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7-methoxycoumarin-4-acetic acid-APGSKGDA-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-ASGPAGPA-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-DKGESGPA-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-DRGETGP-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-DRGETGPA-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-DSGETGP-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-DSGETGPA-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-EPGPPGPA-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-ERGETGPA-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-ERGETGPAG-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-ERGETGPAGG-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-ERGETGPSG-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-VGPAGK-dinitrophenyl + H2O
?
-
-
-
-
?
acetyl-D-Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
acetyl-D-Ala-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
acetyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
acetyl-Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin + H2O
acetyl-Gly-Pro-7-amino-4-trifluoromethylcoumarin
-
-
-
?
acetyl-Gly-Pro-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate + H2O
acetyl-Gly-Pro + 9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate
-
-
-
-
?
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
-
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
-
-
?
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
-
-
-
?
Ala-Pro-7-amido-4-methylcoumarin + H2O
Ala-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Ala-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Ala-Pro + 7-amino-4-trifluoromethylcoumarin + H2O
-
-
-
-
?
Ala-Pro-Ala-Pro-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate + H2O
Ala-Pro-Ala-Pro + 9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate
-
-
-
-
?
Ala-Ser-Gly-Pro-Asn-Gln + H2O
Ala-Ser-Gly-Pro + Asn-Gln
-
-
-
?
Ala-Ser-Gly-Pro-Ser-Ser + H2O
Ala-Ser-Gly-Pro + Ser-Ser
-
-
-
?
alpha2-antiplasmin + H2O
?
alpha2-antiplasmin + H2O
truncated alpha2-antiplasmin + Met
-
-
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
Arg-Pro-7-amido-4-methylcoumarin + H2O
Arg-Pro + 7-amino-4-methylcoumarin
-
preferred substrate
-
-
?
B-type natriuretic peptide + H2O
?
efficiently hydrolysed and mostly preferred substrate
-
-
?
benzyloxycarbonyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-7-amido-4-methyl-3-carbamoylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro + 7-amino-4-methyl-3-carbamoylcoumarin
-
-
-
-
?
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
-
-
-
-
?
Boc-Ala-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
Boc-Ala-Gly-Pro-Arg + 7-amino-4-methylcoumarin
complement C1q tumor necrosis factor-related protein 6 + H2O
?
-
cleavage at position 26 after a Val-Pro sequence
-
-
?
CXCL-5 + H2O
?
-
processing of CXCL-5 at position 42, which is after an Ala-Pro sequence
-
-
?
D-Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
D-Ala-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
denatured type I collagen + H2O
?
-
-
-
-
?
extracellular matrix protein 1 + H2O
?
-
cleavage occurrs at position 142 after a Lys-Pro sequence
-
-
?
extracellular matrix protein CN-I + H2O
?
-
-
-
-
?
extracellular matrix protein CN-III + H2O
?
-
-
-
-
?
extracellular matrix protein CN-V + H2O
?
-
-
-
-
?
fibrillin-2 + H2O
?
-
cleavage occurrs at position 60, in the propeptide domain, after a Gly-Pro sequence
-
-
?
GASGPAGPA + H2O
GASGP + AGPA
-
-
-
?
GEPGPPGPA + H2O
GEP + GPPGP + L-Ala
-
-
-
?
GFSPFQRED + H2O
?
low activity
-
-
?
Gln-Pro-7-amido-4-methylcoumarin + H2O
Gln-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Glu-Pro-7-amido-4-methylcoumarin + H2O
Glu-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
glucagon-like peptide-1 + H2O
?
slow hydrolysis
-
-
?
glucose-dependent insulinotropic peptide + H2O
?
slow hydrolysis
-
-
?
Gly-Pro-4-trifluoromethylcoumarin-7-amide + H2O
Gly-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
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
-
-
-
?
GTAGPNQEQE + H2O
GTAGP + NQEQE
-
-
-
?
GTSGPNQEQE + H2O
GTSGP + NQEQE
-
-
-
?
Ile-Pro-7-amido-4-methylcoumarin + H2O
Ile-Pro + 7-amino-4-methylcoumarin
-
most preferred substrate
-
-
?
Ile-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Ile-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
L-Ala-L-Pro-7-amido-4-methylcoumarin + H2O
L-Ala-L-Pro + 7-amino-4-methylcoumarin
-
-
-
?
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
?
FRET-peptide
-
-
?
Leu-Pro-7-amido-4-methylcoumarin + H2O
Leu-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Lys-Ala-7-amido-4-trifluoromethylcoumarin + H2O
Lys-Ala + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
Lys-Pro-4-trifluoromethylcoumarin-7-amide + H2O
Lys-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
Lys-Pro-7-amido-4-methylcoumarin + H2O
Lys-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
lysyl oxidase homolog 2 + H2O
?
-
cleavage at position 36 after a Tyr-Pro sequence that follows the signal peptide
-
-
?
MEPLGRQLTSGP-7-amido-4-methylcoumarin + H2O
MEPLGRQLTSGP + 7-amino-4-methylcoumarin
-
-
-
?
MEPLGWQLTSGP-7-amido-4-methylcoumarin + H2O
MEPLGWQLTSGP + 7-amino-4-methylcoumarin
-
-
-
?
Met-alpha2-antiplasmin + H2O
?
Met-Pro-7-amido-4-methylcoumarin + H2O
Met-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Leu-Phe-His + H2O
?
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Ala + H2O
N-benzyloxycarbonyl-Gly-Pro + L-Ala
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Glu + H2O
N-benzyloxycarbonyl-Gly-Pro + L-Glu
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-His + H2O
N-benzyloxycarbonyl-Gly-Pro + L-His
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Leu + H2O
N-benzyloxycarbonyl-Gly-Pro + L-Leu
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Met + H2O
N-benzyloxycarbonyl-Gly-Pro + L-Met
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Met-His + H2O
N-benzyloxycarbonyl-Gly-Pro + Met-His
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Met-His-Arg-Ser + H2O
N-benzyloxycarbonyl-Gly-Pro + Met-His-Arg-Ser
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Phe + H2O
N-benzyloxycarbonyl-Gly-Pro + L-Phe
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Phe-His + H2O
N-benzyloxycarbonyl-Gly-Pro + L-Phe-L-His
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Phe-His-Arg + H2O
N-benzyloxycarbonyl-Gly-Pro + Phe-His-Arg
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Phe-His-Arg-Ser + H2O
N-benzyloxycarbonyl-Gly-Pro + Phe-His-Arg-Ser
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Ser + H2O
N-benzyloxycarbonyl-Gly-Pro + L-Ser
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Tyr + H2O
N-benzyloxycarbonyl-Gly-Pro + L-Tyr
-
-
-
-
?
N-formyl-Gly-Pro-7-amido-4-methyl-3-carbamoylcoumarin + H2O
N-formyl-Gly-Pro + 7-amino-4-methyl-3-carbamoylcoumarin
-
-
-
-
?
N-methyl-Gly-Pro-7-amido-4-methyl-3-carbamoylcoumarin + H2O
N-methyl-Gly-Pro + 7-amino-4-methyl-3-carbamoylcoumarin
-
-
-
-
?
neuropeptide Y + H2O
?
efficiently hydrolysed and mostly preferred substrate
-
-
?
peptide YY + H2O
?
efficiently hydrolysed substrate
-
-
?
Phe-Pro-7-amido-4-methylcoumarin + H2O
Phe-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Phe-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Phe-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
pre-digested collagen + H2O
?
-
-
-
-
?
precursor Met-alpha2-antiplasmin + H2O
L-Asn-alpha2-antiplasmin + ?
-
the enzyme cleaves between Pro12 and Asn13
-
-
?
Pro-Pro-7-amido-4-methylcoumarin + H2O
Pro-Pro + 7-amino-4-methylcoumarin
-
preferred substrate
-
-
?
RPKPQQFFGLM + H2O
RPKP + L-Gln-L-Gln + FFGLM
the substance P-derived sequence is cleaved although it does not contain Gly-Pro
-
-
?
Ser-Pro-7-amido-4-methylcoumarin + H2O
Ser-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Substance P + H2O
?
efficiently hydrolysed substrate
-
-
?
Thr-Ala-Gly-Pro-Asn-Gln + H2O
Thr-Ala-Gly-Pro + Asn-Gln
-
-
-
?
Thr-Pro-7-amido-4-methylcoumarin + H2O
Thr-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Thr-Ser-Gly-Pro-Asn-Gln + H2O
Thr-Ser-Gly-Pro + Asn-Gln
-
-
-
?
Thr-Ser-Gly-Pro-Asn-Ser + H2O
Thr-Ser-Gly-Pro + Asn-Ser
-
-
-
?
Thr-Ser-Gly-Pro-Ser-Gln + H2O
Thr-Ser-Gly-Pro + Ser-Gln
-
-
-
?
Tic-Pro-7-amido-4-trifluoromethylcoumarin + H2O
?
-
-
-
-
?
TSGP-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate + H2O
TSGP + 9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate
-
-
-
-
?
type III collagen + H2O
?
-
-
-
-
?
type V collagen + H2O
?
-
-
-
-
?
Tyr-Pro-7-amido-4-methylcoumarin + H2O
Tyr-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Val-Pro-7-amido-4-methylcoumarin + H2O
Val-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
Z-Gly-L-Pro + 7-amino-4-methylcoumarin
-
-
-
?
additional information
?
-
Ala-Pro-4-trifluoromethylcoumarin-7-amide + H2O
Ala-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
Ala-Pro-4-trifluoromethylcoumarin-7-amide + H2O
Ala-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
?
alpha2-antiplasmin + H2O
?
-
-
-
-
?
alpha2-antiplasmin + H2O
?
-
-
-
?
alpha2-antiplasmin + H2O
?
alpha2-antiplasmin is cleaved N-terminally to Asn-alpha2-antiplasmin that is rapidly cross-linked to fibrin and protects it from digestion by plasmin
-
-
?
alpha2-antiplasmin + H2O
?
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
-
-
?
alpha2-antiplasmin + H2O
?
efficiently hydrolysed substrate
-
-
?
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-Ala-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
Boc-Ala-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Boc-Ala-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
Boc-Ala-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Boc-Ala-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
Boc-Ala-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Collagen + H2O
?
-
-
-
-
?
Collagen + H2O
?
-
cleavage of type I collagen by fibroblast activation protein-? enhances class A scavenger receptor mediated macrophage adhesion
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
seprase-dimer
-
-
?
Gelatin + H2O
?
-
gelatin cleavage results in 51 fragments
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
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
-
-
-
?
L-Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
L-Ala-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
L-Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
L-Ala-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
L-Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
L-Ala-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
Met-alpha2-antiplasmin + H2O
?
-
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
-
-
?
Met-alpha2-antiplasmin + H2O
?
-
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
-
-
?
Type I collagen + H2O
?
-
-
-
?
Type I collagen + H2O
?
-
-
-
?
Type I collagen + H2O
?
-
-
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
glycosylated form has both postprolyl depeptidyl peptidase and postgelatinase activity, nonglycosylated isoform has no detectable gelatinase activity
-
?
additional information
?
-
-
glycosylated form has both postprolyl depeptidyl peptidase and postgelatinase activity, nonglycosylated isoform has no detectable gelatinase activity
-
?
additional information
?
-
may contribute to invasiveness in malignant cancers
-
?
additional information
?
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cleaves alpha2-antiplasmin with Arg as the sixth amino acid approximately 8fold faster than alpha2-antiplasmin with Trp at this position
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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
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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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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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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'
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does not cleave native human collagens, fibronectin or laminin
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FAP-alpha is an endopeptidase cleaving large protein with Gly(2)-Pro(1)-cleaving specificity
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does not hydrolyze succinyl-L-Ala-L-Pro-7-amido-4-methylcoumarin and H-Gly-Pro-7-amido-4-methylcoumarin
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the enzyme acts as both a dipeptidyl peptidase and an endopeptidyl peptidase
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a post-proline cleaving serine peptidase
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a post-proline cleaving serine peptidase
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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
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additional information
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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
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the enzyme is a is a prolyl specific serine protease
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shows no activity with Gly-Pro-Gly-Pro-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate
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the enzyme has both dipeptidyl aminopeptidase and endopeptidase activities, and can hydrolyze the post-proline bond
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