Information on EC 3.4.21.B6 - prostasin and Organism(s) Homo sapiens and UniProt Accession Q16651

for references in articles please use BRENDA:EC3.4.21.B6
Word Map on EC 3.4.21.B6
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This record set is specific for:
Homo sapiens
UNIPROT: Q16651


The expected taxonomic range for this enzyme is: Tetrapoda


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
3.4.21.B6
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
prostasin
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cleavage of C-N-linkage
-
-
hydrolysis of peptide bond
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
157857-10-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
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-KHYR-7-amido-4-methylcoumarin + H2O
acetyl-KHYR + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
human Toll-like receptor 4 + H2O
truncated Toll-like receptor 4 + ectodomain
show the reaction diagram
-
reduction in the full-length form and reduction of the activation of the substrate. Substrate mutations K560A/K561A, K595A and R598A in the ectodomain abolish or reduce the enzyme activity, respectively
-
-
?
N-t-Boc-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
proform epithelial sodium channel + H2O
mature epithelial sodium channel + ?
show the reaction diagram
-
-
-
-
?
proform G protein-coupled protease activated receptor-2 + H2O
mature G protein-coupled protease activated receptor-2 + ?
show the reaction diagram
-
-
-
-
?
Toll-like receptor 4 + H2O
truncated Toll-like receptor 4 + ectodomain
show the reaction diagram
-
reduction in the full-length form and reduction of the activation of the substrate
-
-
?
7-amido-4-carbamoylmethylcoumarin-KHYRSVAS-K(DNP)R + H2O
?
show the reaction diagram
-
-
-
-
?
7-amido-4-carbamoylmethylcoumarin-KHYRSVAW-K(DNP)R + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-DHYR-7-amido-4-carbamoylmethylcoumarin + H2O
acetyl-DHYR + 7-amino-4-carbamoylmethylcoumarin
show the reaction diagram
-
suboptimal substrate
-
-
?
acetyl-KDYR-7-amido-4-carbamoylmethylcoumarin + H2O
acetyl-KDYR + 7-amino-4-carbamoylmethylcoumarin
show the reaction diagram
-
suboptimal substrate
-
-
?
acetyl-KHDR-7-amido-4-carbamoylmethylcoumarin + H2O
acetyl-KHDR + 7-amino-4-carbamoylmethylcoumarin
show the reaction diagram
-
suboptimal substrate
-
-
?
acetyl-KHYR-7-amido-4-carbamoylmethylcoumarin + H2O
acetyl-KHYR + 7-amino-4-carbamoylmethylcoumarin
show the reaction diagram
acetyl-KHYR-7-amido-4-methylcoumarin + H2O
acetyl-KHYR + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
acetyl-PRLR-7-amido-4-carbamoylmethylcoumarin + H2O
acetyl-PRLR + 7-amino-4-carbamoylmethylcoumarin
show the reaction diagram
benzyloxycarbonyl-Gly-Pro-Arg-7-amido-4-trifluoromethylcoumarin
benzyloxycarbonyl-Gly-Pro-Arg + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
?
D-Phe-Phe-Arg 4-methylcoumarin 7-amide
?
show the reaction diagram
-
-
-
?
D-Phe-Phe-Arg-7-amido-4-methylcoumarin + H2O
D-Phe-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
D-Pro-Phe-Arg 4-methylcoumarin 7-amide
?
show the reaction diagram
-
-
-
?
D-Pro-Phe-Arg 4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
fluorogenic substrate
-
?
D-Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
D-Pro-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
D-Val-Leu-Arg 4-methylcoumarin 7-amide
?
show the reaction diagram
-
-
-
?
D-Val-Leu-Arg-7-amido-4-methylcoumarin + H2O
D-Val-Leu-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
Protein + H2O
?
show the reaction diagram
tosyl-Gly-L-Pro-L-Arg-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
Z-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
Z-Gly-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
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
proform epithelial sodium channel + H2O
mature epithelial sodium channel + ?
show the reaction diagram
-
-
-
-
?
proform G protein-coupled protease activated receptor-2 + H2O
mature G protein-coupled protease activated receptor-2 + ?
show the reaction diagram
-
-
-
-
?
Toll-like receptor 4 + H2O
truncated Toll-like receptor 4 + ectodomain
show the reaction diagram
-
reduction in the full-length form and reduction of the activation of the substrate
-
-
?
Protein + H2O
?
show the reaction diagram
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-3-phenyl-L-prolinamide
-
-
(3S)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-3-methyl-L-prolinamide
-
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-(cyclohexylmethoxy)-L-prolinamide
-
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-(cyclopentylmethoxy)-L-prolinamide
-
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-([[4-(methylsulfonyl)benzyl]carbamoyl]oxy)-L-prolinamide
-
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-hydroxy-L-prolinamide
-
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[(4-chlorobenzyl)oxy]-L-prolinamide
-
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[(4-fluorobenzyl)oxy]-L-prolinamide
-
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[(4-methylbenzyl)oxy]-L-prolinamide
-
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[(dimethylcarbamoyl)oxy]-L-prolinamide
-
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[(morpholin-4-ylcarbonyl)oxy]-L-prolinamide
-
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[(phenylcarbamoyl)oxy]-L-prolinamide
-
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[(piperidin-1-ylcarbonyl)oxy]-L-prolinamide
-
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[(pyrrolidin-1-ylcarbonyl)oxy]-L-prolinamide
-
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[[3-(trifluoromethyl)benzyl]oxy]-L-prolinamide
-
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[[4-(trifluoromethyl)benzyl]oxy]-L-prolinamide
-
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-4-(benzyloxy)-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-L-prolinamide
-
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-4-[(benzylcarbamoyl)oxy]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-L-prolinamide
-
-
bacterial lipopolysaccharide
viral promoter-driven expression of the human prostasin in the bladder of transgenic mice attenuates the bacterial lipopolysaccharide induction of nitric oxide synthase, whereas induction of cyclooxygenase-2, TNF-alpha, IL-1beta and IL-6 expression is not reduced
-
benzyl [(1S)-2-[[(1S)-1-[[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]carbamoyl]-3-phenylpropyl]amino]-1-(1H-imidazol-4-ylmethyl)-2-oxoethyl]carbamate
-
-
benzyl [(1S)-5-amino-1-[[(1S)-1-[[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]carbamoyl]-3-phenylpropyl]carbamoyl]pentyl]carbamate
-
-
N-[(1S)-1-[[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]carbamoyl]-3-methylbutyl]-N2-[(benzyloxy)carbonyl]-L-lysinamide
-
-
N-[(1S)-1-[[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]carbamoyl]-3-methylbutyl]-Nalpha-[(benzyloxy)carbonyl]-L-histidinamide
-
-
N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-L-prolinamide
-
-
Protease nexin-1
-
inhibits prostasin´s serine protease activity, capable of binding to membrane-anchored prostasin
-
antipain
Aprotinin
benzamidine
Brij 35
-
activity decreases with increasing detergent concentration
CaCl2
-
-
camostat mesilate
-
potent inhibitor; potent prostasin inhibitor, 0.1 mM almost completely inhibits prostasin activity in vitro by 98.3%
CoCl2
-
-
CuCl2
-
-
EDTA
-
reduces enzyme activity by 30%
hepatocyte growth factor activator inhibitor-1
-
-
-
hepatocyte growth factor activator inhibitor-1A
-
-
-
hepatocyte growth factor activator inhibitor-1B
-
-
-
leupeptin
LiCl
-
-
MgCl2
-
-
NaCl
-
-
NiCl2
-
-
placental bikunin
-
-
-
prostasin-binding protein
-
Protease nexin-1
-
saline
-
reduces prostasin in nomotensive subjects
-
spironolactone
-
decreases urinary prostasin in nomotensives in whom the renin/aldosterone axis is activated by a low Na+ intake, ineffective in individuals with high Na+ intake
Tween 20
-
activity decreases with increasing detergent concentration
ZnCl2
-
with acetyl-KHYR-7-amino-3-carbamoylmethyl-4-methylcoumarin
additional information
-
not inhibited by alpha1-antitrypsin, alpha1-antitrypsinPDX, alpha1-antichymotrypsin, and soybean trypsin inhibitor
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
nerve growth factor
-
induces prostasin expression
-
sterol-regulatory element-binding protein-1c
-
-
-
sterol-regulatory element-binding protein-2
-
-
-
CHAPS
-
increases enzyme activity up to 4fold with increasing concentration
DMSO
-
increases enzyme activity up to 2fold with increasing concentration
hepsin
-
hepsin activates prostasin by cleaving in the amino-terminal pro-peptide region of prostasin at Arg44
-
matriptase
-
transcription factor sterol regulatory element-binding protein-2
-
up-regulates protein expression
-
ZnCl2
-
with acetyl-PRLR-7-amino-3-carbamoylmethyl-4-methylcoumarin
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0335 - 0.0493
acetyl-KHYR-7-amido-4-methylcoumarin
0.0555 - 0.86
acetyl-KDYR-7-amido-4-carbamoylmethylcoumarin
0.193
acetyl-KHYR-7-amido-4-carbamoylmethylcoumarin
-
-
0.0786 - 0.141
acetyl-PRLR-7-amido-4-carbamoylmethylcoumarin
827
D-Phe-Phe-Arg 7-amido-4-methylcoumarin
-
pH 9, 25°C
108
D-Pro-Phe-Arg 7-amido-4-methylcoumarin
-
pH 9, 25°C
255
D-Val-Leu-Arg-7-amido-4-methylcoumarin
-
pH 9, 25°C
717
Z-Gly-Pro-Arg-7-amido-4-trifluoromethylcoumarin
-
pH 9, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12 - 0.27
acetyl-KHYR-7-amido-4-methylcoumarin
0.083 - 6.53
acetyl-KDYR-7-amido-4-carbamoylmethylcoumarin
1.97
acetyl-KHYR-7-amido-4-carbamoylmethylcoumarin
-
-
0.381 - 6.08
acetyl-PRLR-7-amido-4-carbamoylmethylcoumarin
0.29
D-Phe-Phe-Arg 7-amido-4-methylcoumarin
-
pH 9, 25°C
0.068
D-Pro-Phe-Arg 7-amido-4-methylcoumarin
-
pH 9, 25°C
0.105
D-Val-Leu-Arg-7-amido-4-methylcoumarin
-
pH 9, 25°C
0.287
Z-Gly-Pro-Arg-7-amido-4-trifluoromethylcoumarin
-
pH 9, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000267
(3R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-3-phenyl-L-prolinamide
-
-
0.000049
(3S)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-3-methyl-L-prolinamide
-
-
0.000019
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-(cyclohexylmethoxy)-L-prolinamide
-
-
0.000065
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-(cyclopentylmethoxy)-L-prolinamide
-
-
0.000176
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-([[4-(methylsulfonyl)benzyl]carbamoyl]oxy)-L-prolinamide
-
-
0.00104
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-hydroxy-L-prolinamide
-
-
0.000012
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[(4-chlorobenzyl)oxy]-L-prolinamide
-
-
0.000027
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[(4-fluorobenzyl)oxy]-L-prolinamide
-
-
0.000045
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[(4-methylbenzyl)oxy]-L-prolinamide
-
-
0.00155
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[(dimethylcarbamoyl)oxy]-L-prolinamide
-
-
0.00051
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[(morpholin-4-ylcarbonyl)oxy]-L-prolinamide
-
-
0.00013
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[(phenylcarbamoyl)oxy]-L-prolinamide
-
-
0.000029
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[(piperidin-1-ylcarbonyl)oxy]-L-prolinamide
-
-
0.000101
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[(pyrrolidin-1-ylcarbonyl)oxy]-L-prolinamide
-
-
0.000041
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[[3-(trifluoromethyl)benzyl]oxy]-L-prolinamide
-
-
0.000028
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[[4-(trifluoromethyl)benzyl]oxy]-L-prolinamide
-
-
0.000049
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-4-(benzyloxy)-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-L-prolinamide
-
-
0.000065
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-4-[(benzylcarbamoyl)oxy]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-L-prolinamide
-
-
0.0021
benzyl [(1S)-2-[[(1S)-1-[[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]carbamoyl]-3-phenylpropyl]amino]-1-(1H-imidazol-4-ylmethyl)-2-oxoethyl]carbamate
-
-
0.00578
benzyl [(1S)-5-amino-1-[[(1S)-1-[[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]carbamoyl]-3-phenylpropyl]carbamoyl]pentyl]carbamate
-
-
0.0152
N-[(1S)-1-[[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]carbamoyl]-3-methylbutyl]-N2-[(benzyloxy)carbonyl]-L-lysinamide
-
-
0.00572
N-[(1S)-1-[[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]carbamoyl]-3-methylbutyl]-Nalpha-[(benzyloxy)carbonyl]-L-histidinamide
-
-
0.0014
N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-L-prolinamide
-
-
0.0000014
Aprotinin
-
-
1.15
CaCl2
-
with acetyl-KHYR-7-amido-4-carbamoylmethylcoumarin
0.047 - 0.57
CoCl2
0.0021
CuCl2
-
with acetyl-PRLR-7-amido-4-carbamoylmethylcoumarin
21.3
LiCl
-
with acetyl-KHYR-7-amido-4-carbamoylmethylcoumarin
1.42
MgCl2
-
with acetyl-KHYR-7-amido-4-carbamoylmethylcoumarin
22.4
NaCl
-
with acetyl-KHYR-7-amido-4-carbamoylmethylcoumarin
26.3
NaF
-
with acetyl-KHYR-7-amido-4-carbamoylmethylcoumarin
16.4
NaI
-
with acetyl-KHYR-7-amido-4-carbamoylmethylcoumarin
0.01
NiCl2
-
with acetyl-PRLR-7-amido-4-carbamoylmethylcoumarin
0.000005
placental bikunin
-
-
-
0.0048
ZnCl2
-
with acetyl-PRLR-7-amido-4-carbamoylmethylcoumarin
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5 - 9.5
-
50% activity at pH 8.5 and pH 9.5
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
-
isoelectric focusing, pH gradient 3.5-10
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
co-expression of matriptase and its substrate serine protease prostasin
Manually annotated by BRENDA team
-
strong expression association between matriptase and its substrate prostasin in breast cancer
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
a benign prostatic hyperplasia cell line
Manually annotated by BRENDA team
-
prostasin is expressed abundantly in normal epithelia
Manually annotated by BRENDA team
-
enzyme levels significantly higher than those in control cells
Manually annotated by BRENDA team
-
downregulation of the enzyme in high-grade prostate cancer as well as in invasive prostate cancer cells
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24000
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purified refolded prostasin, gel filtration
27879
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1 * 27879, refolded and purified prostasin variant 26, calculated from sequence
28351
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1 * 28351, refolded and purified prostasin variant 28, calculated from sequence
40000
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x * 40000, SDS-PAGE
35000
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SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 40000, SDS-PAGE
monomer
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1 * 27879, refolded and purified prostasin variant 26, calculated from sequence; 1 * 28351, refolded and purified prostasin variant 28, calculated from sequence
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
glycoprotein
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method. Active prostasin is crystallized, and the structure is determined to 1.45 A resolution. These apoprotein crystals are soaked with nafamostat, allowing the structure of the inhibited acyl-enzyme intermediate structure to be determined to 2.0 A resolution
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structure of the extracellular portion of the membrane associated serine protease solved to high resolution in complex with a nonselective d-FFR chloromethyl ketone inhibitor, in an apo form, in a form where the apo crystal is soaked with the covalent inhibitor camostat and in complex with the protein inhibitor aprotinin. It is also crystallized in the presence of the divalent cation Ca2+
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X-ray crystal structures of prostasin with small molecule inhibitors
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
standard method
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1960fold
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by gel filtration
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by sequential anion exchange and aprotinin affinity chromatography, by Ni-NTA His-bind chromatography
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DEAE Sepharose column chromatography, and hepatocyte growth factor activator inhibitor-1 mAb M19 immunoaffinity column chromatography
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homogeneity
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Ni-Sepharose column chromatography, HiTrap Q column chromatography, and Supderdex 200 gel filtration; Ni-Sepharose column chromatography, HiTrap Q column chromatography, and Superdex 200 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in HEK-293 cells
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expressed in Mus musculus urinary bladder epithelium; into vector pREP8, expression in the bladder of transgenic mice
expression of the prostasin proenzyme in Escherichia coli as insoluble inclusion bodies, refolding and activating via proteolytic removal of the N-terminal propeptide
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expressed in FT-293 cells
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expressed in HEK-293 cells
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expressed in silkworm larvae by recombinant baculovirus
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expressed in the prostate carcinoma cell line PC-3
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expression in Sf9 cells
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into pCRT7/NT-TOPO and expressed in Escherichia coli BL21(DE3)pLysS, into pcDNA3.1/V5-His-TOPO and expressed in CHO cells and HEK-293 cells, overexpression in CF epithelial cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
high-fat diet triggers the suppression of the enzyme expression by inducing endoplasmic reticulum stress
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prostasin expression increases during human Caco-2 cell differentiation and barrier formation
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prostasin is down-regulated in human prostate, breast, and gastric cancers and invasive cancer cell lines
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prostasin is highly overexpressed in ovarian cancer cell lines
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the mRNA level of prostasin is slightly but significantly decreased in both mild/moderate dysplasia and severe dysplasia and in carcinomas compared to normal tissue from the same individual
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H85A/D134A/S238A
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protease-dead mutant
R44A
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the mutant cannot be activated by cleavage through hepsin or matriptase
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
medicine