
kallikrein-8
KLK8
neuropsin
S01.244
-
-
-
-
kallikrein-8
-
-
-
-
neuropsin
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
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
cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys
enzyme is a trypsin-type serine protease
cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys
enzyme is a trypsin-type serine protease
-
cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys
enzyme is a trypsin-type serine protease
cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys
enzyme is a trypsin-type serine protease
-
cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys
enzyme is a trypsin-type serine protease
cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys
substrate binding site structure defining the specificity for Arg and Lys in the S1 pocket
cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys
the ordered kallikrein loop projects proline towards the active site to restrict smaller residues or proline at the P2 position of substrates
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
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-
-
-
CAS REGISTRY NUMBER
COMMENTARY
171715-15-4
-
9001-01-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-Val-Leu-Arg-4-nitroanilide + H2O
D-Val-Leu-Arg + 4-nitroaniline
native and recombinant enzyme
-
?
D-Val-Leu-Lys-4-nitroanilide + H2O
D-Val-Leu-Lys + 4-nitroaniline
native and recombinant enzyme
-
?
Pro-Phe-Arg-4-methylcoumaryl-7-amide
Pro-Phe-Arg + 7-amino-4-methylcoumarin
recombinant wild-type and mutants
-
?
tert-butyloxycarbonyl-Ala-Gly-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Ala-Gly-Pro-Arg + 7-amino-4-methylcoumarin
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
wild-type and mutants
-
?
tert-butyloxycarbonyl-Asp-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Asp-Pro-Arg + 7-amino-4-methylcoumarin
recombinant, not native, enzyme
-
?
tert-butyloxycarbonyl-Glu-Gly-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Glu-Gly-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-Glu-Lys-Lys-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Glu-Lys-Lys + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-Leu-Arg-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Leu-Arg-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-Leu-Thr-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Leu-Thr-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-pyroglutamyl-Gly-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-pyroglutamyl-Gly-Arg + 7-amino-4-methylcoumarin
recombinant and native enzyme
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
acetyl-Pro-Phe-Arg-4-nitroanilide + H2O
acetyl-Pro-Phe-Arg + 4-nitroaniline
low activity
-
?
acetyl-Pro-Phe-Arg-4-nitroanilide + H2O
acetyl-Pro-Phe-Arg + 4-nitroaniline
recombinant, not native enzyme
-
?
Fibronectin + H2O
?
affects cell adhesion or cell migration by modulating the content and/or chemical characteristics of fibronectin in the extracellular matrix
-
-
?
polypeptide + H2O
peptides
enzyme has significant limbic effects by changing the extracellular matrix environment
-
?
polypeptide + H2O
peptides
enzyme is implicated in various neurological processes including formation of memory
-
?
tert-butyloxycarbonyl-Glu-Gly-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Glu-Gly-Arg + 7-amino-4-methylcoumarin
native and recombinant enzyme
-
?
tert-butyloxycarbonyl-Glu-Gly-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Glu-Gly-Arg + 7-amino-4-methylcoumarin
recombinant, not native, enzyme
-
?
tert-butyloxycarbonyl-Glu-Lys-Lys-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Glu-Lys-Lys + 7-amino-4-methylcoumarin
low activity
-
?
tert-butyloxycarbonyl-Glu-Lys-Lys-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Glu-Lys-Lys + 7-amino-4-methylcoumarin
recombinant and native enzyme
-
?
tert-butyloxycarbonyl-Leu-Arg-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Leu-Arg-Arg + 7-amino-4-methylcoumarin
low activity
-
?
tert-butyloxycarbonyl-Leu-Arg-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Leu-Arg-Arg + 7-amino-4-methylcoumarin
recombinant, not native, enzyme
-
?
tert-butyloxycarbonyl-Leu-Thr-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Leu-Thr-Arg + 7-amino-4-methylcoumarin
low activity
-
?
tert-butyloxycarbonyl-Leu-Thr-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Leu-Thr-Arg + 7-amino-4-methylcoumarin
recombinant, not native, enzyme
-
?
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
native and recombinant enzyme
-
?
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
recombinant wild-type and mutants
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
best substrate
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
best substrate
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
native and recombinant enzyme
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
recombinant wild-type and mutants
-
?
additional information
?
-
recombinant enzyme is produced as inactive proform and needs to be processed by an endoprotease, e.g. protease-1, EC 3.4.21.50, or trypsin, EC 3.4.21.4, for activation by specific cleavage of the Lys32-Ile33 bond near the N-terminus
-
-
?
additional information
?
-
-
recombinant enzyme is produced as inactive proform and needs to be processed by an endoprotease, e.g. protease-1, EC 3.4.21.50, or trypsin, EC 3.4.21.4, for activation by specific cleavage of the Lys32-Ile33 bond near the N-terminus
-
-
?
additional information
?
-
recombinant enzyme is produced as inactive proform and needs to be processed by an endoprotease, e.g. protease-1, EC 3.4.21.50, or trypsin, EC 3.4.21.4, for activation by specific cleavage of the Lys32-Ile33 bond near the N-terminus
-
-
?
additional information
?
-
-
recombinant enzyme is produced as inactive proform and needs to be processed by an endoprotease, e.g. protease-1, EC 3.4.21.50, or trypsin, EC 3.4.21.4, for activation by specific cleavage of the Lys32-Ile33 bond near the N-terminus
-
-
?
additional information
?
-
loop C and the N-linked oligosaccharide chain on the kallikrein loop affect the catalytic efficiency and P2 specificity, respectively
-
-
?
additional information
?
-
-
loop C and the N-linked oligosaccharide chain on the kallikrein loop affect the catalytic efficiency and P2 specificity, respectively
-
-
?
additional information
?
-
substrate specificty of native and recombinant enzyme
-
-
?
additional information
?
-
-
substrate specificty of native and recombinant enzyme
-
-
?
additional information
?
-
disulfide bonds SS1 in loop E, Gly142-Leu155, and SS6 in loop G, Ser185-Gly197, are essential for catalytic activity
-
-
?
additional information
?
-
-
disulfide bonds SS1 in loop E, Gly142-Leu155, and SS6 in loop G, Ser185-Gly197, are essential for catalytic activity
-
-
?
additional information
?
-
-
enzyme is involved in the synaptogenesis/maturation of orphan and small synaptic boutons in the Schaffer-collateral pathway
-
-
?
additional information
?
-
-
enzyme is necessary for establishment of long-term potentiation and has a significant role in memory acquisition
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Fibronectin + H2O
?
affects cell adhesion or cell migration by modulating the content and/or chemical characteristics of fibronectin in the extracellular matrix
-
-
?
polypeptide + H2O
peptides
enzyme has significant limbic effects by changing the extracellular matrix environment
-
?
polypeptide + H2O
peptides
enzyme is implicated in various neurological processes including formation of memory
-
?
additional information
?
-
-
enzyme is involved in the synaptogenesis/maturation of orphan and small synaptic boutons in the Schaffer-collateral pathway
-
-
?
additional information
?
-
-
enzyme is necessary for establishment of long-term potentiation and has a significant role in memory acquisition
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
trans-epoxysuccinyl-L-leucylamido(4-guanidinobutane)
i.e. E-64, 15% inhibition at 0.1 mM
serine protease inhibitor-3
formation of a SDS-stable complex, bimolecular kinetics
-
additional information
no or very slight inhibition by pepstatin A, trypsin inhibitor, Ca2+, Mg2+, and metal chelators
-
additional information
-
no or very slight inhibition by pepstatin A, trypsin inhibitor, Ca2+, Mg2+, and metal chelators
-
additional information
enzyme is strongly inhibited by low molecular weight protease inhibitors that bind to His and Ser residues in the active center of serine proteases
-
additional information
-
enzyme is strongly inhibited by low molecular weight protease inhibitors that bind to His and Ser residues in the active center of serine proteases
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
enzyme is induced and activated by uterine decidualization
-
additional information
-
enzyme is induced and activated by uterine decidualization
-
additional information
-
single tetanus evokes a neuropsin-dependent form that follows downstream signaling into integrin/actin signal and L-type voltage-dependent Ca2+ channel pathway. A neuropsin-independent form of synaptic capture is evoked by a stronger (two) tetanus
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.36
Pro-Phe-Arg-4-methylcoumaryl-7-amide
recombinant wild-type enzyme, pH 8.0, 25°C
0.32
tert-butyloxycarbonyl-Asp(benzyloxy)-Pro-Arg-4-methylcoumaryl-7-amide
recombinant wild-type enzyme, pH 8.0, 25°C
0.34
tert-butyloxycarbonyl-Asp-Pro-Arg-4-methylcoumaryl-7-amide
recombinant enzyme, pH 8.0, 37°C
0.22
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide
recombinant wild-type enzyme, pH 8.0, 25°C
0.5
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide
recombinant enzyme, pH 8.0, 37°C
0.54
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide
native enzyme, pH 8.0, 37°C
0.27
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
recombinant enzyme, pH 8.0, 37°C
0.28
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
recombinant wild-type enzyme, pH 8.0, 25°C
0.3
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
native enzyme, pH 8.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
193
Pro-Phe-Arg-4-methylcoumaryl-7-amide
recombinant wild-type enzyme, pH 8.0, 25°C
31.3
tert-butyloxycarbonyl-Asp(benzyloxy)-Pro-Arg-4-methylcoumaryl-7-amide
recombinant wild-type enzyme, pH 8.0, 25°C
34.8
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide
recombinant wild-type enzyme, pH 8.0, 25°C
100
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
recombinant wild-type enzyme, pH 8.0, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
oligodendrocytes only express Klk8 mRNA after injury to the central nervous system
low activity in nonpregnant uteri, increased activity in pregnant uteri, highest at midgestational period
-
the epidermis of the skin is one of the tissues that exhibits a high level of KLK8 expression
-
interaction between murine serpinB6 and mK8 is at least 10fold faster than that observed for serpinB6 and hK8
expression of Klk8 in the imiquimod-treated skin is significantly higher than that in untreated skin
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
disruption of loop C and the kallikrein loop enhances the regulated secretion, no loop disruption does lead to inhibition of secretion
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
hyperkeratosis and acanthosis in sodium lauryl sulfate-stimulated skin are markedly inhibited in neuropsin knockout mice. Knockdown of KLK8/neuropsin decreases keratin 10 expression
physiological function
physiological function
-
in the hippocampus, Klk8 is involved in activity-dependent synaptic changes such as long-term potentiation. Klk8 is involved in tissue development and rearrangement in the skin
physiological function
function of kallikrein 8 in regulating the expression of microtubule associated dendrite growth marker microtubule-associated protein (MAP2)c, dendrite architecture and protein kinase A (PKA)-CREB signaling. Knockdown of KLK8 via siRNA transfection in mouse primary hippocampal neurons or via intra-hippocampal administration of KLK8 antisense oligonucleotides in vivo reduces expression of MAP2c, dendrite length, dendrite branching and spine density. The KLK8-mediated MAP2c deficiency in turn inactivates protein kinase A, and downstream transcription factor phosphorylates CREB, leading to downregulation of memory-linked genes and consequent impaired memory consolidation
physiological function
no statistically significant difference is observed in the number of Ki-67-positive keratinocytes between wild-type and Klk8 knockout mice, nor is epidermal thickness affected in Klk8 knockout mice. Topical application of imiquimod on the ear of wild-type mice results in increased ear thickness, which is significantly reduced in Klk8 knockout mice from day 5 post-treatment. The reduced ear swelling is mostly due to the decrease in dermal inflammatory cell infiltration and oedema rather than epidermal acanthosis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
glycoprotein
enzyme has a putative N-glycoslyation site at Asn95 of the kallikrein loop
glycoprotein
N-glycosylated at the kallikrein loop, residues His91-Ile103, oligosacchride chain is essential for activity
proteolytic modification
recombinant enzyme is produced as inactive proform and needs to be processed by an endoprotease, e.g. protease-1, EC 3.4.21.50, or trypsin, EC 3.4.21.4, for activation by specific cleavage of the Lys32-Ile33 bond near the N-terminus
proteolytic modification
-
recombinant enzyme is produced as inactive proform and needs to be processed by an endoprotease, e.g. protease-1, EC 3.4.21.50, or trypsin, EC 3.4.21.4, for activation by specific cleavage of the Lys32-Ile33 bond near the N-terminus
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
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
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
additional deletion N113-E115 in mutant N110S: decreased kcat and Km, increased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
additional information
-
additional deletion N113-E115 in mutant N110S: decreased kcat and Km, increased activity with substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
additional information
-
enzyme knock-out mice are significantly impaired in the Morris water maze and Y-mazes and fail to exhibit early phase long-term potentiation by a single tetanus. A dose of recombinant enzyme alone, without tetanic stimulation, elicits either long-lasting potentiation or depression, depending on the dose, by increase of phosphorylation at different sites on the GluR1 subunit of the AMPA receptor
additional information
-
enzyme-deficient mouse, number of L1-immunoreactive boutons is markedly higher than in wild-type, their number reverts to wild-type level upon microinjection of enzyme. L1-immunoreactive boutons are hypertrophied in the mutant
additional information
-
Klk8-/- mice, show less proliferation and an increase in the number of cell layers in the stratum corneum. Inefficient cleavage of adhesion molecules DSG1 and CDSN in Klk8-/- skin, which contributes to a delay in corneocyte shedding, resulting in hyperkeratosis phenotype
additional information
-
neuropsin-deficient mice, are significantly impaired in hippocampus-dependent behavioral memory. Synaptic late associativity is impaired
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant from SF21 insect cells
recombinant from SF9 insect cells
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into the expression cosmid cassette pAxCAwt as a transfer vector for adenovirus preparation, transfection into primary keratinocyte cultures from the skin of Klk8-/- mice
-
overexpression of proneuropsin in Spodoptera frugiperda insect cells via baculovirus infection
overexpression of proneuropsin in Spodoptera frugiperda insect cells via baculovirus infection
overexpression of proneuropsin in Spodoptera frugiperda insect cells via baculovirus infection
-
overexpression of proneuropsin in Spodoptera frugiperda insect cells via baculovirus infection
overexpression of proneuropsin in Spodoptera frugiperda insect cells via baculovirus infection
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of Klk8 in the imiquimod-treated skin is significantly higher than that in untreated skin
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
-
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
enzyme might contribute to the remodeling of extracellular components after decidualization
medicine
medicine
-
in psoriatic lesion, KLK8 modulates hyperproliferation and prevents excessive hyperkeratosis by shedding the corneocytes
medicine
-
occurrence of two synaptic capture mechanisms for a weakly stimulated synapse to acquire persistency (i.e., neuropsin dependent and independent). Neuropsin-dependent late associativity may serve in the acquisition of nonaversive memory (e.g., inquisitive behavior)
medicine
imiquimod-treated skin of wild-type mice shows characteristic neutrophil microabscess formation in the epidermis, which is markedly reduced in Klk8 knockout mice. Klk8 is crucial for microabscess formation in the upper epidermis, where Klk8 is significantly involved in IL-36 expression
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JOURNAL
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ORGANISM (UNIPROT)
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Boeckmann, B.; Bairoch, A.; Apweiler, R.; Blatter, M.C.; Estreicher, A.; Gasteiger, E.; Martin M.J.; Michoud, K.; O'Donovan, C.; Phan, I.; Pilbout, S.; Schneider, M.
The SWISS-PROT protein knowledgebase and its supplement TrEMBL
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Homo sapiens (O60259), Mus musculus (P07628), Mus musculus (Q61955), Rattus norvegicus (O88780), Rattus norvegicus (P36374)
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Crystallization and preliminary X-ray analysis of neuropsin, a serine protease expressed in the limbic system of mouse brain
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1997
Mus musculus (Q61955), Mus musculus
Yoshida, S.; Taniguchi, M.; Hirata, A.; Shiosaka, S.
Sequence analysis and expression of human neuropsin cDNA and gene
Gene
213
9-16
1998
Homo sapiens (O60259), Homo sapiens, Mus musculus (Q61955), Mus musculus
Shimizu, C.; Yoshida, S.; Shibata, M.; Kato, K.; Momota, Y.; Matsumoto, K.; Shiosaka, T.; Midorikawa, R.; Kamachi, T.; Kawabe, A.; Shiosaka, S.
Characterization of recombinant and brain neuropsin, a plasticity-related serine protease
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Mus musculus (Q61955), Mus musculus
Kishi, T.; Kato, M.; Shimizu, T.; Kato, K.; Matsumoto, K.; Yoshida, S.; Shiosaka, S.; Hakoshima, T.
Crystal structure of neuropsin, a hippocampal protease involved in kindling epileptogenesis
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274
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Mus musculus (Q61955), Mus musculus
Tani, N.; Matsumoto, K.; Ota, I.; Yoshida, S.; Takada, Y.; Shiosaka, S.; Matsuura, N.
Effects of fibronectin cleaved by neuropsin on cell adhesion and migration
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39
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Mus musculus (Q61955), Mus musculus
Kato, K.; Kishi, T.; Kamachi, T.; Akisada, M.; Oka, T.; Midorikawa, R.; Takio, K.; Dohmae, N.; Bird, P.I.; Sun, J.; Scott, F.; Miyake, Y.; Yamamoto, K.; Machida, A.; Tanaka, T.; Matsumoto, K.; Shibata, M.; Shiosaka, S.
Serine proteinase inhibitor 3 and murinoglobulin I are potent inhibitors of neuropsin in adult mouse brain
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276
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Mus musculus (Q61955), Mus musculus
Oka, T.; Hakoshima, T.; Itakura, M.; Yamamori, S.; Takahashi, M.; Hashimoto, Y.; Shiosaka, S.; Kato, K.
Role of loop structures of neuropsin in the activity of serine protease and regulated secretion
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277
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2002
Mus musculus (Q61955), Mus musculus
Matsumoto-Miyai, K.; Kitagawa, R.; Ninomiya, A.; Momota, Y.; Yoshida, S.; Shiosaka, S.
Decidualization induces the expression and activation of an extracellular protease neuropsin in mouse uterus
Biol. Reprod.
67
1414-1418
2002
Mus musculus (Q61955), Mus musculus
Chen, Z.L.; Yoshida, S.; Kato, K.; Momota, Y.; Suzuki, J.; Tanaka, T.; Ito, J.; Nishino, H.; Aimoto, S.; Kiyama, H.; Shiosaka, S.
Expression and activity-dependent changes of a novel limbic-serine protease gene in the hippocampus
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15
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1995
Mus musculus (Q61955), Mus musculus
Nakamura, Y.; Tamura, H.; Horinouchi, K.; Shiosaka, S.
Role of neuropsin in formation and maturation of Schaffer-collateral L1cam-immunoreactive synaptic boutons
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119
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Mus musculus
Tamura, H.; Ishikawa, Y.; Hino, N.; Maeda, M.; Yoshida, S.; Kaku, S.; Shiosaka, S.
Neuropsin is essential for early processes of memory acquisition and Schaffer collateral long-term potentiation in adult mouse hippocampus in vivo
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570
541-551
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Mus musculus
Scott, F.L.; Sun, J.; Whisstock, J.C.; Kato, K.; Bird, P.I.
SerpinB6 is an inhibitor of kallikrein-8 in keratinocytes
J. Biochem.
142
435-442
2007
Homo sapiens, Mus musculus
Kishibe, M.; Bando, Y.; Terayama, R.; Namikawa, K.; Takahashi, H.; Hashimoto, Y.; Ishida-Yamamoto, A.; Jiang, Y.P.; Mitrovic, B.; Perez, D.; Iizuka, H.; Yoshida, S.
Kallikrein 8 is involved in skin desquamation in cooperation with other kallikreins
J. Biol. Chem.
282
5834-5841
2007
Mus musculus, Mus musculus C57BL/6
Ishikawa, Y.; Horii, Y.; Tamura, H.; Shiosaka, S.
Neuropsin (KLK8)-dependent and -independent synaptic tagging in the Schaffer-collateral pathway of mouse hippocampus
J. Neurosci.
28
843-849
2008
Mus musculus
Pettus, J.R.; Johnson, J.J.; Shi, Z.; Davis, J.W.; Koblinski, J.; Ghosh, S.; Liu, Y.; Ravosa, M.J.; Frazier, S.; Stack, M.S.
Multiple kallikrein (KLK 5, 7, 8, and 10) expression in squamous cell carcinoma of the oral cavity
Histol. Histopathol.
24
197-207
2009
Homo sapiens, Mus musculus
Yoshida, S.
Klk8, a multifunctional protease in the brain and skin: analysis of knockout mice
Biol. Chem.
391
375-380
2010
Mus musculus
Shingaki, K.; Matsuzaki, S.; Taniguchi, M.; Kubo, T.; Fujiwara, T.; Yamamoto, A.; Tamura, H.; Maeda, T.; Ooi, K.; Matsumoto, K.; Shiosaka, S.; Tohyama, M.
Molecular mechanism of kallikrein-related peptidase 8/neuropsin-induced hyperkeratosis in inflamed skin
Br. J. Dermatol.
163
466-475
2010
Homo sapiens, Mus musculus
Iinuma, S.; Kishibe, M.; Saito, N.; Igawa, S.; Honma, M.; Takahashi, H.; Bando, Y.; Yoshida, S.; Iizuka, H.; Ishida-Yamamoto, A.
Klk8 is required for microabscess formation in a mouse imiquimod model of psoriasis
Exp. Dermatol.
24
887-889
2015
Mus musculus (Q61955)
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