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Information on EC 3.4.21.B39 - stratum corneum tryptic enzyme and Organism(s) Homo sapiens and UniProt Accession Q9Y337

for references in articles please use BRENDA:EC3.4.21.B39
preliminary BRENDA-supplied EC number
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.B39 stratum corneum tryptic enzyme
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Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: Q9Y337
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
proteolytic cleavage of polypeptides
Synonyms
GK-5, hK5, HSC tryptic enzyme, human kallikrein 5, human stratum corneum trypsin-like enzyme, human tissue kallikrein 5, K5, kallikrein 5, kallikrein protein 5, kallikrein-5, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
HSC tryptic enzyme
247
-
human kallikrein 5
247
-
human stratum corneum trypsin-like enzyme
273740
-
human tissue kallikrein 5
247
-
kallikrein 5
kallikrein protein 5
273740
-
kallikrein-5
247
-
kallikrein-like protein 2
247
-
kallikrein-related peptidase 5
273740
-
KLK-L2
247
-
S01.017
-
-
-
-
strateum-corneum trypsin-like serine protease
273740
-
stratum corneum tryptic enzyme
247
-
tissue kallikrein 5
additional information
247
the enzyme belongs to the human kallikrein, KLK, gene family
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
proteolytic cleavage of polypeptides
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
272788-46-2
-
9001-01-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Abz-APGRVVGGA-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
?
show the reaction diagram
-
-
-
-
?
D-Ile-Pro-Arg-p-nitroanilide + H2O
D-Ile-Pro-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
defensin-1alpha + H2O
?
show the reaction diagram
-
KLK5 is capable of processing defensin-1alpha and may be important in vaginal host defense
-
-
?
desmocollin-2 + H2O
?
show the reaction diagram
-
-
-
-
?
desmocollin-3 + H2O
?
show the reaction diagram
-
-
-
-
?
desmoglein protein 1 + H2O
?
show the reaction diagram
-
-
-
-
?
FSR-amido-4-methylcoumarin + H2O
FSR + 7-amino-4-methylcoumarin
show the reaction diagram
fluorogenic trypsin-like peptide substrate
-
-
?
human plasminogen + H2O
human plasmin + ?
show the reaction diagram
-
generation of a 29 kDa fragment
-
-
?
mucin 4 + H2O
?
show the reaction diagram
-
-
-
-
?
mucin 5B + H2O
?
show the reaction diagram
-
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
proform filaggrin + H2O
mature filaggrin + ?
show the reaction diagram
tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
best substrate
-
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
best substrate
-
-
?
VPR-amido-4-methylcoumarin + H2O
VPR + 7-amino-4-methylcoumarin
show the reaction diagram
fluorogenic trypsin-like peptide substrate
-
-
?
Abz-KLRSSKQ-EDDnp + H2O
?
show the reaction diagram
-
-
-
-
?
Ala-Thr-Pro-Lys-Ile-Phe-Asn + H2O
Ala-Thr-Pro-Lys + Ile-Phe-Asn
show the reaction diagram
-
moderate cleavage efficiency
-
-
?
Asp-Gly-Asp-Lys-Ile-Ile-Glu + H2O
Asp-Gly-Asp-Lys + Ile-Ile-Glu
show the reaction diagram
-
low cleavage efficiency
-
-
?
Asp-Thr-Arg-Ala-Ile-Gly + H2O
Asp-Thr-Arg + Ala-Ile-Gly
show the reaction diagram
-
moderate cleavage efficiency
-
-
?
Boc-Gln-Ala-Arg-7-amido-4-methyl-coumarin + H2O
Boc-Gln-Ala-Arg + 7-amino-4-methyl-coumarin
show the reaction diagram
-
-
-
-
?
Boc-Gln-Arg-Arg-7-amido-4-methyl-coumarin + H2O
Boc-Gln-Arg-Arg + 7-amino-4-methyl-coumarin
show the reaction diagram
-
-
-
-
?
Boc-Gln-Gly-Arg-7-amido-4-methyl-coumarin + H2O
Boc-Gln-Gly-Arg + 7-amino-4-methyl-coumarin
show the reaction diagram
-
-
-
-
?
Boc-Leu-Arg-Arg-7-amido-4-methyl-coumarin + H2O
Boc-Leu-Arg-Arg + 7-amino-4-methyl-coumarin
show the reaction diagram
-
-
-
-
?
Boc-Leu-GLy-Arg-7-amido-4-methylcoumarin + H2O
Boc-Leu-Gly-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Boc-Leu-Lys-Arg-7-amido-4-methyl-coumarin + H2O
Boc-Leu-Lys-Arg + 7-amino-4-methyl-coumarin
show the reaction diagram
-
-
-
-
?
Boc-Phe-Ser-Arg-7-amido-4-methyl-coumarin + H2O
Boc-Phe-Ser-Arg + 7-amino-4-methyl-coumarin
show the reaction diagram
-
-
-
-
?
Boc-Val-Leu-Lys-7-amido-4-methyl-coumarin + H2O
Boc-Val-Leu-Lys + 7-amino-4-methyl-coumarin
show the reaction diagram
-
-
-
-
?
Boc-Val-Pro-Arg-7-amido-4-methyl-coumarin + H2O
Boc-Val-Pro-Arg + 7-amino-4-methyl-coumarin
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
Cbz-L-Pro-Phe-Arg-p-nitroanilide + H2O
Cbz-L-Pro-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
desmocollin-3 + H2O
?
show the reaction diagram
-
-
-
-
?
desmoglein 1 + H2O
?
show the reaction diagram
-
-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
-
-
-
-
?
fibrinogen Aalpha chain + H2O
?
show the reaction diagram
-
cleavage after Arg348 and Arg407
-
-
?
fibrinogen Bbeta chain + H2O
?
show the reaction diagram
-
cleavage after Lys53 and Arg14
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Gln-Glu-Asp-Lys-Val-Leu-Gly + H2O
Gln-Glu-Asp-Lys + Val-Leu-Gly
show the reaction diagram
-
low cleavage efficiency
-
-
?
Gln-Gly-Asp-Lys-Ile-Ile-Asp + H2O
Gln-Gly-Asp-Lys + Ile-Ile-Asp
show the reaction diagram
-
low cleavage efficiency
-
-
?
Glu-Thr-Arg-Ile-Ile-Lys + H2O
Glu-Thr-Arg + Ile-Ile-Lys
show the reaction diagram
-
moderate cleavage efficiency
-
-
?
hK3 + H2O
?
show the reaction diagram
-
hK5 can inactivate hK3 by subsequent cleavage after activation
-
-
-
Ile-Gln-Ser-Arg-Ile-Val-Gly + H2O
Ile-Gln-Ser-Arg + Ile-Val-Gly
show the reaction diagram
-
high cleavage efficiency
-
-
?
Ile-Leu-Ser-Arg-Ile-Val
Ile-Leu-Ser-Arg + Ile-Val
show the reaction diagram
-
optimal substrate sequences for KLK5
-
-
-
Ile-Leu-Ser-Arg-Ile-Val-Gly + H2O
Ile-Leu-Ser-Arg + Ile-Val-Gly
show the reaction diagram
-
high cleavage efficiency
-
-
?
insulin-like growth factor-binding protein 1 + H2O
insulin-like growth factor-binding protein 1a + insulin-like growth factor-binding protein 1b
show the reaction diagram
-
cleavage after Lys137
-
-
?
insulin-like growth factor-binding protein 1 + H2O
insulin-like growth factor-binding protein 4a + insulin-like growth factor-binding protein 4b
show the reaction diagram
-
cleavage after Arg170
-
-
?
insulin-like growth factor-binding protein 2 + H2O
insulin-like growth factor-binding protein 2a + insulin-like growth factor-binding protein 2b
show the reaction diagram
-
cleavage after Arg164
-
-
?
insulin-like growth factor-binding protein 3 + H2O
insulin-like growth factor-binding protein 3a + insulin-like growth factor-binding protein 3b + insulin-like growth factor-binding protein 3c
show the reaction diagram
-
cleavage after Arg158 and Arg206
-
-
?
insulin-like growth factor-binding protein 5 + H2O
insulin-like growth factor-binding protein 5a + insulin-like growth factor-binding protein 5b + insulin-like growth factor-binding protein 5c
show the reaction diagram
-
cleavage after Arg123 and Arg212
-
-
?
kallikrein 7 + H2O
?
show the reaction diagram
-
Gln-Gly-Asp-Lys-/-Ile-Ile. KLK7 is activated at a low rate
-
-
?
kininogen + H2O
?
show the reaction diagram
-
cleavage after Arg222, Arg252 and Arg374
-
-
?
L-Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
L-Pro-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N(p-tosyl)-Arg-Gly-Val 4-nitroanilide
?
show the reaction diagram
-
-
-
-
?
plasminogen + H2O
?
show the reaction diagram
-
cleavage after Lys77 andA rg529
-
-
?
pro-hK2 + H2O
hK2 + ?
show the reaction diagram
-
hK5 can activate hK2 through cleavage after Lys137
-
-
?
pro-hK3 + H2O
hK3 + ?
show the reaction diagram
-
hK5 can activate hK3 through cleavage after Arg85 and Lys182
-
-
?
Pro-Phe-Ser-Arg-7-amido-4-methyl-coumarin + H2O
Pro-Phe-Ser-Arg + 7-amino-4-methyl-coumarin
show the reaction diagram
-
-
-
-
?
pro-[stratum corneum chymotryptic enzyme] + H2O
stratum corneum chymotryptic enzyme + ?
show the reaction diagram
-
stratum corneum tryptic enzyme activates stratum corneum chymotryptic enzyme through cleavage of the 31 kDa proenzyme resulting in the mature 28 kDa enzyme
-
-
?
Ser-Ser-Ser-Arg-Ile-Ile-Asn + H2O
Ser-Ser-Ser-Arg + Ile-Ile-Asn
show the reaction diagram
-
moderate cleavage efficiency
-
-
?
tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
best substrate
-
-
?
tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
best substrate
-
-
?
Tos-Gly-Pro-Arg-7-amido-4-methyl-coumarin + H2O
Tos-Gly-Pro-Arg + 7-amino-4-methyl-coumarin
show the reaction diagram
-
-
-
-
?
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Vitronectin + H2O
?
show the reaction diagram
-
cleavage after Arg8
-
-
?
Z-Gly-Gly-Arg-7-amido-4-methyl-coumarin + H2O
Z-Gly-Gly-Arg + 7-amino-4-methyl-coumarin
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
defensin-1alpha + H2O
?
show the reaction diagram
-
KLK5 is capable of processing defensin-1alpha and may be important in vaginal host defense
-
-
?
desmocollin-2 + H2O
?
show the reaction diagram
-
-
-
-
?
desmocollin-3 + H2O
?
show the reaction diagram
-
-
-
-
?
desmoglein protein 1 + H2O
?
show the reaction diagram
-
-
-
-
?
mucin 4 + H2O
?
show the reaction diagram
-
-
-
-
?
mucin 5B + H2O
?
show the reaction diagram
-
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
proform filaggrin + H2O
mature filaggrin + ?
show the reaction diagram
-
the enzyme and profilaggrin co-localize in the stratum granulosum in human epidermis. The enzyme interacts with its substrates in granular cells
-
-
?
desmocollin-3 + H2O
?
show the reaction diagram
-
-
-
-
?
desmoglein 1 + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha1-antitrypsin
-
-
-
alpha2-Macroglobulin
-
-
-
citrate
-
-
lympho-epithelial Kazal type inhibitor fragment D5
-
-
-
lympho-epithelial Kazal type inhibitor fragment D6
-
-
-
lympho-epithelial Kazal type inhibitor fragment D8-D11
-
-
-
lympho-epithelial Kazal type inhibitor fragment D9-D15
-
-
-
8,8'-paepalantine dimer
-
potent competitive inhibitor
alpha2-antiplasmin
-
50% inhibition at 0.8 microM in 0.6 min
-
antithrombin III
-
50% inhibition at 0.8 microM in 6 min
-
chymostatin
-
-
leupeptin
-
-
lymphoepithelial Kazal-type 5 serine protease inhibitor
-
-
-
paepalantine
-
-
SPINK9
-
vioxanthin
-
potent competitive inhibitor
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
androgens
slight up-regulation
-
dermatan
-
-
estrogen
up-regulaion
heparin
-
-
progestins
up-regulaion
citrate
-
17% activation at 120 nM, 32% activation at 1200 nM
additional information
-
no significant effect on enzyme activity by chondroitin
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6
L-Ile-Pro-Arg-p-nitroanilide
-
in 0.1 M Tris, 0.5 M NaCl, pH 8
0.004
Abz-KLRSSKQ-EDDnp
-
pH and temperature not specified in the publication
0.61
Boc-Gln-Ala-Arg-7-amido-4-methyl-coumarin
-
100 mM phosphate, 0.01% Tween 20, pH 8.0, 37C
1.41
Boc-Gln-Arg-Arg-7-amido-4-methyl-coumarin
-
100 mM phosphate, 0.01% Tween 20, pH 8.0, 37C
0.57
Boc-Gln-Gly-Arg-7-amido-4-methyl-coumarin
-
100 mM phosphate, 0.01% Tween 20, pH 8.0, 37C
0.48
Boc-Leu-Arg-Arg-7-amido-4-methyl-coumarin
-
100 mM phosphate, 0.01% Tween 20, pH 8.0, 37C
0.15
Boc-Leu-GLy-Arg-7-amido-4-methylcoumarin
-
100 mM phosphate, 0.01% Tween 20, pH 8.0, 37C
1.01
Boc-Leu-Lys-Arg-7-amido-4-methyl-coumarin
-
100 mM phosphate, 0.01% Tween 20, pH 8.0, 37C
0.19
Boc-Phe-Ser-Arg-7-amido-4-methyl-coumarin
-
100 mM phosphate, 0.01% Tween 20, pH 8.0, 37C
0.64
Boc-Val-Leu-Lys-7-amido-4-methyl-coumarin
-
100 mM phosphate, 0.01% Tween 20, pH 8.0, 37C
0.02
Boc-Val-Pro-Arg-7-amido-4-methyl-coumarin
-
100 mM phosphate, 0.01% Tween 20, pH 8.0, 37C
1.77
H-Pro-Phe-Ser-Arg-7-amido-4-methyl-coumarin
-
100 mM phosphate, 0.01% Tween 20, pH 8.0, 37C
1.69
Tos-Gly-Pro-Arg-7-amido-4-methyl-coumarin
-
100 mM phosphate, 0.01% Tween 20, pH 8.0, 37C
0.31
Z-Gly-Gly-Arg-7-amido-4-methyl-coumarin
-
100 mM phosphate, 0.01% Tween 20, pH 8.0, 37C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.5
Abz-KLRSSKQ-EDDnp
-
pH and temperature not specified in the publication
1.78
Boc-Gln-Ala-Arg-7-amido-4-methyl-coumarin
-
100 mM phosphate, 0.01% Tween 20, pH 8.0, 37C
0.41
Boc-Gln-Arg-Arg-7-amido-4-methyl-coumarin
-
100 mM phosphate, 0.01% Tween 20, pH 8.0, 37C
0.18
Boc-Gln-Gly-Arg-7-amido-4-methyl-coumarin
-
100 mM phosphate, 0.01% Tween 20, pH 8.0, 37C
0.31
Boc-Leu-Arg-Arg-7-amido-4-methyl-coumarin
-
100 mM phosphate, 0.01% Tween 20, pH 8.0, 37C
0.07
Boc-Leu-GLy-Arg-7-amido-4-methylcoumarin
-
100 mM phosphate, 0.01% Tween 20, pH 8.0, 37C
0.82
Boc-Leu-Lys-Arg-7-amido-4-methyl-coumarin
-
100 mM phosphate, 0.01% Tween 20, pH 8.0, 37C
2.83
Boc-Phe-Ser-Arg-7-amido-4-methyl-coumarin
-
100 mM phosphate, 0.01% Tween 20, pH 8.0, 37C
0.08
Boc-Val-Leu-Lys-7-amido-4-methyl-coumarin
-
100 mM phosphate, 0.01% Tween 20, pH 8.0, 37C
3.28
Boc-Val-Pro-Arg-7-amido-4-methyl-coumarin
-
100 mM phosphate, 0.01% Tween 20, pH 8.0, 37C
0.47
H-Pro-Phe-Ser-Arg-7-amido-4-methyl-coumarin
-
100 mM phosphate, 0.01% Tween 20, pH 8.0, 37C
0.35
Tos-Gly-Pro-Arg-7-amido-4-methyl-coumarin
-
100 mM phosphate, 0.01% Tween 20, pH 8.0, 37C
0.04
Z-Gly-Gly-Arg-7-amido-4-methyl-coumarin
-
100 mM phosphate, 0.01% Tween 20, pH 8.0, 37C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2125
Abz-KLRSSKQ-EDDnp
-
pH and temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000328
lympho-epithelial Kazal type inhibitor fragment D5
-
-
-
0.0000833
lympho-epithelial Kazal type inhibitor fragment D6
-
-
-
0.0000037
lympho-epithelial Kazal type inhibitor fragment D8-11
-
-
-
0.0001187
lympho-epithelial Kazal type inhibitor fragment D9-15
-
-
-
0.0244
8,8'-paepalantine dimer
-
pH and temperature not specified in the publication
0.00107
alpha2-antiplasmin
-
-
-
0.0091
antithrombin III
-
-
-
0.0017
leupeptin
-
at 25C in 0.2 M NaCl, 0.1 M Tris-HCl (pH 8.0), and 9% (w/v) Me2SO
0.0475
paepalantine
-
pH and temperature not specified in the publication
0.000065
serine protease inhibitor Kazal type 9
-
-
-
0.000257
SPINK9
-
pH 8, 21C
-
0.0229
vioxanthin
-
pH and temperature not specified in the publication
0.002 - 0.008
Zn2+
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0729
8,8'-paepalantine dimer
Homo sapiens
-
pH and temperature not specified in the publication
0.3674
paepalantine
Homo sapiens
-
pH and temperature not specified in the publication
0.0537
vioxanthin
Homo sapiens
-
pH and temperature not specified in the publication
0.009
Zn2+
Homo sapiens
-
in 150 mM NaCl, 20 mM HEPES, 0.04 mM imidazole, 0.005% (v/v) Tween 20, at pH 7.0
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
from ovarian cancer patients
Manually annotated by BRENDA team
-
level of KLK 5 peaks around 4 days post ovulation
Manually annotated by BRENDA team
of plantar skin
Manually annotated by BRENDA team
-
interfollicular epidermis; terminal
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
gene overexpression in a subset of more aggressive ovarian tumors
Manually annotated by BRENDA team
-
KLK5 peaks slightly at mid-cycle and shows a major peak at day 25 of menstrual cycle
Manually annotated by BRENDA team
-
female and male
Manually annotated by BRENDA team
-
enzyme expression
Manually annotated by BRENDA team
-
lexpression
Manually annotated by BRENDA team
-
pre-malignant keratinocyte cell line
Manually annotated by BRENDA team
-
high expression
Manually annotated by BRENDA team
-
low expression
Manually annotated by BRENDA team
-
high expression
Manually annotated by BRENDA team
-
low expression
Manually annotated by BRENDA team
-
specimens from patients with benign prostatic hyperplasia (BPH) show higher levels of KLK5 mRNA expression than those from patients with prostate cancer
Manually annotated by BRENDA team
-
high expression
Manually annotated by BRENDA team
-
decreased immunohistochemical expression compared to normal cells
Manually annotated by BRENDA team
-
high expression
Manually annotated by BRENDA team
-
expression
Manually annotated by BRENDA team
-
expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
KLK5 knockdown in normal cultured human epidermal keratinocytes results in higher levels of profilaggrin
malfunction
physiological function
additional information
-
potential role of endogenous KLK5 expression in supporting CaP cells to cope with the cytostatic phenomena induced by chemotherapeutic agents practiced in standard first-line CaP chemotherapy
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
KLK5_HUMAN
293
0
32020
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
-
recombinant deglycosylated enzyme, gel filtration
30000
-
recombinant glycosylated protein, gel filtration
33000
about, native and recombinant enzyme, gel filtration
40000
-
native glycosylated enzyme, gel filtration
26000
-
calculated from sequence
30000
-
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 25000-33000, native enzyme, SDS-PAGE; 1 * 30000-37000, recombinant enzyme, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
can be processed to active enzyme from inactive precursor by trypsin
glycoprotein
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
crystallized in complex with leupeptin, sitting drop vapour diffusion method with 0.2 M ammonium sulfate, 0.1 M Mes (pH 5.6) and 30% (w/v) PEG monomethyl ether 500
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
enzyme knockout in NHEK cells using KLK5 shRNA expressing vectors
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
from epidermis; recombinant from CHO-K1 cells
recombinant as His-tagged enzyme from Escherichia coli BL21(DE3)
-
recombinant enzyme from CHO-CCL-61 cells and from Pichia pastoris
-
heparin-Sepharose column chromatography and benzamidine-Sepharose column chromatography
-
reversed phase chromatography
-
two chromatography steps, 95% purity
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
cloned from a keratinocyte library, DNA sequence determination and analysis, expression in CHO-K1 cells via infection with Semliki Forest Virus system
cloned from RNA isolated from HaCaT cells, expression as His-tagged enzyme in Escherichia coli BL21(DE3)
-
DNA sequence determination and analysis, expression in CHO-CCL-61 cells, in Escherichia coli, and in Pichia pastoris
-
expressed in insect cells
-
gene KLK5, genetic organization and structure of the kallikrein gene family, clustered on chromosome 19q13.3-q13.4
KLK5 quantitative real-time PCR expression analysis
-
expressed in a baculovirus-insect cell system
-
expressed in insect cell/baculovirus expression system
-
expression in Pichia pastoris
-
gene KLK5, located at the chromosomal locus 19q13.3-q13.4, quantitative real-time PCR expression analysis, 10 transcription factors as potential regulators were found on the control regions of both KLK5 and KLK7
-
overexpression in OV-MZ-6 cancer cell line inoculated into the peritoneal cavity of nude mice promotes tumor growth in mice
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
KLK5 gene expression is severely upregulated in androgen-independent prostate cancer cells after treatment with the chemotherapeutic agents docetaxel and mitoxantrone
-
the enzyme is upregulated in some types of cancers, mainly prostate and ovarian cancers
-
10 transcription factors as potential regulators are found on the control regions of both KLK5 and KLK7
-
expression of kallikrein 5 is higher in oral squamous cell carcinoma cell compared to pre-malignant cells
-
kallikrein 5 has increased activity levels in eczematous lesions
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
-
KLK5 is a promising biomarker for prostate cancer diagnosis and prognosis
medicine
-
regulation by protease inhibitors may have potential clinical applications
diagnostics
-
KLK5 is a potential biomarker for breast cancer
medicine
-
KLK5 mRNA, analyzed by quantitative PCR in prostate needle biopsies, could be an independent biomarker for the differential diagnosis and prognosis in prostate cancer
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Nucleic Acids Res.
31
365-370
2003
Homo sapiens (Q9Y337), Mus musculus (P15945)
Manually annotated by BRENDA team
Yousef, G.M.; Diamandis, E.P.
The new human tissue kallikrein gene family: structure, function, and association to disease
Endocr. Rev.
22
184-204
2001
Homo sapiens (Q9Y337)
Manually annotated by BRENDA team
Brattsand, M.; Egelrud, T.
Purification, molecular cloning, and expression of a human stratum corneum trypsin-like serine protease with possible function in desquamation
J. Biol. Chem.
274
30033-30040
1999
Homo sapiens, Homo sapiens (Q9Y337)
Manually annotated by BRENDA team
Ekholm, I.E.; Brattsand, M.; Egelrud, T.
Stratum corneum tryptic enzyme in normal epidermis: a missing link in the desquamation process?
J. Invest. Dermatol.
114
56-63
2000
Homo sapiens, Homo sapiens (Q9Y337)
Manually annotated by BRENDA team
Yousef, G.M.; Kapadia, C.; Polymeris, M.E.; Borgono, C.; Hutchinson, S.; Wasney, G.A.; Soosaipillai, A.; Diamandis, E.P.
The human kallikrein protein 5 (hK5) is enzymatically active, glycosylated and forms complexes with two protease inhibitors in ovarian cancer fluids
Biochim. Biophys. Acta
1628
88-96
2003
Homo sapiens, Homo sapiens (Q9Y337)
Manually annotated by BRENDA team
Prezas, P.; Arlt, M.J.; Viktorov, P.; Soosaipillai, A.; Holzscheiter, L.; Schmitt, M.; Talieri, M.; Diamandis, E.P.; Krueger, A.; Magdolen, V.
Overexpression of the human tissue kallikrein genes KLK4, 5, 6, and 7 increases the malignant phenotype of ovarian cancer cells
Biol. Chem.
387
807-811
2006
Homo sapiens
Manually annotated by BRENDA team
Caubet, C.; Jonca, N.; Brattsand, M.; Guerrin, M.; Bernard, D.; Schmidt, R.; Egelrud, T.; Simon, M.; Serre, G.
Degradation of corneodesmosome proteins by two serine proteases of the kallikrein family, SCTE/KLK5/hK5 and SCCE/KLK7/hK7
J. Invest. Dermatol.
122
1235-1244
2004
Homo sapiens
Manually annotated by BRENDA team
Michael, I.P.; Sotiropoulou, G.; Pampalakis, G.; Magklara, A.; Ghosh, M.; Wasney, G.; Diamandis, E.P.
Biochemical and enzymatic characterization of human kallikrein 5 (hK5), a novel serine protease potentially involved in cancer progression
J. Biol. Chem.
280
14628-14635
2005
Homo sapiens
Manually annotated by BRENDA team
Michael, I.P.; Pampalakis, G.; Mikolajczyk, S.D.; Malm, J.; Sotiropoulou, G.; Diamandis, E.P.
Human tissue kallikrein 5 is a member of a proteolytic cascade pathway involved in seminal clot liquefaction and potentially in prostate cancer progression
J. Biol. Chem.
281
12743-12750
2006
Homo sapiens
Manually annotated by BRENDA team
Komatsu, N.; Tsai, B.; Sidiropoulos, M.; Saijoh, K.; Levesque, M.A.; Takehara, K.; Diamandis, E.P.
Quantification of eight tissue kallikreins in the Stratum corneum and sweat
J. Invest. Dermatol.
126
925-929
2006
Homo sapiens
Manually annotated by BRENDA team
Kurlender, L.; Yousef, G.M.; Memari, N.; Robb, J.D.; Michael, I.P.; Borgono, C.; Katsaros, D.; Stephan, C.; Jung, K.; Diamandis, E.P.
Differential expression of a human kallikrein 5 (KLK5) splice variant in ovarian and prostate cancer
Tumour Biol.
25
149-156
2004
Homo sapiens
Manually annotated by BRENDA team
Yousef, G.M.; White, N.M.; Kurlender, L.; Michael, I.; Memari, N.; Robb, J.D.; Katsaros, D.; Stephan, C.; Jung, K.; Diamandis, E.P.
The kallikrein gene 5 splice variant 2 is a new biomarker for breast and ovarian cancer
Tumour Biol.
25
221-227
2005
Homo sapiens
Manually annotated by BRENDA team
Petraki, C.D.; Gregorakis, A.K.; Vaslamatzis, M.M.; Papanastasiou, P.A.; Yousef, G.M.; Levesque, M.A.; Diamandis, E.P.
Prognostic Implications of the Immunohistochemical Expression of Human Kallikreins 5, 6, 10 and 11 in Renal Cell Carcinoma
Tumour Biol.
27
1-7
2006
Homo sapiens
Manually annotated by BRENDA team
Shinoda, Y.; Kozaki, K.; Imoto, I.; Obara, W.; Tsuda, H.; Mizutani, Y.; Shuin, T.; Fujioka, T.; Miki, T.; Inazawa, J.
Association of KLK5 overexpression with invasiveness of urinary bladder carcinoma cells
Cancer Sci.
98
1078-1086
2007
Homo sapiens
Manually annotated by BRENDA team
Voegeli, R.; Rawlings, A.V.; Doppler, S.; Heiland, J.; Schreier, T.
Profiling of serine protease activities in human stratum corneum and detection of a stratum corneum tryptase-like enzyme
Int. J. Cosmet. Sci.
29
191-200
2007
Homo sapiens
Manually annotated by BRENDA team
Debela, M.; Magdolen, V.; Schechter, N.; Valachova, M.; Lottspeich, F.; Craik, C.S.; Choe, Y.; Bode, W.; Goettig, P.
Specificity profiling of seven human tissue kallikreins reveals individual subsite preferences
J. Biol. Chem.
281
25678-25688
2006
Homo sapiens (Q9Y337)
Manually annotated by BRENDA team
Debela, M.; Goettig, P.; Magdolen, V.; Huber, R.; Schechter, N.M.; Bode, W.
Structural basis of the zinc inhibition of human tissue kallikrein 5
J. Mol. Biol.
373
1017-1031
2007
Homo sapiens, Homo sapiens (Q9Y337)
Manually annotated by BRENDA team
Deraison, C.; Bonnart, C.; Lopez, F.; Besson, C.; Robinson, R.; Jayakumar, A.; Wagberg, F.; Brattsand, M.; Hachem, J.P.; Leonardsson, G.; Hovnanian, A.
LEKTI fragments specifically inhibit KLK5, KLK7, and KLK14 and control desquamation through a pH-dependent interaction
Mol. Biol. Cell
18
3607-3619
2007
Homo sapiens (Q9Y337)
Manually annotated by BRENDA team
Shaw, J.L.; Petraki, C.; Watson, C.; Bocking, A.; Diamandis, E.P.
Role of tissue kallikrein-related peptidases in cervical mucus remodeling and host defense
Biol. Chem.
389
1513-1522
2008
Homo sapiens (Q9Y337)
Manually annotated by BRENDA team
Debela, M.; Beaufort, N.; Magdolen, V.; Schechter, N.M.; Craik, C.S.; Schmitt, M.; Bode, W.; Goettig, P.
Structures and specificity of the human kallikrein-related peptidases KLK 4, 5, 6, and 7
Biol. Chem.
389
623-632
2008
Homo sapiens
Manually annotated by BRENDA team
Korbakis, D.; Gregorakis, A.K.; Scorilas, A.
Quantitative analysis of human kallikrein 5 (KLK5) expression in prostate needle biopsies: an independent cancer biomarker
Clin. Chem.
55
904-913
2009
Homo sapiens, Homo sapiens (Q9Y337)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Brattsand, M.; Stefansson, K.; Hubiche, T.; Nilsson, S.K.; Egelrud, T.
SPINK9: A selective, skin-specific Kazal-type serine protease inhibitor
J. Invest. Dermatol.
129
1656-1665
2009
Homo sapiens
Manually annotated by BRENDA team
Meyer-Hoffert, U.; Wu, Z.; Schroeder, J.M.
Identification of lympho-epithelial Kazal-type inhibitor 2 in human skin as a kallikrein-related peptidase 5-specific protease inhibitor
PLoS ONE
4
e4372
2009
Homo sapiens
Manually annotated by BRENDA team
Mavridis, K.; Talieri, M.; Scorilas, A.
KLK5 gene expression is severely upregulated in androgen-independent prostate cancer cells after treatment with the chemotherapeutic agents docetaxel and mitoxantrone
Biol. Chem.
391
467-474
2010
Homo sapiens (Q9Y337)
Manually annotated by BRENDA team
Li, X.; Liu, J.; Wang, Y.; Zhang, L.; Ning, L.; Feng, Y.
Parallel underexpression of kallikrein 5 and kallikrein 7 mRNA in breast malignancies
Cancer Sci.
100
601-607
2009
Homo sapiens
Manually annotated by BRENDA team
Teixeira, T.S.; Freitas, R.F.; Abrahao, O.; Devienne, K.F.; de Souza, L.R.; Blaber, S.I.; Blaber, M.; Kondo, M.Y.; Juliano, M.A.; Juliano, L.; Puzer, L.
Biological evaluation and docking studies of natural isocoumarins as inhibitors for human kallikrein 5 and 7
Bioorg. Med. Chem. Lett.
21
6112-6115
2011
Homo sapiens
Manually annotated by BRENDA team
Britland, S.; Hoyle, M.
Transcriptional gene silencing of kallikrein 5 and kallikrein 7 using siRNA prevents epithelial cell detachment induced by alkaline shock in an in vitro model of eczema
Biotechnol. Prog.
28
485-489
2011
Homo sapiens
Manually annotated by BRENDA team
Jiang, R.; Shi, Z.; Johnson, J.J.; Liu, Y.; Stack, M.S.
Kallikrein-5 promotes cleavage of desmoglein-1 and loss of cell-cell cohesion in oral squamous cell carcinoma
J. Biol. Chem.
286
9127-9135
2011
Homo sapiens
Manually annotated by BRENDA team
De Souza, L.; M. Melo, P.; Paschoalin, T.; Carmona, A.; Kondo, M.; Hirata, I.; Blaber, M.; Tersariol, I.; Takatsuka, J.; Juliano, M.; Juliano, L.; Gomes, R.; Puzer, L.
Human tissue kallikreins 3 and 5 can act as plasminogen activator releasing active plasmin
Biochem. Biophys. Res. Commun.
433
333-337
2013
Homo sapiens (Q9Y337)
Manually annotated by BRENDA team
Sakabe, J.; Yamamoto, M.; Hirakawa, S.; Motoyama, A.; Ohta, I.; Tatsuno, K.; Ito, T.; Kabashima, K.; Hibino, T.; Tokura, Y.
Kallikrein-related peptidase 5 functions in proteolytic processing of profilaggrin in cultured human keratinocytes
J. Biol. Chem.
288
17179-17189
2013
Homo sapiens, Homo sapiens (Q9Y337)
Manually annotated by BRENDA team
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