Information on EC 3.4.21.B6 - prostasin

Word Map on EC 3.4.21.B6
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The expected taxonomic range for this enzyme is: Tetrapoda

EC NUMBER
COMMENTARY hide
3.4.21.B6
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
prostasin
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
endoprotease activity. Trypsin-like enzymatic activity
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cleavage of C-N-linkage
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
157857-10-8
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
spatial and temporal co-expression of matriptase and prostasin
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
epithelial sodium channel gamma subunit + H2O
?
show the reaction diagram
-
the enzyme activates epithelial sodium channels by inducing cleavage of the gamma-subunit at a site distal to the furin cleavage site
-
-
?
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 filaggrin + H2O
mature filaggrin + ?
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
-
-
-
-
?
Protein + H2O
?
show the reaction diagram
Toll-like receptor 4 + H2O
truncated Toll-like receptor 4 + ectodomain
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 filaggrin + H2O
mature filaggrin + ?
show the reaction diagram
Q9ESD1
-
-
-
?
proform G protein-coupled protease activated receptor-2 + H2O
mature G protein-coupled protease activated receptor-2 + ?
show the reaction diagram
-
-
-
-
?
Protein + H2O
?
show the reaction diagram
Toll-like receptor 4 + H2O
truncated Toll-like receptor 4 + ectodomain
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
-
-
antipain
Aprotinin
bacterial lipopolysaccharide
-
benzamidine
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
-
-
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
-
-
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
-
-
NaCl
-
-
NiCl2
-
-
placental bikunin
-
-
-
prostasin-binding protein
-
Protease nexin-1
-
saline
-
reduces prostasin in nomotensive subjects
-
soybean trypsin inhbitor
-
-
-
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
TGF-beta1
-
suppresses prostasin promoter activity in a time- and concentration-dependent manner, inhibition of prostasin expression by the induction of IkappaBalpha and the subsequent inhibition of NF-kappaB/Rel activity, may inhibit sodium reabsorption through a reduction in prostasin expression and subsequent inhibition of ENaC activity
-
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
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
-
nerve growth factor
-
induces prostasin expression
-
sterol-regulatory element-binding protein-1c
-
-
-
sterol-regulatory element-binding protein-2
-
-
-
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
0.0555 - 0.86
acetyl-KDYR-7-amido-4-carbamoylmethylcoumarin
0.193
acetyl-KHYR-7-amido-4-carbamoylmethylcoumarin
-
-
0.0335 - 0.0493
acetyl-KHYR-7-amido-4-methylcoumarin
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
0.083 - 6.53
acetyl-KDYR-7-amido-4-carbamoylmethylcoumarin
1.97
acetyl-KHYR-7-amido-4-carbamoylmethylcoumarin
Homo sapiens
-
-
0.12 - 0.27
acetyl-KHYR-7-amido-4-methylcoumarin
0.381 - 6.08
acetyl-PRLR-7-amido-4-carbamoylmethylcoumarin
0.29
D-Phe-Phe-Arg 7-amido-4-methylcoumarin
Homo sapiens
-
pH 9, 25°C
0.068
D-Pro-Phe-Arg 7-amido-4-methylcoumarin
Homo sapiens
-
pH 9, 25°C
0.105
D-Val-Leu-Arg-7-amido-4-methylcoumarin
Homo sapiens
-
pH 9, 25°C
0.287
Z-Gly-Pro-Arg-7-amido-4-trifluoromethylcoumarin
Homo sapiens
-
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
-
-
0.0000014
Aprotinin
-
-
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
-
-
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
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
-
-
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
-
a benign prostatic hyperplasia cell line
Manually annotated by BRENDA team
-
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
-
simple, stratified, and pseudo-stratified epithelium of the digestive tract
Manually annotated by BRENDA team
-
simple, stratified, and pseudo-stratified epithelium of the integumentary system
Manually annotated by BRENDA team
-
during menstrual cycle
Manually annotated by BRENDA team
-
enzyme levels significantly higher than those in control cells
Manually annotated by BRENDA team
-
simple, stratified, and pseudo-stratified epithelium of the respiratory tract
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
simple, stratified, and pseudo-stratified epithelium of the urogenital tract
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24000
-
purified refolded prostasin, gel filtration
27879
-
1 * 27879, refolded and purified prostasin variant 26, calculated from sequence
28351
-
1 * 28351, refolded and purified prostasin variant 28, calculated from sequence
35000
-
SDS-PAGE
37000
-
SDS-PAGE, mature active enzyme
39000
-
SDS-PAGE, immature enzyme
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 40000, SDS-PAGE
monomer
-
1 * 27879, refolded and purified prostasin variant 26, calculated from sequence; 1 * 28351, refolded and purified prostasin variant 28, calculated from sequence
additional information
from the N-terminus, prostasin comprises a pro-domain and a serine protease domain with trypsin-like activity, prostasin contains an N-terminal secretion signal that is cleaved during intracellular transport in the endoplasmic reticulum and a GPI-anchor is attached at the C-terminal
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
-
proteolytic modification
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
1960fold
-
by gel filtration
-
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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standard method
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in FT-293 cells
-
expressed in HEK-293 cells
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expressed in HEK-293T cells
-
expressed in M-1 cells
expressed in MDCK cells
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expressed in Mus musculus urinary bladder epithelium; into vector pREP8, expression in the bladder of transgenic mice
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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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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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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subcloned into pGEM-T easy vector, subcloned into pGL3-basic vector and expressed in M-1 cells
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subcloned into the pREP8 plasmid, transfected into the HEK-293 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
high-fat diet triggers the suppression of the enzyme expression by inducing endoplasmic reticulum stress
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
-
protease-dead mutant
R44A
-
the mutant cannot be activated by cleavage through hepsin or matriptase
S238A
inactive
S313N/S314L
lacks the preferred GPI attachment sites and shows decreased activity
S313N/S314L/R322A
mutant alters both the preferred GPI attachment sites and the potential COOH-terminal tryptic cleavage site, activity is not different from wild type prostasin
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
additional information