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Information on EC 3.4.21.B28 - fibroblast activation protein alpha subunit and Organism(s) Homo sapiens and UniProt Accession Q12884

for references in articles please use BRENDA:EC3.4.21.B28
preliminary BRENDA-supplied EC number
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Homo sapiens
UNIPROT: Q12884
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Tetrapoda
Reaction Schemes
fibroblast activation protein requires substrates with Pro at P1 and Gly or D-amino acids at P2. Met-alpha2-antiplasmin is cleaved N-terminally at Pro3-Leu4 and Pro12-Asn13 into Asn-alpha2-antiplasmin that is rapidly cross-linked to fibrin and protects it from digestion by plasmin
fibroblast activation protein requires substrates with Pro at P1 and Gly or D-amino acids at P2. Met-alpha2-antiplasmin is cleaved N-terminally at Pro3-Leu4 and Pro12-Asn13 into Asn-alpha2-antiplasmin that is rapidly cross-linked to fibrin and protects it from digestion by plasmin.
Synonyms
fap, fapalpha, fap-alpha, fibroblast activation protein-alpha, antiplasmin-cleaving enzyme, fibroblast activation factor, z-pro-prolinal-insensitive peptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
antiplasmin-cleaving enzyme
-
fibroblast activation factor
-
fibroblast activation protein
-
fibroblast activation protein alpha
member of the group type II integral serine proteases, subfamily S9b, with gelatinase and N-terminal post-prolyl amino peptidase activities
fibroblast activation protein-alpha
-
gelatinase
-
S09.007
Merops ID
surface expressed protease
-
antiplasmin-cleaving enzyme
FAP-alpha
FAP-specific protease
-
FAPalpha
fibroblast activation protein
fibroblast activation protein alpha
fibroblast activation protein protease
-
-
fibroblast activation protein-alpha
fibroblast activation protein-specific protease
-
seprase
type II transmembrane serine protease
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
fibroblast activation protein requires substrates with Pro at P1 and Gly or D-amino acids at P2. Met-alpha2-antiplasmin is cleaved N-terminally at Pro3-Leu4 and Pro12-Asn13 into Asn-alpha2-antiplasmin that is rapidly cross-linked to fibrin and protects it from digestion by plasmin
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
cleavage of C-N-linkage
hydrolysis of peptide bond
-
-
cleavage of C-N-linkage
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
352031-63-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-D-Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
acetyl-D-Ala-Pro + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
?
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin + H2O
acetyl-Gly-Pro-7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
?
Ala-Pro-4-trifluoromethylcoumarin-7-amide + H2O
Ala-Pro + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
?
Ala-Ser-Gly-Pro-Asn-Gln + H2O
Ala-Ser-Gly-Pro + Asn-Gln
show the reaction diagram
-
-
-
?
Ala-Ser-Gly-Pro-Ser-Ser + H2O
Ala-Ser-Gly-Pro + Ser-Ser
show the reaction diagram
-
-
-
?
alpha2-antiplasmin + H2O
?
show the reaction diagram
Arg-Lys-(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-D-Ala-Pro-Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid)-Arg + H2O
Arg-Lys-(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-D-Ala-Pro + Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid)-Arg
show the reaction diagram
-
-
-
?
Arg-Lys-(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-D-Ser-Pro-Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid)-Arg + H2O
Arg-Lys-(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-D-Ser-Pro + Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid)-Arg
show the reaction diagram
-
-
-
?
B-type natriuretic peptide + H2O
?
show the reaction diagram
efficiently hydrolysed and mostly preferred substrate
-
-
?
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
D-Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
D-Ala-Pro + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
?
glucagon-like peptide-1 + H2O
?
show the reaction diagram
slow hydrolysis
-
-
?
glucose-dependent insulinotropic peptide + H2O
?
show the reaction diagram
slow hydrolysis
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
Gly-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Gly-Pro + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
?
Gly-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Gly-Pro + 7-amino-4-trifluoromethylcoumarin + H2O
show the reaction diagram
-
-
-
?
L-Ala-L-Pro-7-amido-4-methylcoumarin + H2O
L-Ala-L-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
L-Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
L-Ala-Pro + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
?
L-Arg-Lys-(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-Gly-Pro-Asn-Gln-Gln-Gln-Glu(5-[(2-aminoethyl)amino]-naphthalene-1-sulfonic acid)-Arg + H2O
?
show the reaction diagram
FRET-peptide
-
-
?
MEPLGRQLTSGP-7-amido-4-methylcoumarin + H2O
MEPLGRQLTSGP + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
MEPLGWQLTSGP-7-amido-4-methylcoumarin + H2O
MEPLGWQLTSGP + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
neuropeptide Y + H2O
?
show the reaction diagram
efficiently hydrolysed and mostly preferred substrate
-
-
?
peptide YY + H2O
?
show the reaction diagram
efficiently hydrolysed substrate
-
-
?
Substance P + H2O
?
show the reaction diagram
efficiently hydrolysed substrate
-
-
?
Thr-Ala-Gly-Pro-Asn-Gln + H2O
Thr-Ala-Gly-Pro + Asn-Gln
show the reaction diagram
-
-
-
?
Thr-Ser-Gly-Pro-Asn-Gln + H2O
Thr-Ser-Gly-Pro + Asn-Gln
show the reaction diagram
-
-
-
?
Thr-Ser-Gly-Pro-Asn-Ser + H2O
Thr-Ser-Gly-Pro + Asn-Ser
show the reaction diagram
-
-
-
?
Thr-Ser-Gly-Pro-Ser-Gln + H2O
Thr-Ser-Gly-Pro + Ser-Gln
show the reaction diagram
-
-
-
?
Type I collagen + H2O
?
show the reaction diagram
-
-
-
?
Z-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
Z-Gly-L-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
7-methoxycoumarin-4-acetic acid-APGSKGDA-dinitrophenyl + H2O
?
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-ASGPAGPA-dinitrophenyl + H2O
?
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-DKGESGPA-dinitrophenyl + H2O
?
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-DRGETGP-dinitrophenyl + H2O
?
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-DRGETGPA-dinitrophenyl + H2O
?
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-DSGETGP-dinitrophenyl + H2O
?
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-DSGETGPA-dinitrophenyl + H2O
?
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-EPGPPGPA-dinitrophenyl + H2O
?
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-ERGETGPA-dinitrophenyl + H2O
?
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-ERGETGPAG-dinitrophenyl + H2O
?
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-ERGETGPAGG-dinitrophenyl + H2O
?
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-ERGETGPSG-dinitrophenyl + H2O
?
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-VGPAGK-dinitrophenyl + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
acetyl-Gly-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Ala-Pro-4-trifluoromethylcoumarin-7-amide + H2O
Ala-Pro + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
?
Ala-Pro-4-trifluoromethylcoumarin-7-amide + H2O
Ala-Pro-4 + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
?
Ala-Pro-7-amido-4-methylcoumarin + H2O
Ala-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Ala-Pro + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Ala-Pro + 7-amino-4-trifluoromethylcoumarin + H2O
show the reaction diagram
-
-
-
-
?
alpha2-antiplasmin + H2O
?
show the reaction diagram
alpha2-antiplasmin + H2O
truncated alpha2-antiplasmin + Met
show the reaction diagram
-
-
cleaves Met from the N-terminus yielding Asn as the N-terminal amino acid
-
?
Arg-Lys(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-Gly-Pro-Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]-naphthalene-1-sulfonic acid)-Arg + H2O
Arg-Lys(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-Gly-Pro + Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]-naphthalene-1-sulfonic acid)-Arg
show the reaction diagram
-
-
-
-
?
Arg-Pro-7-amido-4-methylcoumarin + H2O
Arg-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
preferred substrate
-
-
?
benzyloxycarbonyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-L-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-7-amido-4-methyl-3-carbamoylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro + 7-amino-4-methyl-3-carbamoylcoumarin
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
biotinyl-Gly-Pro-7-amido-4-methyl-3-carbamoylcoumarin + H2O
biotinyl-Gly-Pro + 7-amino-4-methyl-3-carbamoylcoumarin
show the reaction diagram
-
-
-
-
?
Boc-Ala-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
Boc-Ala-Gly-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
denatured type I collagen + H2O
?
show the reaction diagram
-
-
-
-
?
GASGPAGPA + H2O
GASGP + AGPA
show the reaction diagram
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
GEPGPPGPA + H2O
GEP + GPPGP + L-Ala
show the reaction diagram
-
-
-
?
GFSPFQRED + H2O
?
show the reaction diagram
low activity
-
-
?
Gln-Pro-7-amido-4-methylcoumarin + H2O
Gln-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Glu-Pro-7-amido-4-methylcoumarin + H2O
Glu-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Gly-Pro-4-trifluoromethylcoumarin-7-amide + H2O
Gly-Pro + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
Gly-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Gly-Pro + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
GTAGPNQEQE + H2O
GTAGP + NQEQE
show the reaction diagram
-
-
-
?
GTSGPNQEQE + H2O
GTSGP + NQEQE
show the reaction diagram
-
-
-
?
Ile-Pro-7-amido-4-methylcoumarin + H2O
Ile-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
most preferred substrate
-
-
?
Ile-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Ile-Pro + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
L-Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
L-Ala-Pro + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
Leu-Pro-7-amido-4-methylcoumarin + H2O
Leu-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Lys-Ala-7-amido-4-trifluoromethylcoumarin + H2O
Lys-Ala + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
Lys-Pro-4-trifluoromethylcoumarin-7-amide + H2O
Lys-Pro + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
?
Lys-Pro-7-amido-4-methylcoumarin + H2O
Lys-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Met-alpha2-antiplasmin + H2O
?
show the reaction diagram
Met-Pro-7-amido-4-methylcoumarin + H2O
Met-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N-formyl-Gly-Pro-7-amido-4-methyl-3-carbamoylcoumarin + H2O
N-formyl-Gly-Pro + 7-amino-4-methyl-3-carbamoylcoumarin
show the reaction diagram
-
-
-
-
?
N-methyl-Gly-Pro-7-amido-4-methyl-3-carbamoylcoumarin + H2O
N-methyl-Gly-Pro + 7-amino-4-methyl-3-carbamoylcoumarin
show the reaction diagram
-
-
-
-
?
Phe-Pro-7-amido-4-methylcoumarin + H2O
Phe-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Phe-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Phe-Pro + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
pre-digested collagen + H2O
?
show the reaction diagram
-
-
-
-
?
precursor Met-alpha2-antiplasmin + H2O
L-Asn-alpha2-antiplasmin + ?
show the reaction diagram
-
the enzyme cleaves between Pro12 and Asn13
-
-
?
Pro-Pro-7-amido-4-methylcoumarin + H2O
Pro-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
preferred substrate
-
-
?
RPKPQQFFGLM + H2O
RPKP + L-Gln-L-Gln + FFGLM
show the reaction diagram
the substance P-derived sequence is cleaved although it does not contain Gly-Pro
-
-
?
Ser-Pro-7-amido-4-methylcoumarin + H2O
Ser-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Thr-Pro-7-amido-4-methylcoumarin + H2O
Thr-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Tic-Pro-7-amido-4-trifluoromethylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Type I collagen + H2O
?
show the reaction diagram
-
-
-
?
Tyr-Pro-7-amido-4-methylcoumarin + H2O
Tyr-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Val-Pro-7-amido-4-methylcoumarin + H2O
Val-Pro + 7-amino-4-methylcoumarin
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
alpha2-antiplasmin + H2O
?
show the reaction diagram
B-type natriuretic peptide + H2O
?
show the reaction diagram
efficiently hydrolysed and mostly preferred substrate
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
?
glucagon-like peptide-1 + H2O
?
show the reaction diagram
slow hydrolysis
-
-
?
glucose-dependent insulinotropic peptide + H2O
?
show the reaction diagram
slow hydrolysis
-
-
?
neuropeptide Y + H2O
?
show the reaction diagram
efficiently hydrolysed and mostly preferred substrate
-
-
?
peptide YY + H2O
?
show the reaction diagram
efficiently hydrolysed substrate
-
-
?
Substance P + H2O
?
show the reaction diagram
efficiently hydrolysed substrate
-
-
?
alpha2-antiplasmin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
Met-alpha2-antiplasmin + H2O
?
show the reaction diagram
-
APCE and rFAP cleave both Pro3-Leu4 and Pro12-Asn13 bonds of Met-alpha2-antiplasmin, but relative kcat /Km values for Pro12-Asn13 are about 16fold higher than for Pro3-Leu4. Conversion of Met-alpha2-antiplasmin by membrane or soluble FAP to the more easily fibrin-incorporable form, Asn-alpha2-antiplasmin, may increase plasmin inhibition within fibrin surrounding certain neoplasms and have an impact on growth and therapeutic susceptibility
-
-
?
pre-digested collagen + H2O
?
show the reaction diagram
-
-
-
-
?
Type I collagen + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
inhibition at 140 mM
4-(2-aminoethyl)-benzenesulfonyl fluoride hydrochloride
AEBSF, inhibition at 5 mM
4-(2-aminoethyl)-benzenesulfonylfluoride
5 mM
4-amidino phenylsulfonyl fluoride
APSF, inhibition at 0.05 mM
4-amidino-phenylsulfonylfluoride
0.5 mM
acetyl-Gly-boro-Pro
-
acetyl-Gly-Pro-CN
-
chymostatin
50% inhibition at 0.16 mM
diisopropyl fluorophosphate
0.005 mM
diisopropylfluorophosphate
inhibition at 0.005 mM
dimethyl sulfoxide
50% inhibition at 4%
dithiothreitol
inhibition at 10 mM
FRQLTSG-pipecolinyl-NQEQV
-
Ile-boro-Pro
-
Ile-Pro-CN
-
L-Val-aminoacyl-proline boronic acid
PT-100
N-ethylmaleimide
-
N-[2-[(2R)-2-(dihydroxyboranyl)pyrrolidin-1-yl]-2-oxoethyl]-9-N-methyl-5-oxoprolinamide
-
Phe-Arg-8-amino-3,6-dioxaoctanoyl-Gly-(R)-fluoropyrrolidide
-
Phe-Arg-8-amino-3,6-dioxaoctanoyl-Gly-(S)-fluoropyrrolidide
-
Phe-Arg-8-amino-3,6-dioxaoctanoyl-Gly-pipecolinyl-NQEQV
-
Phe-Arg-8-amino-3,6-dioxaoctanoyl-Gly-piperidide
-
Phe-Arg-8-amino-3,6-dioxaoctanoyl-Gly-pyrrolidide
-
Phe-Gly-8-amino-3,6-dioxaoctanoyl-Gly-pipecolinyl-NQEQV
-
Phe-Gly-8-amino-3,6-dioxaoctanoyl-Gly-pipecolinyl-NQGQV
-
Phe-Gly-8-amino-3,6-dioxaoctanoyl-Gly-pyrrolidide
-
phenylmethylsulfonyl fluoride
Phenylmethylsulfonylfluoride
1 mM
Talabostat
-
Val-boro-Pro
-
Val-Pro-CN
-
ValboroPro
complete inhibition at 0.05 mM
[(2R)-1-(4-oxo-4-phenylbutanoyl)pyrrolidin-2-yl]boronic acid
-
[(2R)-1-(N-acetyl-L-alanyl)pyrrolidin-2-yl]boronic acid
-
[(2R)-1-(N-acetyl-N-methylglycyl)pyrrolidin-2-yl]boronic acid
-
[(2R)-1-(N-acetylglycyl)pyrrolidin-2-yl]boronic acid
-
[(2R)-1-[(1-oxo-1,3-dihydro-2H-isoindol-2-yl)acetyl]pyrrolidin-2-yl]-9-boronic acid
-
[(2R)-1-[(2-oxopyridin-1(2H)-yl)acetyl]pyrrolidin-2-yl]-9-boronic acid
-
[(2R)-1-[N-(2,2-dimethylpropanoyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
-
[(2R)-1-[N-(2-methylpropanoyl)glycyl]pyrrolidin-2-yl-9]-boronic acid
-
[(2R)-1-[N-(cyclohexylcarbonyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
-
[(2R)-1-[N-(cyclopentylcarbonyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
-
[(2R)-1-[N-(methylsulfonyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
-
[(2R)-1-[N-(phenylcarbonyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
-
[(2R)-1-[N-methyl-N-(2-methylpropanoyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
-
[(2R)-1-[N-methyl-N-(phenylcarbonyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
-
[(2R)-1-[N-[(2,5-dichlorophenyl)carbonyl]glycyl]-9-pyrrolidin-2-yl]boronic acid
-
[(2R)-1-[N-[(2,6-dichlorophenyl)carbonyl]glycyl]-9-pyrrolidin-2-yl]boronic acid
-
1-benzyl-7-(but-2-yn-1-yl)-3-methyl-8-(piperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
1-[(4-methoxyquinazolin-2-yl)methyl]-3,7-dimethyl-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
1-[(4-methoxyquinazolin-2-yl)methyl]-3-methyl-7-(3-methylbut-2-en-1-yl)-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
1-[(4-methoxyquinazolin-2-yl)methyl]-3-methyl-7-(4-methylpent-3-en-1-yl)-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
3,7-dimethyl-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
3-[[7-(but-2-yn-1-yl)-3-methyl-2,6-dioxo-8-(piperazin-1-yl)-2,3,6,7-tetrahydro-1H-purin-1-yl]methyl]benzonitrile
-
4'-[[7-(but-2-yn-1-yl)-3-methyl-2,6-dioxo-8-(piperazin-1-yl)-2,3,6,7-tetrahydro-1H-purin-1-yl]methyl]biphenyl-2-carbonitrile
-
7-(but-2-yn-1-yl)-1-[(4-methoxyquinazolin-2-yl)methyl]-3-methyl-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-1-[(4-methoxyquinazolin-2-yl)methyl]-3-methyl-8-(piperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-1-[[2-(hydroxymethyl)-1,3-thiazol-4-yl]methyl]-3-methyl-8-(piperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-1-(naphthalen-2-ylmethyl)-8-(piperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-8-(piperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-8-(piperidin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-1-[(5-methyl-2-phenyl-2H-1,2,3-triazol-4-yl)methyl]-8-(piperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-8-(3-oxopiperazin-1-yl)-1-(pyridin-2-ylmethyl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-8-(3-oxopiperazin-1-yl)-1-(pyridin-3-ylmethyl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-8-(3-oxopiperazin-1-yl)-1-(pyridin-4-ylmethyl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-8-(piperazin-1-yl)-1-(quinazolin-2-ylmethyl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-8-(piperazin-1-yl)-1-(quinolin-2-ylmethyl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-8-(piperazin-1-yl)-1-[4-(1H-1,2,4-triazol-1-yl)benzyl]-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-8-(piperazin-1-yl)-1-[4-(1H-pyrazol-1-yl)benzyl]-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-8-ethoxy-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-8-[(3S)-3-(hydroxymethyl)-5-oxopiperazin-1-yl]-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-8-[(8aS)-hexahydropyrrolo[1,2-a]pyrazin-2(1H)-yl]-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-3,7-dihydro-1H-purine-2,6-dione
-
7-benzyl-1-[(4-methoxyquinazolin-2-yl)methyl]-3-methyl-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
8-[(3R)-3-aminopiperidin-1-yl]-7-(but-2-yn-1-yl)-3-methyl-1-(propan-2-yl)-3,7-dihydro-1H-purine-2,6-dione
-
acetyl-Arg-(8-amino-3,6-dioxaoctanoic acid)-D-Ala-L-boroPro
-
selectively inhibits antiplasmin-cleaving enzyme vs. plasma dipeptidyl peptidase IV
acetyl-Arg-(8-amino-3,6-dioxaoctanoic acid)-D-Asp-L-boroPro
-
-
acetyl-Arg-(8-amino-3,6-dioxaoctanoic acid)-Gly-L-boroPro
-
-
acetyl-Arg-(8-amino-3,6-dioxaoctanoic acid)-Ser-Gly-L-boroPro
-
-
acetyl-Arg-Gly-Gly-L-boroPro
-
-
acetyl-Arg-peg-D-Asp-L-boroPro
-
-
acetyl-Arg-peg-Gly-L-boroPro
-
-
acetyl-Arg-peg-Ser-Gly-L-boroPro
-
-
acetyl-Gly-L-boroPro
-
-
acetyl-Gly-Pro-boronic acid
-
-
Ala-ProP(OPh)2
-
-
alogliptin
-
diisopropylfluorophosphate
-
50% inhibition at 0.02 mM
dutogliptin
-
Gly-ProP(OPh)2
-
-
Leu-Pro-PO(OPh)2
-
-
linagliptin
-
N-[(3R)-1-[7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-yl]piperidin-3-yl]acetamide
-
N-[2-(2-cyano-4,4-difluoropyrrolidin-1-yl)-2-oxoethyl]quinoline-4-carboxamide
-
N-[2-([7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-yl]amino)ethyl]acetamide
-
N-[2-([7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-yl]amino)ethyl]pyridine-4-carboxamide
-
N2-[7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-yl]glycinamide
-
Phe-ProP(OPh)2
-
-
phenylmethylsulfonyl fluoride
-
50% inhibition at 0.1 mM
Pro-ProP(OPh)2
-
-
saxagliptin
-
Ser-ProP(OPh)2
-
-
sitagliptin
-
Tyr-ProP(OPh)2
-
-
Val-boroPro
-
-
Val-ProP(OPh)2
-
-
vildagliptin
-
[(2S)-1-(D-valyl)pyrrolidin-2-yl]boronic acid
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
trans-epoxysuccinyl-L-leucylamido(4-guanidino)-butane
activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.541
acetyl-D-Ala-Pro-7-amido-4-trifluoromethylcoumarin
23°C
0.087 - 2.3
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
0.2
Ala-Pro-4-trifluoromethylcoumarin-7-amide
pH 8.5
0.0022
Ala-Ser-Gly-Pro-Asn-Gln
23°C
0.0043
Ala-Ser-Gly-Pro-Ser-Ser
23°C
0.0008
Arg-Lys-(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-D-Ala-Pro-Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid)-Arg
23°C
0.0006
Arg-Lys-(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-D-Ser-Pro-Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid)-Arg
23°C
0.09
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin
pH 7.5, 22°C
0.213
D-Ala-Pro-7-amido-4-trifluoromethylcoumarin
23°C
0.455 - 1
Gly-Pro-7-amido-4-methylcoumarin
0.062 - 1.8
Gly-Pro-7-amido-4-trifluoromethylcoumarin
0.2 - 0.323
L-Ala-Pro-7-amido-4-trifluoromethylcoumarin
0.029
L-Arg-Lys-(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-Gly-Pro-Asn-Gln-Gln-Gln-Glu(5-[(2-aminoethyl)amino]-naphthalene-1-sulfonic acid)-Arg
recombinant enzyme
0.021
MEPLGRQLTSGP-7-amido-4-methylcoumarin
pH 7.5, 22°C
0.07
MEPLGWQLTSGP-7-amido-4-methylcoumarin
pH 7.5, 22°C
0.0007
Thr-Ala-Gly-Pro-Asn-Gln
23°C
0.0013
Thr-Ser-Gly-Pro-Asn-Gln
23°C
0.0022
Thr-Ser-Gly-Pro-Asn-Ser
23°C
0.0019
Thr-Ser-Gly-Pro-Ser-Gln
23°C
0.051
7-methoxycoumarin-4-acetic acid-APGSKGDA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.0361
7-methoxycoumarin-4-acetic acid-ASGPAGPA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.046
7-methoxycoumarin-4-acetic acid-DKGESGPA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.0238
7-methoxycoumarin-4-acetic acid-DRGETGP-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.021
7-methoxycoumarin-4-acetic acid-DRGETGPA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.0396
7-methoxycoumarin-4-acetic acid-DSGETGP-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.0202
7-methoxycoumarin-4-acetic acid-DSGETGPA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.0269
7-methoxycoumarin-4-acetic acid-EPGPPGPA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.0567
7-methoxycoumarin-4-acetic acid-ERGETGPA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.043
7-methoxycoumarin-4-acetic acid-ERGETGPAG-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.0371
7-methoxycoumarin-4-acetic acid-ERGETGPAGG-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.0513
7-methoxycoumarin-4-acetic acid-ERGETGPSG-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.052
7-methoxycoumarin-4-acetic acid-VGPAGK-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.46
Ala-Pro-4-trifluoromethylcoumarin-7-amide
-
pH 7.8, 37°C
0.244 - 0.323
Ala-Pro-7-amido-4-trifluoromethylcoumarin
0.026 - 0.029
Arg-Lys(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-Gly-Pro-Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]-naphthalene-1-sulfonic acid)-Arg
0.101 - 0.124
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin
0.248
Gly-Pro-7-amido-4-trifluoromethylcoumarin
-
at 23°C in 50 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, pH 7.4
0.106
Ile-Pro-7-amido-4-trifluoromethylcoumarin
-
at 23°C in 50 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, pH 7.4
0.189
Lys-Ala-7-amido-4-trifluoromethylcoumarin
-
at 23°C in 50 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, pH 7.4
0.9
Lys-Pro-4-trifluoromethylcoumarin-7-amide
-
pH 7.8, 37°C
0.245
Phe-Pro-7-amido-4-trifluoromethylcoumarin
-
at 23°C in 50 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, pH 7.4
0.053
Tic-Pro-7-amido-4-trifluoromethylcoumarin
-
in 25 mM sodium phosphate buffer, pH 7.5, containing 1.0 mM EDTA and 2% (v/v) methanol, at 22°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3
acetyl-D-Ala-Pro-7-amido-4-trifluoromethylcoumarin
23°C
0.05 - 14
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
2
Ala-Pro-4-trifluoromethylcoumarin-7-amide
pH 8.5
2.7
Ala-Ser-Gly-Pro-Asn-Gln
23°C
5.5
Ala-Ser-Gly-Pro-Ser-Ser
23°C
0.19
Arg-Lys-(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-D-Ala-Pro-Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid)-Arg
23°C
0.22
Arg-Lys-(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-D-Ser-Pro-Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid)-Arg
23°C
36.4
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin
pH 7.5, 22°C
1.5
D-Ala-Pro-7-amido-4-trifluoromethylcoumarin
23°C
29.1
Gly-Pro-7-amido-4-methylcoumarin
pH 7.5, 22°C
0.03 - 5.6
Gly-Pro-7-amido-4-trifluoromethylcoumarin
1.08
L-Ala-Pro-7-amido-4-trifluoromethylcoumarin
recombinant enzyme
1.2
L-Arg-Lys-(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-Gly-Pro-Asn-Gln-Gln-Gln-Glu(5-[(2-aminoethyl)amino]-naphthalene-1-sulfonic acid)-Arg
recombinant enzyme
70.2
MEPLGRQLTSGP-7-amido-4-methylcoumarin
pH 7.5, 22°C
55.3
MEPLGWQLTSGP-7-amido-4-methylcoumarin
pH 7.5, 22°C
1.5
Thr-Ala-Gly-Pro-Asn-Gln
23°C
1.6
Thr-Ser-Gly-Pro-Asn-Gln
23°C
3.1
Thr-Ser-Gly-Pro-Asn-Ser
23°C
2
Thr-Ser-Gly-Pro-Ser-Gln
23°C
0.015
7-methoxycoumarin-4-acetic acid-APGSKGDA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.196
7-methoxycoumarin-4-acetic acid-ASGPAGPA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.067
7-methoxycoumarin-4-acetic acid-DKGESGPA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.003
7-methoxycoumarin-4-acetic acid-DRGETGP-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.081
7-methoxycoumarin-4-acetic acid-DRGETGPA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.003
7-methoxycoumarin-4-acetic acid-DSGETGP-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.059
7-methoxycoumarin-4-acetic acid-DSGETGPA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.115
7-methoxycoumarin-4-acetic acid-EPGPPGPA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.141
7-methoxycoumarin-4-acetic acid-ERGETGPA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.121
7-methoxycoumarin-4-acetic acid-ERGETGPAG-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.079
7-methoxycoumarin-4-acetic acid-ERGETGPAGG-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.268
7-methoxycoumarin-4-acetic acid-ERGETGPSG-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.095
7-methoxycoumarin-4-acetic acid-VGPAGK-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.995 - 14.2
Ala-Pro-7-amido-4-trifluoromethylcoumarin
1.06 - 1.2
Arg-Lys(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-Gly-Pro-Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]-naphthalene-1-sulfonic acid)-Arg
0.51 - 0.54
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin
5.6
Gly-Pro-7-amido-4-trifluoromethylcoumarin
-
at 23°C in 50 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, pH 7.4
6.9
Ile-Pro-7-amido-4-trifluoromethylcoumarin
-
at 23°C in 50 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, pH 7.4
0.01
Lys-Ala-7-amido-4-trifluoromethylcoumarin
-
at 23°C in 50 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, pH 7.4
1.1
Phe-Pro-7-amido-4-trifluoromethylcoumarin
-
at 23°C in 50 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, pH 7.4
1.19
Tic-Pro-7-amido-4-trifluoromethylcoumarin
-
in 25 mM sodium phosphate buffer, pH 7.5, containing 1.0 mM EDTA and 2% (v/v) methanol, at 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22
Tic-Pro-7-amido-4-trifluoromethylcoumarin
-
in 25 mM sodium phosphate buffer, pH 7.5, containing 1.0 mM EDTA and 2% (v/v) methanol, at 22°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.023
acetyl-Gly-boro-Pro
6.8
acetyl-Gly-Pro-CN
0.014
FRQLTSG-pipecolinyl-NQEQV
pH 7.5, 22°C
0.014
Ile-boro-Pro
0.84
Ile-Pro-CN
0.000146
N-[2-[(2R)-2-(dihydroxyboranyl)pyrrolidin-1-yl]-2-oxoethyl]-9-N-methyl-5-oxoprolinamide
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.0553
Phe-Arg-8-amino-3,6-dioxaoctanoyl-Gly-(R)-fluoropyrrolidide
pH 7.5, 22°C
0.0538
Phe-Arg-8-amino-3,6-dioxaoctanoyl-Gly-(S)-fluoropyrrolidide
pH 7.5, 22°C
0.015
Phe-Arg-8-amino-3,6-dioxaoctanoyl-Gly-pipecolinyl-NQEQV
pH 7.5, 22°C
0.264
Phe-Arg-8-amino-3,6-dioxaoctanoyl-Gly-piperidide
pH 7.5, 22°C
0.068
Phe-Arg-8-amino-3,6-dioxaoctanoyl-Gly-pyrrolidide
pH 7.5, 22°C
0.057
Phe-Gly-8-amino-3,6-dioxaoctanoyl-Gly-pipecolinyl-NQEQV
pH 7.5, 22°C
0.0145
Phe-Gly-8-amino-3,6-dioxaoctanoyl-Gly-pipecolinyl-NQGQV
pH 7.5, 22°C
0.703
Phe-Gly-8-amino-3,6-dioxaoctanoyl-Gly-pyrrolidide
pH 7.5, 22°C
0.0062
Val-boro-Pro
0.034
Val-Pro-CN
0.000094
[(2R)-1-(4-oxo-4-phenylbutanoyl)pyrrolidin-2-yl]boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.00035
[(2R)-1-(N-acetyl-L-alanyl)pyrrolidin-2-yl]boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.000161
[(2R)-1-(N-acetyl-N-methylglycyl)pyrrolidin-2-yl]boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.000023
[(2R)-1-(N-acetylglycyl)pyrrolidin-2-yl]boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.0000075
[(2R)-1-[(1-oxo-1,3-dihydro-2H-isoindol-2-yl)acetyl]pyrrolidin-2-yl]-9-boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.0029
[(2R)-1-[(2-oxopyridin-1(2H)-yl)acetyl]pyrrolidin-2-yl]-9-boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.000751
[(2R)-1-[N-(2,2-dimethylpropanoyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.000051
[(2R)-1-[N-(2-methylpropanoyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.000014
[(2R)-1-[N-(cyclohexylcarbonyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.00002
[(2R)-1-[N-(cyclopentylcarbonyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.000246
[(2R)-1-[N-(methylsulfonyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.000142
[(2R)-1-[N-(phenylcarbonyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.000265
[(2R)-1-[N-methyl-N-(2-methylpropanoyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.000191
[(2R)-1-[N-methyl-N-(phenylcarbonyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.000029
[(2R)-1-[N-[(2,5-dichlorophenyl)carbonyl]glycyl]-9-pyrrolidin-2-yl]boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.000012
[(2R)-1-[N-[(2,6-dichlorophenyl)carbonyl]glycyl]-9-pyrrolidin-2-yl]boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.0000057
acetyl-Arg-(8-amino-3,6-dioxaoctanoic acid)-D-Ala-L-boroPro
-
in 25 mM sodium phosphate buffer, pH 7.5, containing 1.0 mM EDTA and 2% (v/v) methanol, at 22°C
0.001377
acetyl-Arg-(8-amino-3,6-dioxaoctanoic acid)-D-Asp-L-boroPro
-
in 25 mM sodium phosphate buffer, pH 7.5, containing 1.0 mM EDTA and 2% (v/v) methanol, at 22°C
0.0000018
acetyl-Arg-(8-amino-3,6-dioxaoctanoic acid)-Gly-L-boroPro
-
in 25 mM sodium phosphate buffer, pH 7.5, containing 1.0 mM EDTA and 2% (v/v) methanol, at 22°C
0.0000027
acetyl-Arg-(8-amino-3,6-dioxaoctanoic acid)-Ser-Gly-L-boroPro
-
in 25 mM sodium phosphate buffer, pH 7.5, containing 1.0 mM EDTA and 2% (v/v) methanol, at 22°C
0.0000172
acetyl-Arg-Gly-Gly-L-boroPro
-
in 25 mM sodium phosphate buffer, pH 7.5, containing 1.0 mM EDTA and 2% (v/v) methanol, at 22°C
0.0000207
acetyl-Gly-L-boroPro
-
in 25 mM sodium phosphate buffer, pH 7.5, containing 1.0 mM EDTA and 2% (v/v) methanol, at 22°C
0.000023
acetyl-Gly-Pro-boronic acid
-
-
0.00327
Gly-ProP(OPh)2
-
in 25 mM Tris, containing 140 mM NaCl and 10 mM KCl, pH 7.9
0.006
Leu-Pro-PO(OPh)2
-
in 25 mM Tris, containing 140 mM NaCl and 10 mM KCl, pH 7.9
0.0046
Pro-ProP(OPh)2
-
in 25 mM Tris, containing 140 mM NaCl and 10 mM KCl, pH 7.9
0.00216
Ser-ProP(OPh)2
-
in 25 mM Tris, containing 140 mM NaCl and 10 mM KCl, pH 7.9
0.00259
Tyr-ProP(OPh)2
-
in 25 mM Tris, containing 140 mM NaCl and 10 mM KCl, pH 7.9
0.00363
Val-ProP(OPh)2
-
in 25 mM Tris, containing 140 mM NaCl and 10 mM KCl, pH 7.9
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.091
Phe-Arg-(8-amino-3,6-dioxaoctanoic acid)-Gly-[R]-fluoropyrrolidide
Homo sapiens
cleavage of Met-alpha2-antiplasmin
0.00004
Talabostat
Homo sapiens
-
0.1
1-benzyl-7-(but-2-yn-1-yl)-3-methyl-8-(piperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
above, pH and temperature not specified in the publication
0.1
1-[(4-methoxyquinazolin-2-yl)methyl]-3,7-dimethyl-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
above, pH and temperature not specified in the publication
0.05
1-[(4-methoxyquinazolin-2-yl)methyl]-3-methyl-7-(4-methylpent-3-en-1-yl)-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.1
3,7-dimethyl-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
above, pH and temperature not specified in the publication
0.1
3-[[7-(but-2-yn-1-yl)-3-methyl-2,6-dioxo-8-(piperazin-1-yl)-2,3,6,7-tetrahydro-1H-purin-1-yl]methyl]benzonitrile
Homo sapiens
above, pH and temperature not specified in the publication
0.1
4'-[[7-(but-2-yn-1-yl)-3-methyl-2,6-dioxo-8-(piperazin-1-yl)-2,3,6,7-tetrahydro-1H-purin-1-yl]methyl]biphenyl-2-carbonitrile
Homo sapiens
above, pH and temperature not specified in the publication
0.0058
7-(but-2-yn-1-yl)-1-[(4-methoxyquinazolin-2-yl)methyl]-3-methyl-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0012
7-(but-2-yn-1-yl)-1-[(4-methoxyquinazolin-2-yl)methyl]-3-methyl-8-(piperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.1
7-(but-2-yn-1-yl)-1-[[2-(hydroxymethyl)-1,3-thiazol-4-yl]methyl]-3-methyl-8-(piperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
above, pH and temperature not specified in the publication
0.041
7-(but-2-yn-1-yl)-3-methyl-1-(naphthalen-2-ylmethyl)-8-(piperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0019
7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.00074
7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-8-(piperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.01
7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-8-(piperidin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.1
7-(but-2-yn-1-yl)-3-methyl-1-[(5-methyl-2-phenyl-2H-1,2,3-triazol-4-yl)methyl]-8-(piperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
above, pH and temperature not specified in the publication
0.0125
7-(but-2-yn-1-yl)-3-methyl-8-(3-oxopiperazin-1-yl)-1-(pyridin-2-ylmethyl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.1
7-(but-2-yn-1-yl)-3-methyl-8-(3-oxopiperazin-1-yl)-1-(pyridin-3-ylmethyl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
above, pH and temperature not specified in the publication
0.1
7-(but-2-yn-1-yl)-3-methyl-8-(3-oxopiperazin-1-yl)-1-(pyridin-4-ylmethyl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
above, pH and temperature not specified in the publication
0.1
7-(but-2-yn-1-yl)-3-methyl-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
above, pH and temperature not specified in the publication
0.0018
7-(but-2-yn-1-yl)-3-methyl-8-(piperazin-1-yl)-1-(quinazolin-2-ylmethyl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0103
7-(but-2-yn-1-yl)-3-methyl-8-(piperazin-1-yl)-1-(quinolin-2-ylmethyl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.1
7-(but-2-yn-1-yl)-3-methyl-8-(piperazin-1-yl)-1-[4-(1H-1,2,4-triazol-1-yl)benzyl]-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
above, pH and temperature not specified in the publication
0.05
7-(but-2-yn-1-yl)-3-methyl-8-(piperazin-1-yl)-1-[4-(1H-pyrazol-1-yl)benzyl]-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.1
7-(but-2-yn-1-yl)-8-ethoxy-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
above, pH and temperature not specified in the publication
0.0033
7-(but-2-yn-1-yl)-8-[(3S)-3-(hydroxymethyl)-5-oxopiperazin-1-yl]-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.011
7-(but-2-yn-1-yl)-8-[(8aS)-hexahydropyrrolo[1,2-a]pyrazin-2(1H)-yl]-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.1
8-[(3R)-3-aminopiperidin-1-yl]-7-(but-2-yn-1-yl)-3-methyl-1-(propan-2-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
above, pH and temperature not specified in the publication
0.1
alogliptin
Homo sapiens
above, pH and temperature not specified in the publication
0.00752
dutogliptin
Homo sapiens
pH and temperature not specified in the publication
0.000089 - 0.00037
linagliptin
Homo sapiens
pH and temperature not specified in the publication
0.01
N-[(3R)-1-[7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-yl]piperidin-3-yl]acetamide
Homo sapiens
pH and temperature not specified in the publication
0.0000033
N-[2-(2-cyano-4,4-difluoropyrrolidin-1-yl)-2-oxoethyl]quinoline-4-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.01
N-[2-([7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-yl]amino)ethyl]acetamide
Homo sapiens
pH and temperature not specified in the publication
0.01
N-[2-([7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-yl]amino)ethyl]pyridine-4-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.1
N2-[7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-yl]glycinamide
Homo sapiens
above, pH and temperature not specified in the publication
0.0026
saxagliptin
Homo sapiens
pH and temperature not specified in the publication
0.1
sitagliptin
Homo sapiens
above, pH and temperature not specified in the publication
0.073
vildagliptin
Homo sapiens
pH and temperature not specified in the publication
0.00007
[(2S)-1-(D-valyl)pyrrolidin-2-yl]boronic acid
Homo sapiens
pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
wild type enzyme
8.5
recombinant enzyme
7.5
-
substrate: Arg-Lys(DABCYL)-Thr-Ser-Gly-Pro-Asn-Gln-Glu-Gln-Glu(EDANS)-Arg, APCE or rFAP
8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
transiently expressed in certain normal fetal mesenchymal tissues
Manually annotated by BRENDA team
the induced seprase expression of ovarian tumor cells influences their collagen contraction and invasion capability. Tumor cells with reduced seprase expression, due to manipulation by RNA interference, show a reduction of type I collagen gel contraction
Manually annotated by BRENDA team
expressed in both premalignant and malignant forms of squamous cell carcinoma, but are lacking in normal esophageal epithelia, suggesting that the enzyme is involved in squamous cell carcinoma neoplastic progression
Manually annotated by BRENDA team
-
malignant mesenchymal cells
Manually annotated by BRENDA team
-
cancer stroma cells
Manually annotated by BRENDA team
-
higher levels in cancer tissue than normal tissue
Manually annotated by BRENDA team
-
mainly located, seprase-expressing carcinoma tissue more often found in the scirrhous type than in other types of gastric carcinoma
Manually annotated by BRENDA team
the protease fibroblast activation protein is a specific marker of activated mesenchymal cells in tumour stroma and fibrotic liver
Manually annotated by BRENDA team
-
expression in idiopathic pulmonary fibrosis, not expressed in normal lung tissue or tissue with evidence of centriacinar emphysema
Manually annotated by BRENDA team
-
embryonic
Manually annotated by BRENDA team
-
the enzyme is coexpressed with dipeptidyl peptidase-IV in adult humans
Manually annotated by BRENDA team
-
the enzyme is coexpressed with dipeptidyl peptidase-IV in adult humans
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
-
siRNA knockdown of FAP-alpha in a glioma cell line shows decreased invasion through brain extracellular matrix proteoglycan brevican and denatured collagen
metabolism
FAP-alpha is significantly increased in breast cancer patients with poor outcome and survival
physiological function
additional information
overexpression of FAP-alpha results in a reduction of phosphorylated focal adhesion kinase level in both MCF-7 cells and MDA-MB-231 cells cultured in normal media and serum-free media, while the growth of MDA-MB-231 cells and the adhesion and invasion ability of both MCF-7 cells and MDA-MB-231 cells are not dramatically influenced by FAP-alpha expression
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SEPR_HUMAN
760
1
87713
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
170000
400000
above 400000 Da, complex in nonionic detergents, gel filtration
87720
subunit, calculated from amino acid sequence
95000
recombinant enzyme
97000
100000
-
2 * 100000, multiangle light scattering in combination with gel filtration chromatography and interferometric refractometry
105000
-
1 * 95000 + 1 * 105000, SDS-PAGE
153000
-
recombinant FAP, gel filtration
160000 - 170000
-
-
170000
175000
-
native APCE, gel filtration
200000
-
multiangle light scattering in combination with gel filtration chromatography and interferometric refractometry
215000
-
SDS-PAGE under nonreducing conditions
400000
-
above 400000 Da, complex, gel filtration
90000
-
theoretical value of FAPalpha-His6tag
93000
-
2 * 93000, recombinant FAP, SDS-PAGE
95000
-
1 * 95000 + 1 * 105000, SDS-PAGE
97000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
homodimer
2 * 97000, wild type enzyme
dimer
homodimer
monomer
-
Western immunoblotting
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
glycoprotein
-
N-linked carbohydrate side chains, but on evidence of O-glycans
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
at 4°C, by Syrrx´s automated Nanovolume crystallization technology, Ala657 reduces the acidity in this pocket, which may explain the lower affinity for N-terminal amines
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A657D
increased activity
A657F
decreased activity
A657G
decreased activity
A657N
increased activity
A657Q
decreased activity
A657S
decreased activity
A657T
decreased activity
A657V
decreased activity
E203A
diminished activity
E203A/E204A
diminished activity
E203D
diminished activity
E203D/E204D
diminished activity
E203Q
diminished activity
E203Q/E204Q
diminished activity
E204A
diminished activity
E204D
diminished activity
E204Q
diminished activity
N704A
diminished activity
R123A
diminished activity
R123K
diminished activity
R123M
diminished activity
Y656F
diminished activity
A657D
-
shows a 60fold increase in the catalytic efficiency for the cleavage of dipeptide substrates, catalytic efficiency reduced by ca. 350fold for the cleavage of benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin
S624A
-
inactive mutant
additional information
-
MDA-MB-231 cell mammary adenocarcinoma cells engineered to express active seprase to high levels
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
anti-FLAG affinity chromatography
glycosylated form, near homogeneity
S-200 gel filtration, hydroxylapatite column chromatography, Cibacron blue chromatography, and WGA-agarose column chromatography
ammonium sulfate precipitation, hydrophobic interaction column chromatography, and immunoaffinity column chromatography
-
M2-anti-FLAG resin column chromatography
-
Ni-NTA resin column chromatography
-
partial purification by Sephacryl S-200 gel filtration
-
standard protocol
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
97000 Da subunit
expressed in HEK-293 cells
expressed in WI38 cells
expressed in 293 cells
-
expressed in Schneider S2 cells
-
FAP is expressed in Pichia pastoris
-
into a modified pFastBacHTb vector
-
quantitative real-time PCR enzyme expression analysis
recombinant expression in Escherichia coli TOP10 cells and transfection of SKOV-3 and HO-8910 cells, two poorly differentiated ovarian serous adenocarcinoma cell lines, using a lentivirus expression vector, quantitative real-time PCR enzyme expression analzsis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
FAP-alpha is considerably induced upon differentiation with 10% fetal calf serum, FAP-alpha is elevated in glioblastomas and increases upon tumor stem cell differentiation
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
-
diagnostic and prognostic biomarker for various types of cancer. Development and validation of a combined kinetic fluorometric activity assay for fibroblast activation protein alpha and prolyl oligopeptidase in plasma
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Goldstein, L.A.; Ghersi, G.; Pineiro-Sanchez, M.L.; Salamone, M.; Yeh, Y.; Flessate, D.; Chen, W.T.
Molecular cloning of seprase: a serine integral membrane protease from human melanoma
Biochim. Biophys. Acta
1361
11-19
1997
Homo sapiens (Q12884)
Manually annotated by BRENDA team
Rettig, W.J.; Garin-Chesa, P.; Healey, J.H.; Su, S.L.; Ozer, H.L.; Schwab, M.; Albino, A.P.; Old, L.J.
Regulation and heteromeric structure of the fibroblast activation protein in normal and transformed cells of mesenchymal and neuroectodermal origin
Cancer Res.
53
3327-3335
1993
Homo sapiens
Manually annotated by BRENDA team
Rettig, W.J.; Su, S.L.; Fortunato, S.R.; Scanlan, M.J.; Raj, B.K.; Garin-Chesa, P.; Healey, J.H.; Old, L.J.
Fibroblast activation protein: purification, epitope mapping and induction by growth factors
Int. J. Cancer
58
385-392
1994
Homo sapiens
Manually annotated by BRENDA team
Pineiro-Sanchez, M.L.; Goldstein, L.A.; Dodt, J.; Howard, L.; Yeh, Y.; Tran, H.; Argraves, W.S.; Chen, W.T.
Identification of the 170-kDa melanoma membrane-bound gelatinase (seprase) as a serine integral membrane protease
J. Biol. Chem.
272
7595-7601
1997
Homo sapiens (Q12884), Homo sapiens
Manually annotated by BRENDA team
Park, J.E.; Lenter, M.C.; Zimmermann, R.N.; Garin-Chesa, P.; Old, L.J.; Rettig, W.J.
Fibroblast activation protein, a dual specificity serine protease expressed in reactive human tumor stromal fibroblasts
J. Biol. Chem.
274
36505-36512
1999
Homo sapiens
Manually annotated by BRENDA team
Sun, S.; Albright, C.F.; Fish, B.H.; George, H.J.; Selling, B.H.; Hollis, G.F.; Wynn, R.
Expression, purification, and kinetic characterization of full-length human fibroblast activation protein
Protein Expr. Purif.
24
274-281
2002
Homo sapiens (Q12884), Homo sapiens
Manually annotated by BRENDA team
Iwasa, S.; Okada, K.; Chen, W.T.; Jin, X.; Yamane, T.; Ooi, A.; Mitsumata, M.
Increased expression of seprase, a membrane-type serine protease, is associated with lymph node metastasis in human colorectal cancer
Cancer Lett.
227
229-236
2005
Homo sapiens
Manually annotated by BRENDA team
Huang, Y.; Wang, S.; Kelly, T.
Seprase promotes rapid tumor growth and increased microvessel density in a mouse model of human breast cancer
Cancer Res.
64
2712-2716
2004
Homo sapiens
Manually annotated by BRENDA team
Ghersi, G.; Zhao, Q.; Salamone, M.; Yeh, Y.; Zucker, S.; Chen, W.T.
The protease complex consisting of dipeptidyl peptidase IV and seprase plays a role in the migration and invasion of human endothelial cells in collagenous matrices
Cancer Res.
66
4652-4661
2006
Homo sapiens
Manually annotated by BRENDA team
Acharya, P.S.; Zukas, A.; Chandan, V.; Katzenstein, A.L.; Pure, E.
Fibroblast activation protein: a serine protease expressed at the remodeling interface in idiopathic pulmonary fibrosis
Hum. Pathol.
37
352-360
2006
Homo sapiens
Manually annotated by BRENDA team
Aertgeerts, K.; Levin, I.; Shi, L.; Snell, G.P.; Jennings, A.; Prasad, G.S.; Zhang, Y.; Kraus, M.L.; Salakian, S.; Sridhar, V.; Wijnands, R.; Tennant, M.G.
Structural and kinetic analysis of the substrate specificity of human fibroblast activation protein alpha
J. Biol. Chem.
280
19441-19444
2005
Homo sapiens
Manually annotated by BRENDA team
Mori, Y.; Kono, K.; Matsumoto, Y.; Fujii, H.; Yamane, T.; Mitsumata, M.; Chen, W.T.
The expression of a type II transmembrane serine protease (Seprase) in human gastric carcinoma
Oncology
67
411-419
2004
Homo sapiens
Manually annotated by BRENDA team
Gilmore, B.F.; Lynas, J.F.; Scott, C.J.; McGoohan, C.; Martin, L.; Walker, B.
Dipeptide proline diphenyl phosphonates are potent, irreversible inhibitors of seprase (FAPalpha)
Biochem. Biophys. Res. Commun.
346
436-446
2006
Homo sapiens
Manually annotated by BRENDA team
Meadows, S.A.; Edosada, C.Y.; Mayeda, M.; Tran, T.; Quan, C.; Raab, H.; Wiesmann, C.; Wolf, B.B.
Ala657 and conserved active site residues promote fibroblast activation protein endopeptidase activity via distinct mechanisms of transition state stabilization
Biochemistry
46
4598-4605
2007
Homo sapiens (Q12884)
Manually annotated by BRENDA team
Aggarwal, S.; Brennen, W.N.; Kole, T.P.; Schneider, E.; Topaloglu, O.; Yates, M.; Cotter, R.J.; Denmeade, S.R.
Fibroblast activation protein peptide substrates identified from human collagen I derived gelatin cleavage sites
Biochemistry
47
1076-1086
2008
Homo sapiens
Manually annotated by BRENDA team
O'Brien, P.; O'Connor, B.F.
Seprase: An overview of an important matrix serine protease
Biochim. Biophys. Acta
1784
1130-1145
2008
Bos taurus, Gallus gallus, Mus musculus (P97321), Homo sapiens (Q12884), Xenopus laevis (Q91651)
Manually annotated by BRENDA team
Tran, T.; Quan, C.; Edosada, C.Y.; Mayeda, M.; Wiesmann, C.; Sutherlin, D.; Wolf, B.B.
Synthesis and structure-activity relationship of N-acyl-Gly-, N-acyl-Sar- and N-blocked-boroPro inhibitors of FAP, DPP4, and POP
Bioorg. Med. Chem. Lett.
17
1438-1442
2007
Homo sapiens (Q12884)
Manually annotated by BRENDA team
Lee, K.N.; Jackson, K.W.; Christiansen, V.J.; Lee, C.S.; Chun, J.; McKee, P.A.
Antiplasmin-cleaving enzyme is a soluble form of fibroblast activation protein
Blood
107
1397-1404
2006
Homo sapiens
Manually annotated by BRENDA team
Christiansen, V.J.; Jackson, K.W.; Lee, K.N.; McKee, P.A.
The effect of a single nucleotide polymorphism on human alpha 2-antiplasmin activity
Blood
109
5286-5292
2007
Homo sapiens
Manually annotated by BRENDA team
Ge, Y.; Zhan, F.; Barlogie, B.; Epstein, J.; Shaughnessy, J.J.; Yaccoby, S.
Fibroblast activation protein (FAP) is upregulated in myelomatous bone and supports myeloma cell survival
Br. J. Haematol.
133
83-92
2006
Homo sapiens (Q12884), Homo sapiens
Manually annotated by BRENDA team
Edosada, C.Y.; Quan, C.; Wiesmann, C.; Tran, T.; Sutherlin, D.; Reynolds, M.; Elliott, J.M.; Raab, H.; Fairbrother, W.; Wolf, B.B.
Selective inhibition of fibroblast activation protein protease based on dipeptide substrate specificity
J. Biol. Chem.
281
7437-7444
2006
Homo sapiens
Manually annotated by BRENDA team
Lee, K.N.; Jackson, K.W.; Terzyan, S.; Christiansen, V.J.; McKee,P.A.
Using substrate specificity of antiplasmin-cleaving enzyme for fibroblast activation protein inhibitor design
Biochemistry
48
5149-5158
2009
Homo sapiens (Q12884), Homo sapiens
Manually annotated by BRENDA team
Edosada, C.Y.; Quan, C.; Tran, T.; Pham, V.; Wiesmann, C.; Fairbrother, W.; Wolf, B.B.
Peptide substrate profiling defines fibroblast activation protein as an endopeptidase of strict Gly(2)-Pro(1)-cleaving specificity
FEBS Lett.
580
1581-1586
2006
Homo sapiens (Q12884)
Manually annotated by BRENDA team
Kennedy, A.; Dong, H.; Chen, D.; Chen, W.T.
Elevation of seprase expression and promotion of an invasive phenotype by collagenous matrices in ovarian tumor cells
Int. J. Cancer
124
27-35
2009
Homo sapiens (Q12884)
Manually annotated by BRENDA team
Goscinski, M.A.; Suo, Z.H.; Nesland, J.M.; Chen, W.T.; Zakrzewska, M.; Wang, J.; Zhang, S.; Florenes, V.A.; Giercksky, K.E.
Seprase, dipeptidyl peptidase IV and urokinase-type plasminogen activator expression in dysplasia and invasive squamous cell carcinoma of the esophagus. A study of 229 cases from Anyang Tumor Hospital, Henan Province, China
Oncology
75
49-59
2008
Homo sapiens (Q12884)
Manually annotated by BRENDA team
Mentlein, R.; Hattermann, K.; Hemion, C.; Jungbluth, A.; Held-Feindt, J.
Expression and role of the cell surface protease seprase/fibroblast activation protein-alpha (FAP-alpha) in astroglial tumors
Biol. Chem.
392
199-207
2011
Homo sapiens
Manually annotated by BRENDA team
Keane, F.; Nadvi, N.; Yao, T.; Gorrell, M.
Neuropeptide Y, B-type natriuretic peptide, substance P and peptide YY are novel substrates of fibroblast activation protein-alpha
FEBS J.
278
1316-1332
2011
Homo sapiens (Q12884)
Manually annotated by BRENDA team
Lee, K.; Jackson, K.; Christiansen, V.; Dolence, E.; Mckee, P.
Enhancement of fibrinolysis by inhibiting enzymatic cleavage of precursor alpha2-antiplasmin
J. Thromb. Haemost.
9
987-996
2011
Homo sapiens
Manually annotated by BRENDA team
Yang, L.; Ma, L.; Lai, D.
Over-expression of fibroblast activation protein alpha increases tumor growth in xenografts of ovarian cancer cells
Acta Biochim. Biophys. Sin. (Shanghai)
45
928-937
2013
Homo sapiens (Q12844)
Manually annotated by BRENDA team
Jia, J.; Martin, T.A.; Ye, L.; Jiang, W.G.
FAP-alpha (fibroblast activation protein-alpha) is involved in the control of human breast cancer cell line growth and motility via the FAK pathway
BMC Cell Biol.
15
16
2014
Homo sapiens (Q12844)
Manually annotated by BRENDA team
Yang, W.; Han, W.; Ye, S.; Liu, D.; Wu, J.; Liu, H.; Li, C.; Chen, H.
Fibroblast activation protein-alpha promotes ovarian cancer cell proliferation and invasion via extracellular and intracellular signaling mechanisms
Exp. Mol. Pathol.
95
105-110
2013
Homo sapiens (Q12844)
Manually annotated by BRENDA team
Jambunathan, K.; Watson, D.S.; Endsley, A.N.; Kodukula, K.; Galande, A.K.
Comparative analysis of the substrate preferences of two post-proline cleaving endopeptidases, prolyl oligopeptidase and fibroblast activation protein alpha
FEBS Lett.
586
2507-2512
2012
Homo sapiens (Q12844), Homo sapiens
Manually annotated by BRENDA team
Keane, F.M.; Yao, T.W.; Seelk, S.; Gall, M.G.; Chowdhury, S.; Poplawski, S.E.; Lai, J.H.; Li, Y.; Wu, W.; Farrell, P.; Vieira de Ribeiro, A.J.; Osborne, B.; Yu, D.M.; Seth, D.; Rahman, K.; Haber, P.; Topaloglu, A.K.; Wang, C.; Thomson, S.; Hennessy, A.; Prins, J.; Twigg, S.M.; McLennan, S.V.; McCaughan, G.W.; Ba, B.a.c.
Quantitation of fibroblast activation protein (FAP)-specific protease activity in mouse, baboon and human fluids and organs
FEBS open bio
4
43-54
2013
Papio sp., Mus musculus (P97321), Mus musculus, Homo sapiens (Q12844), Homo sapiens
Manually annotated by BRENDA team
Jansen, K.; De Winter, H.; Heirbaut, L.; Cheng, J.; Joossens, J.; Lambeir, A.; De Meester, I.; Augustyns, K.; Van Der Veken, P.
Selective inhibitors of fibroblast activation protein (FAP) with a xanthine scaffold
MedChemComm
5
1700-1707
2013
Homo sapiens (Q12844)
-
Manually annotated by BRENDA team
Knopf, J.D.; Tholen, S.; Koczorowska, M.M.; De Wever, O.; Biniossek, M.L.; Schilling, O.
The stromal cell-surface protease fibroblast activation protein-alpha localizes to lipid rafts and is recruited to invadopodia
Biochim. Biophys. Acta
1853
2515-2525
2015
Homo sapiens
Manually annotated by BRENDA team
Liu, J.; Huang, C.; Peng, C.; Xu, F.; Li, Y.; Yutaka, Y.; Xiong, B.; Yang, X.
Stromal fibroblast activation protein alpha promotes gastric cancer progression via epithelial-mesenchymal transition through Wnt/ beta-catenin pathway
BMC Cancer
18
1099
2018
Homo sapiens
Manually annotated by BRENDA team
Lv, B.; Xie, F.; Zhao, P.; Ma, X.; Jiang, W.; Yu, J.; Zhang, X.; Jia, J.
Promotion of cellular growth and motility is independent of enzymatic activity of fibroblast activation protein-alpha
Cancer Genomics Proteomics
13
201-208
2016
Homo sapiens
Manually annotated by BRENDA team
Bracke, A.; Van Elzen, R.; Van Der Veken, P.; Augustyns, K.; De Meester, I.; Lambeir, A.M.
The development and validation of a combined kinetic fluorometric activity assay for fibroblast activation protein alpha and prolyl oligopeptidase in plasma
Clin. Chim. Acta
495
154-160
2019
Homo sapiens
Manually annotated by BRENDA team
Busek, P.; Hrabal, P.; Fric, P.; Sedo, A.
Co-expression of the homologous proteases fibroblast activation protein and dipeptidyl peptidase-IV in the adult human Langerhans islets
Histochem. Cell Biol.
143
497-504
2015
Homo sapiens
-
Manually annotated by BRENDA team
Jia, J.; Martin, T.A.; Ye, L.; Meng, L.; Xia, N.; Jiang, W.G.; Zhang, X.
Fibroblast activation protein-alpha promotes the growth and migration of lung cancer cells via the PI3K and sonic hedgehog pathways
Int. J. Mol. Med.
41
275-283
2018
Homo sapiens
Manually annotated by BRENDA team
Gunderson, A.; Yamazaki, T.; McCarty, K.; Phillips, M.; Alice, A.; Bambina, S.; Zebertavage, L.; Friedman, D.; Cottam, B.; Newell, P.; Gough, M.; Crittenden, M.; Van der Veken, P.; Young, K.
Blockade of fibroblast activation protein in combination with radiation treatment in murine models of pancreatic adenocarcinoma
PLoS ONE
14
e0211117
2019
Homo sapiens
Manually annotated by BRENDA team
Busek, P.; Balaziova, E.; Matrasova, I.; Hilser, M.; Tomas, R.; Syrucek, M.; Zemanova, Z.; Krepela, E.; Belacek, J.; Sedo, A.
Fibroblast activation protein alpha is expressed by transformed and stromal cells and is associated with mesenchymal features in glioblastoma
Tumour Biol.
37
13961-13971
2016
Homo sapiens
Manually annotated by BRENDA team