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Information on EC 3.4.21.B28 - fibroblast activation protein alpha subunit
for references in articles please use BRENDA:EC3.4.21.B28
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preliminary BRENDA-supplied EC number
EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.21 Serine endopeptidases
3.4.21.B28 fibroblast activation protein alpha subunit
The expected taxonomic range for this enzyme is: Tetrapoda
- 3.4.21.B28
- polyposis
-
adenomatous
- colorectal
- apc
- polyneuropathy
- adenoma
- polyp
-
amyloid
-
amyloidotic
- transthyretin
- hereditary
-
germline
-
colectomy
-
surveillance
-
endoscopic
- bowel
- desmoids
-
anastomosis
- abdominal
-
proctocolectomy
- duodenal
- ileal
-
prophylactic
-
pouch
-
extracolonic
-
amyloidogenic
-
ileostomy
-
val30met
- rectum
-
gardner
-
colonoscopy
-
pouch-anal
-
hnpcc
- sulindac
-
pancreaticoduodenectomy
- amyloidoses
-
hamartomatous
-
periampullary
-
lynch
-
ampullary
- diagnostics
-
mutyh
-
domino
-
polypectomy
-
tafamidis
-
fundic
-
adenoma-carcinoma
-
prealbumin
-
peutz-jeghers
- medicine
- fibromatosis
- nonpolyposis
Reaction Schemes
showfibroblast 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
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
antiplasmin-cleaving enzyme
APCE
FAP
FAP-alpha
FAP-specific protease
FAPalpha
fibroblast activation protein
fibroblast activation protein alpha
fibroblast activation protein-alpha
fibroblast activation protein-specific protease
seprase
surface expressed protease
antiplasmin-cleaving enzyme
-
soluble form of 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
-
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
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
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
member of the group type II integral serine proteases, subfamily S9b, with gelatinase and N-terminal post-prolyl amino peptidase activities
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REACTION
REACTION DIAGRAM
COMMENTARY
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
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
Arg is optimal at position P7. Peptide cleavage rate increases with Arg in position P6
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
besides glycine, fibroblast activation protein tolerates substrates with D-Ala and D-Ser at P2. Fibroblast activation protein prefers small, uncharged amino acids at P3, but tolerates most amino acids at P4, P1' and P2'
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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cleavage of C-N-linkage
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY
352031-63-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
7-methoxycoumarin-4-acetic acid-APGSKGDA-dinitrophenyl + H2O
?
-
Substrates: -
Products: -
Products: -
?
7-methoxycoumarin-4-acetic acid-ASGPAGPA-dinitrophenyl + H2O
?
-
Substrates: -
Products: -
Products: -
?
7-methoxycoumarin-4-acetic acid-DKGESGPA-dinitrophenyl + H2O
?
-
Substrates: -
Products: -
Products: -
?
7-methoxycoumarin-4-acetic acid-DRGETGP-dinitrophenyl + H2O
?
-
Substrates: -
Products: -
Products: -
?
7-methoxycoumarin-4-acetic acid-DRGETGPA-dinitrophenyl + H2O
?
-
Substrates: -
Products: -
Products: -
?
7-methoxycoumarin-4-acetic acid-DSGETGP-dinitrophenyl + H2O
?
-
Substrates: -
Products: -
Products: -
?
7-methoxycoumarin-4-acetic acid-DSGETGPA-dinitrophenyl + H2O
?
-
Substrates: -
Products: -
Products: -
?
7-methoxycoumarin-4-acetic acid-EPGPPGPA-dinitrophenyl + H2O
?
-
Substrates: -
Products: -
Products: -
?
7-methoxycoumarin-4-acetic acid-ERGETGPA-dinitrophenyl + H2O
?
-
Substrates: -
Products: -
Products: -
?
7-methoxycoumarin-4-acetic acid-ERGETGPAG-dinitrophenyl + H2O
?
-
Substrates: -
Products: -
Products: -
?
7-methoxycoumarin-4-acetic acid-ERGETGPAGG-dinitrophenyl + H2O
?
-
Substrates: -
Products: -
Products: -
?
7-methoxycoumarin-4-acetic acid-ERGETGPSG-dinitrophenyl + H2O
?
-
Substrates: -
Products: -
Products: -
?
7-methoxycoumarin-4-acetic acid-VGPAGK-dinitrophenyl + H2O
?
-
Substrates: -
Products: -
Products: -
?
acetyl-D-Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
acetyl-D-Ala-Pro + 7-amino-4-trifluoromethylcoumarin
Substrates: -
Products: -
Products: -
?
acetyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
acetyl-Gly-Pro + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin + H2O
acetyl-Gly-Pro-7-amino-4-trifluoromethylcoumarin
Substrates: -
Products: -
Products: -
?
acetyl-Gly-Pro-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate + H2O
acetyl-Gly-Pro + 9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate
-
Substrates: -
Products: -
Products: -
?
acetyl-Gly-Pro-Gly-Pro-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate + H2O
acetyl-Gly-Pro-Gly-Pro + 9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate
-
Substrates: most efficient substrate, FAP shows a greater catalytic efficiency for acetyl-Gly-Pro-Gly-Pro-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate than for acetyl-Gly-Pro-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate and TSGP-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate
Products: -
Products: -
?
Ala-Pro-4-trifluoromethylcoumarin-7-amide + H2O
Ala-Pro + 7-amino-4-trifluoromethylcoumarin
Ala-Pro-4-trifluoromethylcoumarin-7-amide + H2O
Ala-Pro-4 + 7-amino-4-trifluoromethylcoumarin
-
Substrates: -
Products: -
Products: -
?
Ala-Pro-7-amido-4-methylcoumarin + H2O
Ala-Pro + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Ala-Pro + 7-amino-4-trifluoromethylcoumarin
-
Substrates: -
Products: -
Products: -
?
Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Ala-Pro + 7-amino-4-trifluoromethylcoumarin + H2O
-
Substrates: -
Products: -
Products: -
?
Ala-Pro-Ala-Pro-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate + H2O
Ala-Pro-Ala-Pro + 9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate
-
Substrates: -
Products: -
Products: -
?
Ala-Ser-Gly-Pro-Asn-Gln + H2O
Ala-Ser-Gly-Pro + Asn-Gln
Substrates: -
Products: -
Products: -
?
Ala-Ser-Gly-Pro-Ser-Ser + H2O
Ala-Ser-Gly-Pro + Ser-Ser
Substrates: -
Products: -
Products: -
?
alpha2-antiplasmin + H2O
truncated alpha2-antiplasmin + Met
-
Substrates: -
Products: cleaves Met from the N-terminus yielding Asn as the N-terminal amino acid
Products: 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
-
Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
Arg-Pro-7-amido-4-methylcoumarin + H2O
Arg-Pro + 7-amino-4-methylcoumarin
-
Substrates: preferred substrate
Products: -
Products: -
?
ARI-3144-amido-4-methylcoumarin + H2O
ARI-3144 + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
B-type natriuretic peptide + H2O
?
Substrates: efficiently hydrolysed and mostly preferred substrate
Products: -
Products: -
?
benzyloxycarbonyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-L-Pro + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Gly-Pro-7-amido-4-methyl-3-carbamoylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro + 7-amino-4-methyl-3-carbamoylcoumarin
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro + 7-amino-4-methylcoumarin
biotinyl-Gly-Pro-7-amido-4-methyl-3-carbamoylcoumarin + H2O
biotinyl-Gly-Pro + 7-amino-4-methyl-3-carbamoylcoumarin
-
Substrates: -
Products: -
Products: -
?
Boc-Ala-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
Boc-Ala-Gly-Pro-Arg + 7-amino-4-methylcoumarin
Boc-Gly-Pro-aminoluciferin + H2O
Boc-Gly-Pro + aminoluciferin
Substrates: -
Products: -
Products: -
?
complement C1q tumor necrosis factor-related protein 6 + H2O
?
-
Substrates: cleavage at position 26 after a Val-Pro sequence
Products: -
Products: -
?
CXCL-5 + H2O
?
-
Substrates: processing of CXCL-5 at position 42, which is after an Ala-Pro sequence
Products: -
Products: -
?
D-Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
D-Ala-Pro + 7-amino-4-trifluoromethylcoumarin
Substrates: -
Products: -
Products: -
?
extracellular matrix protein 1 + H2O
?
-
Substrates: cleavage occurrs at position 142 after a Lys-Pro sequence
Products: -
Products: -
?
fibrillin-2 + H2O
?
-
Substrates: cleavage occurrs at position 60, in the propeptide domain, after a Gly-Pro sequence
Products: -
Products: -
?
Gln-Pro-7-amido-4-methylcoumarin + H2O
Gln-Pro + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Glu-Pro-7-amido-4-methylcoumarin + H2O
Glu-Pro + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
glucagon-like peptide-1 + H2O
?
Substrates: slow hydrolysis
Products: -
Products: -
?
glucose-dependent insulinotropic peptide + H2O
?
Substrates: slow hydrolysis
Products: -
Products: -
?
Gly-Pro-4-trifluoromethylcoumarin-7-amide + H2O
Gly-Pro + 7-amino-4-trifluoromethylcoumarin
-
Substrates: -
Products: -
Products: -
?
Gly-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Gly-Pro + 7-amino-4-trifluoromethylcoumarin
Gly-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Gly-Pro + 7-amino-4-trifluoromethylcoumarin + H2O
Substrates: -
Products: -
Products: -
?
Ile-Pro-7-amido-4-methylcoumarin + H2O
Ile-Pro + 7-amino-4-methylcoumarin
-
Substrates: most preferred substrate
Products: -
Products: -
?
Ile-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Ile-Pro + 7-amino-4-trifluoromethylcoumarin
-
Substrates: -
Products: -
Products: -
?
L-Ala-L-Pro-7-amido-4-methylcoumarin + H2O
L-Ala-L-Pro + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
L-Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
L-Ala-Pro + 7-amino-4-trifluoromethylcoumarin
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
?
Substrates: FRET-peptide
Products: -
Products: -
?
Leu-Pro-7-amido-4-methylcoumarin + H2O
Leu-Pro + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Lys-Ala-7-amido-4-trifluoromethylcoumarin + H2O
Lys-Ala + 7-amino-4-trifluoromethylcoumarin
-
Substrates: -
Products: -
Products: -
?
Lys-Pro-4-trifluoromethylcoumarin-7-amide + H2O
Lys-Pro + 7-amino-4-trifluoromethylcoumarin
-
Substrates: -
Products: -
Products: -
?
Lys-Pro-7-amido-4-methylcoumarin + H2O
Lys-Pro + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
lysyl oxidase homolog 2 + H2O
?
-
Substrates: cleavage at position 36 after a Tyr-Pro sequence that follows the signal peptide
Products: -
Products: -
?
MEPLGRQLTSGP-7-amido-4-methylcoumarin + H2O
MEPLGRQLTSGP + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
MEPLGWQLTSGP-7-amido-4-methylcoumarin + H2O
MEPLGWQLTSGP + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
Met-Pro-7-amido-4-methylcoumarin + H2O
Met-Pro + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
N-benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-Gly-Pro + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
N-benzyloxycarbonyl-Gly-Pro-Ala + H2O
N-benzyloxycarbonyl-Gly-Pro + L-Ala
-
Substrates: -
Products: -
Products: -
?
N-benzyloxycarbonyl-Gly-Pro-Glu + H2O
N-benzyloxycarbonyl-Gly-Pro + L-Glu
-
Substrates: -
Products: -
Products: -
?
N-benzyloxycarbonyl-Gly-Pro-His + H2O
N-benzyloxycarbonyl-Gly-Pro + L-His
-
Substrates: -
Products: -
Products: -
?
N-benzyloxycarbonyl-Gly-Pro-Leu + H2O
N-benzyloxycarbonyl-Gly-Pro + L-Leu
-
Substrates: -
Products: -
Products: -
?
N-benzyloxycarbonyl-Gly-Pro-Met + H2O
N-benzyloxycarbonyl-Gly-Pro + L-Met
-
Substrates: -
Products: -
Products: -
?
N-benzyloxycarbonyl-Gly-Pro-Met-His + H2O
N-benzyloxycarbonyl-Gly-Pro + Met-His
-
Substrates: -
Products: -
Products: -
?
N-benzyloxycarbonyl-Gly-Pro-Met-His-Arg-Ser + H2O
N-benzyloxycarbonyl-Gly-Pro + Met-His-Arg-Ser
-
Substrates: -
Products: -
Products: -
?
N-benzyloxycarbonyl-Gly-Pro-Phe + H2O
N-benzyloxycarbonyl-Gly-Pro + L-Phe
-
Substrates: -
Products: -
Products: -
?
N-benzyloxycarbonyl-Gly-Pro-Phe-His + H2O
N-benzyloxycarbonyl-Gly-Pro + L-Phe-L-His
-
Substrates: -
Products: -
Products: -
?
N-benzyloxycarbonyl-Gly-Pro-Phe-His-Arg + H2O
N-benzyloxycarbonyl-Gly-Pro + Phe-His-Arg
-
Substrates: -
Products: -
Products: -
?
N-benzyloxycarbonyl-Gly-Pro-Phe-His-Arg-Ser + H2O
N-benzyloxycarbonyl-Gly-Pro + Phe-His-Arg-Ser
-
Substrates: -
Products: -
Products: -
?
N-benzyloxycarbonyl-Gly-Pro-Ser + H2O
N-benzyloxycarbonyl-Gly-Pro + L-Ser
-
Substrates: -
Products: -
Products: -
?
N-benzyloxycarbonyl-Gly-Pro-Tyr + H2O
N-benzyloxycarbonyl-Gly-Pro + L-Tyr
-
Substrates: -
Products: -
Products: -
?
N-carbobenzyloxy-Gly-Pro-aminoluciferin + H2O
N-carbobenzyloxy-Gly-Pro + aminoluciferin
Substrates: -
Products: -
Products: -
?
N-formyl-Gly-Pro-7-amido-4-methyl-3-carbamoylcoumarin + H2O
N-formyl-Gly-Pro + 7-amino-4-methyl-3-carbamoylcoumarin
-
Substrates: -
Products: -
Products: -
?
N-methyl-Gly-Pro-7-amido-4-methyl-3-carbamoylcoumarin + H2O
N-methyl-Gly-Pro + 7-amino-4-methyl-3-carbamoylcoumarin
-
Substrates: -
Products: -
Products: -
?
neuropeptide Y + H2O
?
Substrates: efficiently hydrolysed and mostly preferred substrate
Products: -
Products: -
?
peptide YY + H2O
?
Substrates: efficiently hydrolysed substrate
Products: -
Products: -
?
Phe-Pro-7-amido-4-methylcoumarin + H2O
Phe-Pro + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Phe-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Phe-Pro + 7-amino-4-trifluoromethylcoumarin
-
Substrates: -
Products: -
Products: -
?
precursor Met-alpha2-antiplasmin + H2O
L-Asn-alpha2-antiplasmin + ?
-
Substrates: the enzyme cleaves between Pro12 and Asn13
Products: -
Products: -
?
Pro-Pro-7-amido-4-methylcoumarin + H2O
Pro-Pro + 7-amino-4-methylcoumarin
-
Substrates: preferred substrate
Products: -
Products: -
?
RPKPQQFFGLM + H2O
RPKP + L-Gln-L-Gln + FFGLM
Substrates: the substance P-derived sequence is cleaved although it does not contain Gly-Pro
Products: -
Products: -
?
Ser-Pro-7-amido-4-methylcoumarin + H2O
Ser-Pro + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Substance P + H2O
?
Substrates: efficiently hydrolysed substrate
Products: -
Products: -
?
Suc-Ala-Pro-7-amido-4-methylcoumarin + H2O
Suc-Ala-Pro + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
Thr-Ala-Gly-Pro-Asn-Gln + H2O
Thr-Ala-Gly-Pro + Asn-Gln
Substrates: -
Products: -
Products: -
?
Thr-Pro-7-amido-4-methylcoumarin + H2O
Thr-Pro + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Thr-Ser-Gly-Pro-Asn-Gln + H2O
Thr-Ser-Gly-Pro + Asn-Gln
Substrates: -
Products: -
Products: -
?
Thr-Ser-Gly-Pro-Asn-Ser + H2O
Thr-Ser-Gly-Pro + Asn-Ser
Substrates: -
Products: -
Products: -
?
Thr-Ser-Gly-Pro-Ser-Gln + H2O
Thr-Ser-Gly-Pro + Ser-Gln
Substrates: -
Products: -
Products: -
?
TSGP-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate + H2O
TSGP + 9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate
-
Substrates: -
Products: -
Products: -
?
Tyr-Pro-7-amido-4-methylcoumarin + H2O
Tyr-Pro + 7-amino-4-methylcoumarin
-
Substrates: -
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?
Val-Pro-7-amido-4-methylcoumarin + H2O
Val-Pro + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
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?
Z-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
Z-Gly-L-Pro + 7-amino-4-methylcoumarin
Substrates: -
Products: -
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?
Ala-Pro-4-trifluoromethylcoumarin-7-amide + H2O
Ala-Pro + 7-amino-4-trifluoromethylcoumarin
Substrates: -
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?
Ala-Pro-4-trifluoromethylcoumarin-7-amide + H2O
Ala-Pro + 7-amino-4-trifluoromethylcoumarin
-
Substrates: -
Products: -
Products: -
?
alpha2-antiplasmin + H2O
?
Substrates: alpha2-antiplasmin is cleaved N-terminally to Asn-alpha2-antiplasmin that is rapidly cross-linked to fibrin and protects it from digestion by plasmin
Products: -
Products: -
?
alpha2-antiplasmin + H2O
?
Substrates: alpha2-antiplasmin is cleaved N-terminally at Pro12-Asn13 to Asn-alpha2-antiplasmin that is rapidly cross-linked to fibrin and protects it from digestion by plasmin
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Products: -
?
alpha2-antiplasmin + H2O
?
Substrates: efficiently hydrolysed substrate
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Products: -
?
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro + 7-amino-4-methylcoumarin
-
Substrates: -
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Products: -
?
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Boc-Ala-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
Boc-Ala-Gly-Pro-Arg + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
Boc-Ala-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
Boc-Ala-Gly-Pro-Arg + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
Boc-Ala-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
Boc-Ala-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Collagen + H2O
?
-
Substrates: cleavage of type I collagen by fibroblast activation protein-? enhances class A scavenger receptor mediated macrophage adhesion
Products: -
Products: -
?
Gelatin + H2O
?
-
Substrates: gelatin cleavage results in 51 fragments
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?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
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?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
Substrates: -
Products: -
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?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
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?
Gly-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Gly-Pro + 7-amino-4-trifluoromethylcoumarin
-
Substrates: -
Products: -
Products: -
?
Gly-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Gly-Pro + 7-amino-4-trifluoromethylcoumarin
Substrates: -
Products: -
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?
Gly-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Gly-Pro + 7-amino-4-trifluoromethylcoumarin
-
Substrates: -
Products: -
Products: -
?
Gly-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Gly-Pro + 7-amino-4-trifluoromethylcoumarin
Substrates: -
Products: -
Products: -
?
L-Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
L-Ala-Pro + 7-amino-4-trifluoromethylcoumarin
Substrates: -
Products: -
Products: -
?
L-Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
L-Ala-Pro + 7-amino-4-trifluoromethylcoumarin
-
Substrates: -
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Products: -
?
L-Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
L-Ala-Pro + 7-amino-4-trifluoromethylcoumarin
Substrates: -
Products: -
Products: -
?
Met-alpha2-antiplasmin + H2O
?
-
Substrates: 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
Products: -
Products: -
?
Met-alpha2-antiplasmin + H2O
?
-
Substrates: 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
Products: -
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?
additional information
?
-
-
Substrates: no hydrolysis of Pro-7-amino-4-methylcoumarin, Gly-Pro-7-amino-4-methylcoumarin, Ala-Pro-7-amino-4-methylcoumarin, pGly-His-Pro-7-amino-4-methylcoumarin, N-benzyloxycarbonyl-Pro-Phe, Gly-Gly-Pro-Ala and N-benzyloxycarbonyl-Gly-Leu-Phe-His
Products: -
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?
additional information
?
-
Substrates: glycosylated form has both postprolyl depeptidyl peptidase and postgelatinase activity, nonglycosylated isoform has no detectable gelatinase activity
Products: -
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?
additional information
?
-
-
Substrates: glycosylated form has both postprolyl depeptidyl peptidase and postgelatinase activity, nonglycosylated isoform has no detectable gelatinase activity
Products: -
Products: -
?
additional information
?
-
Substrates: may contribute to invasiveness in malignant cancers
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?
additional information
?
-
-
Substrates: cleaves alpha2-antiplasmin with Arg as the sixth amino acid approximately 8fold faster than alpha2-antiplasmin with Trp at this position
Products: -
Products: -
?
additional information
?
-
-
Substrates: shows very weak activity against acetyl-Ser-Pro-7-amido-4-methylcoumarin, Asp-Pro-7-amido-4-methylcoumarin, His-Pro-7-amido-4-methylcoumarin and Asn-Pro-7-amido-4-methylcoumarin, does not cleave succinyl-Gly-Pro-7-amido-4-methyl-3-carbamoylcoumarin, Gly-Ala-7-amido-4-methylcoumarin, acetyl-Ala-Pro-7-amido-4-methylcoumarin, acetyl-Asp-Pro-7-amido-4-methylcoumarin, acetyl-Glu-Pro-7-amido-4-methylcoumarin, acetyl-Phe-Pro-7-amido-4-methylcoumarin, acetyl-His-Pro-7-amido-4-methylcoumarin, acetyl-Ile-Pro-7-amido-4-methylcoumarin, acetyl-Lys-Pro-7-amido-4-methylcoumarin, acetyl-Leu-Pro-7-amido-4-methylcoumarin, acetyl-Met-Pro-7-amido-4-methylcoumarin, acetyl-Asn-Pro-7-amido-4-methylcoumarin, acetyl-Pro-Pro-7-amido-4-methylcoumarin, acetyl-Gln-Pro-7-amido-4-methylcoumarin, acetyl-Arg-Pro-7-amido-4-methylcoumarin, acetyl-Thr-Pro-7-amido-4-methylcoumarin, acetyl-Val-Pro-7-amido-4-methylcoumarin, and acetyl-Tyr-Pro-7-amido-4-methylcoumarin
Products: -
Products: -
?
additional information
?
-
Substrates: FAP cleavage of peptide libraries of short amino acid sequences surrounding the scissile bond (-Pro12-Asn13-) indicates that Gly is required at position P2 and Pro is required at position P1. Arg is optimal at position P7. Peptide cleavage rate increases with Arg in position P6. Placing Arg in P4 or P8 reduces cleavage rates dramatically
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?
additional information
?
-
-
Substrates: FAP cleavage of peptide libraries of short amino acid sequences surrounding the scissile bond (-Pro12-Asn13-) indicates that Gly is required at position P2 and Pro is required at position P1. Arg is optimal at position P7. Peptide cleavage rate increases with Arg in position P6. Placing Arg in P4 or P8 reduces cleavage rates dramatically
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?
additional information
?
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Substrates: fibroblast activation protein requires substrates with Pro at P1 and Gly or D-amino acids at P2. Besides glycine, fibroblast activation protein tolerates substrates with D-Ala and D-Ser at P2. Fibroblast activation protein prefers small, uncharged amino acids at P3, but tolerates most amino acids at P4, P1' and P2'
Products: -
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?
additional information
?
-
-
Substrates: FAP-alpha is an endopeptidase cleaving large protein with Gly(2)-Pro(1)-cleaving specificity
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?
additional information
?
-
-
Substrates: does not cleave native human collagens, fibronectin or laminin
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?
additional information
?
-
Substrates: the enzyme acts as both a dipeptidyl peptidase and an endopeptidyl peptidase
Products: -
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?
additional information
?
-
Substrates: does not hydrolyze succinyl-L-Ala-L-Pro-7-amido-4-methylcoumarin and H-Gly-Pro-7-amido-4-methylcoumarin
Products: -
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?
additional information
?
-
Substrates: a post-proline cleaving serine peptidase
Products: -
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?
additional information
?
-
-
Substrates: a post-proline cleaving serine peptidase
Products: -
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?
additional information
?
-
Substrates: the enzyme exhibits post-proline cleaving dipeptidyl peptidase and endopeptidase activity toward gelatin and alpha2-antiplasmin. Substrate specificity analysis using a internally quenched fluorogenic probes library for screening, overview. The sequence Pro-Tyr-Asp is strongly cleaved by the enzyme, sequence specificity, detailed overview
Products: -
Products: -
?
additional information
?
-
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Substrates: the enzyme exhibits post-proline cleaving dipeptidyl peptidase and endopeptidase activity toward gelatin and alpha2-antiplasmin. Substrate specificity analysis using a internally quenched fluorogenic probes library for screening, overview. The sequence Pro-Tyr-Asp is strongly cleaved by the enzyme, sequence specificity, detailed overview
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is a is a prolyl specific serine protease
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?
additional information
?
-
-
Substrates: shows no activity with Gly-Pro-Gly-Pro-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate
Products: -
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?
additional information
?
-
-
Substrates: the enzyme has both dipeptidyl aminopeptidase and endopeptidase activities, and can hydrolyze the post-proline bond
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
B-type natriuretic peptide + H2O
?
Substrates: efficiently hydrolysed and mostly preferred substrate
Products: -
Products: -
?
Collagen + H2O
?
-
Substrates: cleavage of type I collagen by fibroblast activation protein-? enhances class A scavenger receptor mediated macrophage adhesion
Products: -
Products: -
?
complement C1q tumor necrosis factor-related protein 6 + H2O
?
-
Substrates: cleavage at position 26 after a Val-Pro sequence
Products: -
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?
CXCL-5 + H2O
?
-
Substrates: processing of CXCL-5 at position 42, which is after an Ala-Pro sequence
Products: -
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?
extracellular matrix protein 1 + H2O
?
-
Substrates: cleavage occurrs at position 142 after a Lys-Pro sequence
Products: -
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?
fibrillin-2 + H2O
?
-
Substrates: cleavage occurrs at position 60, in the propeptide domain, after a Gly-Pro sequence
Products: -
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?
glucagon-like peptide-1 + H2O
?
Substrates: slow hydrolysis
Products: -
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?
glucose-dependent insulinotropic peptide + H2O
?
Substrates: slow hydrolysis
Products: -
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?
lysyl oxidase homolog 2 + H2O
?
-
Substrates: cleavage at position 36 after a Tyr-Pro sequence that follows the signal peptide
Products: -
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?
Met-alpha2-antiplasmin + H2O
?
-
Substrates: 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
Products: -
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?
neuropeptide Y + H2O
?
Substrates: efficiently hydrolysed and mostly preferred substrate
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?
peptide YY + H2O
?
Substrates: efficiently hydrolysed substrate
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?
Substance P + H2O
?
Substrates: efficiently hydrolysed substrate
Products: -
Products: -
?
alpha2-antiplasmin + H2O
?
Substrates: alpha2-antiplasmin is cleaved N-terminally to Asn-alpha2-antiplasmin that is rapidly cross-linked to fibrin and protects it from digestion by plasmin
Products: -
Products: -
?
alpha2-antiplasmin + H2O
?
Substrates: efficiently hydrolysed substrate
Products: -
Products: -
?
Gelatin + H2O
?
-
Substrates: gelatin cleavage results in 51 fragments
Products: -
Products: -
?
additional information
?
-
Substrates: may contribute to invasiveness in malignant cancers
Products: -
Products: -
?
additional information
?
-
Substrates: a post-proline cleaving serine peptidase
Products: -
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?
additional information
?
-
-
Substrates: a post-proline cleaving serine peptidase
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has both dipeptidyl aminopeptidase and endopeptidase activities, and can hydrolyze the post-proline bond
Products: -
Products: -
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(S)-N-(2-(2-cyano-4,4-difluoropyrrolidin-1-yl)-2-oxoethyl)quinoline-4-carboxamide
-
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-(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
-
4-(2-aminoethyl)-benzenesulfonyl fluoride hydrochloride
AEBSF, inhibition at 5 mM
4-(2-oxo[(2S)-1-[N-(quinoline-4-carbonyl)glycyl]pyrrolidin-2-yl]acetamido)benzoic acid
-
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
N-(2-[(2S)-2-[[[(3,4-dimethoxyphenyl)methyl]amino](oxo)acetyl]pyrrolidin-1-yl]-2-oxoethyl)quinoline-4-carboxamide
-
N-(2-[(2S)-2-[[[(3-methoxyphenyl)methyl]amino](oxo)acetyl]pyrrolidin-1-yl]-2-oxoethyl)quinoline-4-carboxamide
-
N-(2-[(2S)-2-[[[(4-methoxyphenyl)methyl]amino](oxo)acetyl]pyrrolidin-1-yl]-2-oxoethyl)quinoline-4-carboxamide
-
N-(2-[(2S)-2-[[[2-(3,4-dimethoxyphenyl)ethyl]amino](oxo)acetyl]pyrrolidin-1-yl]-2-oxoethyl)quinoline-4-carboxamide
-
N-(2-[(2S)-2-[[[2-(morpholin-4-yl)-2-oxoethyl]amino](oxo)acetyl]pyrrolidin-1-yl]-2-oxoethyl)quinoline-4-carboxamide
-
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
-
N-[2-[(2R)-2-(dihydroxyboranyl)pyrrolidin-1-yl]-2-oxoethyl]-9-N-methyl-5-oxoprolinamide
-
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
-
tert-butyl N-(oxo[(2S)-1-[N-(quinoline-4-carbonyl)glycyl]pyrrolidin-2-yl]acetyl)glycinate
-
[(2R)-1-[(1-oxo-1,3-dihydro-2H-isoindol-2-yl)acetyl]pyrrolidin-2-yl]-9-boronic acid
-
[(2R)-1-[N-(2,2-dimethylpropanoyl)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
-
additional information
-
not inhibited by JTP-4819, Fmoc-Ala-pyrrCN and N-benzyloxycarbonyl-Phe-Pro-BT
-
additional information
synthesis and inhibitory potencies of selective enzyme inhibitors from a xanthine scaffold, structure-activity relationship analysis using the crystal structures of enzyme complxed with inhibitors, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.026 - 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
0.0008
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
0.106
Ile-Pro-7-amido-4-trifluoromethylcoumarin
-
at 23°C in 50 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, pH 7.4
0.029
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
0.189
Lys-Ala-7-amido-4-trifluoromethylcoumarin
-
at 23°C in 50 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, pH 7.4
0.245
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
0.087
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657N, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.1
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.14
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203D/E204D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.33
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
wild type enzyme, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.42
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657T, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.43
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657V, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.48
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme R123K, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.51
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E204D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.52
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657S, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.57
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203A/E204A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.65
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme R123M, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.67
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme R123A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.69
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E204A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.74
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E204Q, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.78
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.81
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.84
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme Y656F, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657Q, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1.3
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme N704A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1.3
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657F, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1.4
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203Q/E204Q, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
2
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657G, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
2.3
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203Q, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.244
Ala-Pro-7-amido-4-trifluoromethylcoumarin
-
at 23°C in 50 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, pH 7.4
0.026
Arg-Lys(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-Gly-Pro-Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]-naphthalene-1-sulfonic acid)-Arg
-
pH 7.5, 22°C, APCE
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
-
pH 7.5, 22°C, recombinant FAP
0.101
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin
-
pH 7.5, 22°C, recombinant FAP
0.062
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.091
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657Q, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.135
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657S, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.2
Gly-Pro-7-amido-4-trifluoromethylcoumarin
Km above 0.2 mM, wild type enzyme
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
0.25
Gly-Pro-7-amido-4-trifluoromethylcoumarin
wild type enzyme, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.37
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme N704A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.38
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme R123A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.41
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657F, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.42
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657T, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.44
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.45
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E204D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.49
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657V, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.55
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203D/E204D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.67
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme R123M, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.73
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E204A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.75
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E204Q, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.92
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1.1
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme R123K, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1.1
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme Y656F, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1.3
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657G, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1.5
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203Q/E204Q, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1.8
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203Q, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.2
L-Ala-Pro-7-amido-4-trifluoromethylcoumarin
Km above 0.2 mM, wild type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
0.19
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
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
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
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
0.05
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203A/E204A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.13
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E204D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.2
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657F, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.36
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.37
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.37
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme Y656F, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.4
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme R123K, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.45
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E204A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.47
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme R123A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.48
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme R123M, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.6
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E204Q, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.94
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657V, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1.4
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203D/E204D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1.8
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657G, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
2
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657Q, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
4.5
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657T, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
4.7
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657S, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
7.7
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
wild type enzyme, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
8.9
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657N, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
14
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
14.2
Ala-Pro-7-amido-4-trifluoromethylcoumarin
-
at 23°C in 50 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, pH 7.4
1.06
Arg-Lys(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-Gly-Pro-Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]-naphthalene-1-sulfonic acid)-Arg
-
pH 7.5, 22°C, APCE
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
-
pH 7.5, 22°C, recombinant FAP
0.51
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin
-
pH 7.5, 22°C, recombinant FAP
0.03
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.09
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657Q, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.09
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657V, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.12
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme N704A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.15
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme Y656F, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.19
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.19
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E204Q, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.26
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.28
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E204A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.29
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657T, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.33
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E204D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.46
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657S, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.71
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203D/E204D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1.2
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme R123K, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1.7
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme R123A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
2.1
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme R123M, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
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
5.6
Gly-Pro-7-amido-4-trifluoromethylcoumarin
wild type enzyme, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.00327
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
0.000146
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
0.057
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
0.0046
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
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
0.023
acetyl-Gly-boro-Pro
wild type enzyme, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.023
acetyl-Gly-boro-Pro
mutant enzyme A657D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
6.8
acetyl-Gly-Pro-CN
wild type enzyme, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
6.8
acetyl-Gly-Pro-CN
mutant enzyme A657D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.014
Ile-boro-Pro
wild type enzyme, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.014
Ile-boro-Pro
mutant enzyme A657D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.84
Ile-Pro-CN
wild type enzyme, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.84
Ile-Pro-CN
mutant enzyme A657D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.0062
Val-boro-Pro
wild type enzyme, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.0062
Val-boro-Pro
mutant enzyme A657D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.034
Val-Pro-CN
wild type enzyme, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.034
Val-Pro-CN
mutant enzyme A657D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000023
(S)-N-(2-(2-cyano-4,4-difluoropyrrolidin-1-yl)-2-oxoethyl)quinoline-4-carboxamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0000068
(S)-N-(2-(2-cyanopyrrolidin-1-yl)-2-oxoethyl)quinoline-4-carboxamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
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
0.00000042
4-(2-oxo[(2S)-1-[N-(quinoline-4-carbonyl)glycyl]pyrrolidin-2-yl]acetamido)benzoic acid
Homo sapiens
pH not specified in the publication, 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
0.000089 - 0.00037
linagliptin
Homo sapiens
pH and temperature not specified in the publication
0.000000089
N-(2-[(2S)-2-[[[(3,4-dimethoxyphenyl)methyl]amino](oxo)acetyl]pyrrolidin-1-yl]-2-oxoethyl)quinoline-4-carboxamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00000022
N-(2-[(2S)-2-[[[(3-methoxyphenyl)methyl]amino](oxo)acetyl]pyrrolidin-1-yl]-2-oxoethyl)quinoline-4-carboxamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00000018
N-(2-[(2S)-2-[[[(4-methoxyphenyl)methyl]amino](oxo)acetyl]pyrrolidin-1-yl]-2-oxoethyl)quinoline-4-carboxamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00000019
N-(2-[(2S)-2-[[[2-(3,4-dimethoxyphenyl)ethyl]amino](oxo)acetyl]pyrrolidin-1-yl]-2-oxoethyl)quinoline-4-carboxamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00000032
N-(2-[(2S)-2-[[[2-(morpholin-4-yl)-2-oxoethyl]amino](oxo)acetyl]pyrrolidin-1-yl]-2-oxoethyl)quinoline-4-carboxamide
Homo sapiens
pH not specified in the publication, 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
0.091
Phe-Arg-(8-amino-3,6-dioxaoctanoic acid)-Gly-[R]-fluoropyrrolidide
Homo sapiens
cleavage of Met-alpha2-antiplasmin
0.1
sitagliptin
Homo sapiens
above, pH and temperature not specified in the publication
0.00000013
tert-butyl N-(oxo[(2S)-1-[N-(quinoline-4-carbonyl)glycyl]pyrrolidin-2-yl]acetyl)glycinate
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.5
-
substrate: Arg-Lys(DABCYL)-Thr-Ser-Gly-Pro-Asn-Gln-Glu-Gln-Glu(EDANS)-Arg, APCE or rFAP
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
higher levels in cancer tissue than normal tissue
brenda
reveals a high concentration of FAP and vimentin-positive cells
brenda
FAP expression is highly present within the medulla
brenda
-
mainly located, seprase-expressing carcinoma tissue more often found in the scirrhous type than in other types of gastric carcinoma
brenda
FAPa is observed in the E-cadherin positive and vimentin-negative epithelial islands
brenda
-
expression in idiopathic pulmonary fibrosis, not expressed in normal lung tissue or tissue with evidence of centriacinar emphysema
brenda
transiently expressed in certain normal fetal mesenchymal tissues
brenda
-
the enzyme is coexpressed with dipeptidyl peptidase-IV in adult humans
brenda
-
the enzyme is coexpressed with dipeptidyl peptidase-IV in adult humans
brenda
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
brenda
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
brenda
additional information
FAP-alpha is significantly increased in breast cancer patients with poor outcome and survival
brenda
-
colocalized with dipeptidylpeptidase IV in endothelial cells of capillaries, but not of large blood vessels, in invasive breast ductal carcinoma in vivo
brenda
-
reactive tumor stromal fibroblast and granulation tissue during wound healing
brenda
-
of epithelial cancer and foreskin fibroblasts grown to confluence and maintained in low-serum media for up to 10 days
brenda
-
reactive stromal fibromlasts of breast, colorectal, lung and other epithelial cancers
brenda
-
expressed by cancer-associated fibroblasts in the microenvironment of most solid tumors
brenda
-
glioma stem-like cell, isolated from a solid glioblastoma in a long term culture, low expression
brenda
-
increased enzyme expression in a subgroup of high-grade gliomas. The enzyme is expressed by several constituents of the glioblastoma microenvironment, including stromal non-malignant mesenchymal cells recruited to and/or activated in response to glioma growth
brenda
the protease fibroblast activation protein is a specific marker of activated mesenchymal cells in tumour stroma and fibrotic liver
brenda
the protease fibroblast activation protein is a specific marker of activated mesenchymal cells in tumor stroma and fibrotic liver
brenda
-
the protease fibroblast activation protein is a specific marker of activated mesenchymal cells in tumour stroma and fibrotic liver. The enzyme activity is 14 to 18fold greater in cirrhotic than in non-diseased human liver, and almost doubled in alcoholic cirrhosis
brenda
the protease fibroblast activation protein is a specific marker of activated mesenchymal cells in tumour stroma and fibrotic liver
brenda
-
the enzyme is expressed by several constituents of the glioblastoma microenvironment, including stromal non-malignant mesenchymal cells recruited to and/or activated in response to glioma growth
brenda
the protease fibroblast activation protein is a specific marker of activated mesenchymal cells in tumor stroma and fibrotic liver
brenda
-
the protease fibroblast activation protein is a specific marker of activated mesenchymal cells in tumour stroma and fibrotic liver
brenda
-
granulation tissue caused by cancerous ulcer and some goblet cells weakly positive
brenda
additional information
seprase is expressed during wound-healing, normal adult tissues as well as malignant epithelial, neural and haematopoietic cells are generally seprase-negative
brenda
additional information
quantitative real-time PCR enzyme expression analysis
brenda
additional information
the protease fibroblast activation protein is a specific marker of activated mesenchymal cells in tumour stroma and fibrotic liver
brenda
additional information
-
the protease fibroblast activation protein is a specific marker of activated mesenchymal cells in tumour stroma and fibrotic liver
brenda
additional information
the enzyme is widely expressed in tumor microenvironment. No enzyme expression in wild-type SKOV-3 and HO-8910 cells, two poorly differentiated ovarian serous adenocarcinoma cell lines
brenda
additional information
the enzyme is not expressed in normal adult tissues, but is highly expressed on stromal fibroblasts in virtually all epithelial carcinomas and on tumor cells of some sarcomas
brenda
additional information
-
the enzyme is not expressed in normal adult tissues, but is highly expressed on stromal fibroblasts in virtually all epithelial carcinomas and on tumor cells of some sarcomas
brenda
additional information
the protease fibroblast activation protein is a specific marker of activated mesenchymal cells in tumor stroma and fibrotic liver. Highest levels of enzyme activity occur in uterus, pancreas, submaxillary gland and skin, whereas the lowest levels ar found in brain, prostate, leukocytes and testis
brenda
additional information
-
the protease fibroblast activation protein is a specific marker of activated mesenchymal cells in tumor stroma and fibrotic liver. Highest levels of enzyme activity occur in uterus, pancreas, submaxillary gland and skin, whereas the lowest levels ar found in brain, prostate, leukocytes and testis
brenda
additional information
-
expression is very low in adult organs, but is upregulated by activated fibroblasts in sites of tissue remodeling, including fibrosis, atherosclerosis, arthritis and tumors
brenda
additional information
-
the protease fibroblast activation protein is a specific marker of activated mesenchymal cells in tumour stroma and fibrotic liver. The enzyme activity is greatly elevated in tumours and associated lymph nodes and in fungal-infected skin of unhealthy baboons
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
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
evolution
the enzyme exhibits similar substrate specificity and properties compared to prolyl oligopeptidase, EC 3.4.21.26, the latter is specifically inhibited by Z-Pro-prolinal, while the fibroblast activation protein alpha is not. In contrast to prolyl oligopeptidase, fibroblast activation protein alpha is not expressed in normal adult tissues. Substrate specificity preferences among these sequences include Pro-Phe-Thr, which is strongly cleaved by prolyl oligopeptidase, and Pro-Tyr-Asp, which is strongly cleaved by fibroblast activation protein alpha. Pro-Phe/Tyr-Asp/Glu sequences are extensively cleaved by both prolyl oligopeptidase and fibroblast activation protein alpha, but neither enzyme exhibit substantial cleavage of Pro-Asp/Glu-Phe-Tyr
malfunction
-
siRNA knockdown of FAP-alpha in a glioma cell line shows decreased invasion through brain extracellular matrix proteoglycan brevican and denatured collagen
malfunction
-
plasma from FAP-deficient mice exhibits slower than wild-type clotting times
physiological function
in vitro, FAP-alpha promotes proliferation and inhibits migration of breast cancer cells, potentially by regulating the FAK pathway
physiological function
the enzyme promotes ovarian cancer cell proliferation, drug resistance, invasiveness, and migration in vitro and it significantly facilitates tumor growth in xenograft tumor tissues. The enzyme might directly promote tumor growth and invasiveness in ovarian cancer cells
physiological function
fibroblast activation protein-alpha promotes ovarian cancer cell proliferation and invasion via extracellular and intracellular signaling mechanisms, role of the non-enzymatic activities of the enzyme, overview. The enzyme, together with integrin alpha3beta1 and the uPAR signaling complex, mediates cancer cell migration in the HO-8910PM cell line via the small GTPase Rac1. FAP?-mediated upregulation of p-ERK occurs in a time-dependent manner
physiological function
-
the enzyme promotes the ability of proliferation, migration, invasion, apoptosis-inhibition of SGC7901 cells and induces apoptosis of GES1 cells in vitro
physiological function
-
the enzyme plays a role in mediating communication between activated fibroblasts and macrophages
physiological function
-
the enzyme may contributes to the focal matrix-degrading capability of stromal invadopodia
physiological function
-
the enzyme promotes the growth and migration of lung cancer cells via the phosphatidylinositol-3-kinase and sonic hedgehog pathways
physiological function
-
the enzyme promotes cell growth, adhesion, invasion and migration in breast cancer. Its regulatory effects are independent of its enzymatic activity. The PI3K/AKT and MMP2/9 signaling pathway might be involved in the effects of FAPalpha on breast cancer cells
physiological function
-
the enzyme is implicated in the modulation of the bioavailability and thus the function of a number of biologically active peptides. It has the potential to modulate the paracrine signaling in the human Langerhans islets
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q12844_HUMAN
889
0
100539
TrEMBL
Secretory Pathway (Reliability: 2)
SEPR_HUMAN
760
1
87713
Swiss-Prot
Secretory Pathway (Reliability: 3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
-
2 * 100000, multiangle light scattering in combination with gel filtration chromatography and interferometric refractometry
170000
200000
-
multiangle light scattering in combination with gel filtration chromatography and interferometric refractometry
400000
95000
97000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
homodimer
-
2 * 100000, multiangle light scattering in combination with gel filtration chromatography and interferometric refractometry
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
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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
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A657D
S624A
additional information
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
-
FAP serine mutant lacking enzymatic activity, as wild type does not rescue dipeptidyl peptidase IV cell surface expression but is a more potent tumor suppressor than the wild type
S624A
-
FAP serine mutant lacking enzymatic activity, as wild type does not rescue dipeptidyl peptidase IV cell surface expression but is a more potent tumor suppressor than the wild type
-
additional information
-
MDA-MB-231 cell mammary adenocarcinoma cells engineered to express active seprase to high levels
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, hydrophobic interaction column chromatography, and immunoaffinity column chromatography
-
purification protocol employing ammonium sulfate precipitation, ion exchange chromatography, immobilised metal affinity chromatography and ultrafiltration
S-200 gel filtration, hydroxylapatite column chromatography, Cibacron blue chromatography, and WGA-agarose column chromatography
S-200 gel filtration, hydroxylapatite column chromatography, Cibacron blue chromatography, and WGA-agarose column chromatography
S-200 gel filtration, hydroxylapatite column chromatography, Cibacron blue chromatography, and WGA-agarose column chromatography
S-200 gel filtration, hydroxylapatite column chromatography, Cibacron blue chromatography, and WGA-agarose column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in HEK-293 cells
protocol for expression of His6-tagged FAP using a modified baculovirus expression construct and the gp67 secretion signal to produce active soluble recombinant FAP (residues 27-760) in insect cells
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
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
bone marrow mesenchymal stem cells of newly diagnosed patients with acute myeloid leukemia have a significantly higher expression of FAP than healthy donors
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
-
TGFbeta-1 induces expression of FAP in non-stem glioma cells, pericytes, and glioblastoma-derived endothelial and FAP+ mesenchymal cells, but not in glioma stem-like cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
development of bioluminogenic probes for FAP based on N-carbobenzyloxy-Gly-Pro-OH and Boc-Gly-Pro-OH conjugated with aminoluciferin to evaluate FAP inhibitors in vitro. Limit of detection is 0.254 ng/ml
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
medicine
-
tumor suppressor that abrogates tumorigenicity through regulation of cell growth and survival, in vitro, FAP expression restores contact inhibition, leads to cell cylcle arrest at G0/G1 phase, increases susceptibility to stress-induced apoptosis, and leads to caspase activation
medicine
-
role in the invasive and metastatic progression of gastric carcinoma, tendency towards a worse prognosis in patients whose tumors exhibit high levels of the 170000 Da seprase dimer
medicine
-
significant correlation between seprase expression and lymph node metastasis
medicine
-
selectively induced in fibrotic foci, but not in normal or emphysematous lung
medicine
-
protease complex consisting of seprase and dipeptidylpeptidase IV in endothelial cells that are activated to migrate and invade in the extracellular matrix in vitro and are coexpressed with the three major protease systems matrix metalloproteinase, plasminogen activator, and type II transmembrane serine protease, at the cell surface and organize as a complex at invadopodia-like protrusions
medicine
-
expression of active seprase increases tumor growth and microvessel density
medicine
-
fibroblast activation protein alpha has a high-risk correlation with the malignant level of clinical outcomes in gastric cancer patients
medicine
-
the limited expression of the enzyme in healthy tissues together with its presence in both transformed and stromal cells suggests that it may be a candidate target for specific delivery of therapeutic agents in glioblastoma
medicine
-
targeting fibroblast activation protein and cancer-associated fibroblasts in combination with radiation is capable of enhancing anti-tumor T cell infiltrate and function, but does not result in sufficient tumor clearance to extend survival
medicine
bone marrow mesenchymal stem cells of newly diagnosed patients with acute myeloid leukemia have a significantly higher expression of FAP than healthy donors. Expression is positively correlated with the proportion of myeloblasts in bone marrow, and is significantly negatively associated with survival time in eight patients who did not undergo chemotherapy
medicine
both FAP and TGFbeta-1 are upregulated in glioblastomas and display a significant positive correlation
medicine
-
tumor suppressor that abrogates tumorigenicity through regulation of cell growth and survival, in vitro, FAP expression restores contact inhibition, leads to cell cylcle arrest at G0/G1 phase, increases susceptibility to stress-induced apoptosis, and leads to caspase activation
-
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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)
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Collins, P.J.; McMahon, G.; OBrien, P.; OConnor, B.
Purification, identification and characterisation of seprase from bovine serum
Int. J. Biochem. Cell Biol.
36
2320-2333
2004
Bos taurus
brenda
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
brenda
Ramirez-Montagut, T.; Blachere, N.E.; Sviderskaya, E.V.; Bennett, D.C.; Rettig, W.J.; Garin-Chesa, P.; Houghton, A.N.
FAPalpha, a surface peptidase expressed during wound healing, is a tumor suppressor
Oncogene
23
5435-5446
2004
Mus musculus, Mus musculus C57BL/6
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
O'Brien, P.; O'Connor, B.F.
Seprase: An overview of an important matrix serine protease
Biochim. Biophys. Acta
1784
1130-1145
2008
Homo sapiens (Q12884), Mus musculus (P97321), Xenopus laevis (Q91651), Gallus gallus, Bos taurus
brenda
Lai, K.S.; Ho, N.; Cheng, J.D.; Tung, C.
Selective fluorescence probes for dipeptidyl peptidase activity-fibroblast activation protein and dipeptidyl peptidase IV
Bioconjug. Chem.
18
1246-1250
2007
Mus musculus
brenda
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)
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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)
brenda
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)
brenda
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
brenda
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)
brenda
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
brenda
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)
brenda
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)
brenda
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)
brenda
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
brenda
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
Mus musculus (P97321), Mus musculus, Homo sapiens (Q12844), Homo sapiens, Papio sp.
brenda
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)
-
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
-
brenda
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
brenda
Zhang, H.E.; Hamson, E.J.; Koczorowska, M.M.; Tholen, S.; Chowdhury, S.; Bailey, C.G.; Lay, A.J.; Twigg, S.M.; Lee, Q.; Roediger, B.; Biniossek, M.L.; ORourke, M.B.; McCaughan, G.W.; Keane, F.M.; Schilling, O.; Gorrell, M.D.
Identification of novel natural substrates of fibroblast activation protein-alpha by differential degradomics and proteomics
Mol. Cell. Proteomics
18
65-85
2019
Mus musculus
brenda
Mazur, A.; Holthoff, E.; Vadali, S.; Kelly, T.; Post, S.R.
Cleavage of type I collagen by fibroblast activation protein-alpha enhances class A scavenger receptor mediated macrophage adhesion
PLoS ONE
11
e0150287
2016
Mus musculus
brenda
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
brenda
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
brenda
Lin, Y.; Ma, Z.; Li, Z.; Gao, Y.; Qin, X.; Zhang, Z.; Wang, G.; Du, L.; Li, M.
Bioluminescent probe for monitoring endogenous fibroblast activation protein-alpha
Anal. Chem.
91
14873-14878
2019
Mus musculus (P97321)
brenda
Simkova, A.; Ormsby, T.; Sidej, N.; Slavetinska, L.P.; Brynda, J.; Beranova, J.; Sacha, P.; Majer, P.; Konvalinka, J.
Structure-activity relationship and biochemical evaluation of novel fibroblast activation protein and prolyl endopeptidase inhibitors with alpha-ketoamide warheads
Eur. J. Med. Chem.
224
113717
2021
Homo sapiens (Q12884)
brenda
Driesen, R.B.; Hilkens, P.; Smisdom, N.; Vangansewinkel, T.; Dillen, Y.; Ratajczak, J.; Wolfs, E.; Gervois, P.; Ameloot, M.; Bronckaers, A.; Lambrichts, I.
Dental tissue and stem cells revisited new insights from the expression of fibroblast activation protein-alpha
Front. Cell Dev. Biol.
7
389
2019
Homo sapiens (Q12884)
brenda
Krepela, E.; Vanickova, Z.; Hrabal, P.; Zubal, M.; Chmielova, B.; Balaziova, E.; Vymola, P.; Matrasova, I.; Busek, P.; Sedo, A.
Regulation of fibroblast activation protein by transforming growth factor beta-1 in glioblastoma microenvironment
Int. J. Mol. Sci.
22
1046
2021
Homo sapiens (Q12884)
brenda
Mei, S.; Zhang, Y.; Yu, L.; Chen, G.; Zi, F.
Expression and role of fibroblast activation protein alpha in acute myeloid leukemia
Oncol. Rep.
45
641-651
2021
Homo sapiens (Q12884)
brenda
Xi, C.R.; Di Fazio, A.; Nadvi, N.A.; Xiang, M.S.W.; Zhang, H.E.; Deshpande, C.; Chen, Y.; Tabar, M.S.; Wang, X.M.; Bailey, C.G.; McCaughan, G.W.; Church, W.B.; Gorrell, M.D.
An improved production and purification protocol for recombinant soluble human fibroblast activation protein alpha
Protein Expr. Purif.
181
105833
2021
Homo sapiens (Q12884)
brenda
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