Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Abz-DVVNAPVPPSKDD-CONH2 + H2O
Abz-DVVNA + PVPPSKDD-CONH2
-
-
-
?
Abz-DVVNPAVPPSKDD-CONH2 + H2O
Abz-DVVNP + AVPPSKDD-CONH2
-
-
-
?
Abz-DVVNPPVPPSKDD-CONH2 + H2O
Abz-DVVNP + PVPPSKDD-CONH2
-
-
-
?
Ac-EPNAAVP-CONH2 + H2O
Ac-EPNA + AVP-CONH2
Ac-HLLPPPS-CONH2 + H2O
Ac-HLLP + PPS-CONH2
Ac-SLRPAPP-CONH2 + H2O
Ac-SLRP + APP-CONH2
fibrinogen beta-derived peptide
-
-
?
acetyl-EVNPPVPD + H2O
acetyl-EVNP + PVPD
adhesion molecule CD2831 + H2O
?
adhesion molecule CD3246 + H2O
?
collagen binding protein CD2831 + H2O
PAPPNTDEPIVNP + ?
Dabcyl-Lys-EVNPPPPD-EdansGlu + H2O
Dabcyl-Lys-EVNP + PPPD-EdansGlu
-
-
-
?
fibrinogen beta-chain + H2O
?
heat shock protein HSP90beta + H2O
?
-
cleavage between resiudue A702 and A703
-
?
IgA2 heavy chain + H2O
?
-
cleavage within the hinge region PVP-PPPPC
-
?
KAAEEPNAAVPDEIK + H2O
KAAEEPNA + AVPDEIK
peptide based on the cleacage site of HSP90beta
-
-
?
LPXTG cell surface protein CD2831 + H2O
?
-
native CD2830, secreted by live cells, cleaves endogenous CD2831 and CD3246 molecules. Enzyme efficiently cleaves CD2831 between two prolines at all predicted cleavage sites
-
?
LPXTG cell surface protein CD3246 + H2O
?
-
native CD2830, secreted by live cells, cleaves endogenous CD2831 and CD3246 molecules
-
?
YPSSKPLPPVPPVQPLPPVPKLETS + H2O
YPSSKPLP + PVPPVQPLP + PVPKLETS
additional information
?
-
Ac-EPNAAVP-CONH2 + H2O
Ac-EPNA + AVP-CONH2
heat shock protein 90-derived peptide
-
-
?
Ac-EPNAAVP-CONH2 + H2O
Ac-EPNA + AVP-CONH2
heat shock protein 90-derived peptide
-
-
?
Ac-HLLPPPS-CONH2 + H2O
Ac-HLLP + PPS-CONH2
immunoglobulin A1-derived peptide
-
-
?
Ac-HLLPPPS-CONH2 + H2O
Ac-HLLP + PPS-CONH2
immunoglobulin A1-derived peptide
-
-
?
acetyl-EVNPPVPD + H2O
acetyl-EVNP + PVPD
-
-
-
?
acetyl-EVNPPVPD + H2O
acetyl-EVNP + PVPD
-
-
-
?
adhesion molecule CD2831 + H2O
?
-
-
-
?
adhesion molecule CD2831 + H2O
?
-
-
-
-
?
adhesion molecule CD2831 + H2O
?
-
native CD2830, secreted by live cells, cleaves endogenous CD2831 and CD3246 molecules. Enzyme efficiently cleaves CD2831 between two prolines at all predicted cleavage sites
-
?
adhesion molecule CD2831 + H2O
?
-
-
-
?
adhesion molecule CD3246 + H2O
?
-
-
-
?
adhesion molecule CD3246 + H2O
?
-
-
-
-
?
adhesion molecule CD3246 + H2O
?
-
native CD2830, secreted by live cells, cleaves endogenous CD2831 and CD3246 molecules
-
?
adhesion molecule CD3246 + H2O
?
-
-
-
?
collagen binding protein CD2831 + H2O
PAPPNTDEPIVNP + ?
-
the removal of the collagen binding protein CD2831 from cell surface is fully attributable to PPEP-1 activity
-
?
collagen binding protein CD2831 + H2O
PAPPNTDEPIVNP + ?
-
the removal of the collagen binding protein CD2831 from cell surface is fully attributable to PPEP-1 activity
-
?
Fibrinogen + H2O
?
in vitro assay, presence of Zn2+ required
-
-
?
Fibrinogen + H2O
?
in vitro assay, presence of Zn2+ required
-
-
?
fibrinogen beta-chain + H2O
?
almost complete digestion within 1 h
-
-
?
fibrinogen beta-chain + H2O
?
almost complete digestion within 1 h
-
-
?
Fibronectin + H2O
?
-
poor substrate
-
?
Fibronectin + H2O
?
in vitro assay, presence of Zn2+ required
-
-
?
Fibronectin + H2O
?
in vitro assay, presence of Zn2+ required
-
-
?
Fibronectin + H2O
?
-
poor substrate
-
?
YPSSKPLPPVPPVQPLPPVPKLETS + H2O
YPSSKPLP + PVPPVQPLP + PVPKLETS
-
-
-
?
YPSSKPLPPVPPVQPLPPVPKLETS + H2O
YPSSKPLP + PVPPVQPLP + PVPKLETS
-
-
-
?
additional information
?
-
enzyme has a preference for cleaving Pro-Pro bonds. No substrates: different collagen types, casein and gelatin, heat shock protein 90alpha
-
-
?
additional information
?
-
isoform PPEP-1 has a preference for prolines surrounding the scissile bond. It exhibits a high preference for an asparagine at the P2 position and hydrophobic residues at the P3 position
-
-
?
additional information
?
-
-
isoform PPEP-1 has a preference for prolines surrounding the scissile bond. It exhibits a high preference for an asparagine at the P2 position and hydrophobic residues at the P3 position
-
-
?
additional information
?
-
the enzyme exhibits a unique specificity for Pro-Pro peptide bonds within the consensus sequence VNP-PVP. The enzyme prefers proline residues at P1'. The residues Lys-101, Trp-103, and Glu-184 are crucial for proteolytic activity
-
-
?
additional information
?
-
-
the enzyme exhibits a unique specificity for Pro-Pro peptide bonds within the consensus sequence VNP-PVP. The enzyme prefers proline residues at P1'. The residues Lys-101, Trp-103, and Glu-184 are crucial for proteolytic activity
-
-
?
additional information
?
-
isoform PPEP-1 has a preference for prolines surrounding the scissile bond. It exhibits a high preference for an asparagine at the P2 position and hydrophobic residues at the P3 position
-
-
?
additional information
?
-
the enzyme exhibits a unique specificity for Pro-Pro peptide bonds within the consensus sequence VNP-PVP. The enzyme prefers proline residues at P1'. The residues Lys-101, Trp-103, and Glu-184 are crucial for proteolytic activity
-
-
?
additional information
?
-
the enzyme cleaves between two prolines in a PLPPVP motif
-
-
?
additional information
?
-
-
the enzyme cleaves between two prolines in a PLPPVP motif
-
-
?
additional information
?
-
the enzyme poorly cleaves the VNPPVP peptide
-
-
?
additional information
?
-
-
the enzyme poorly cleaves the VNPPVP peptide
-
-
?
additional information
?
-
the enzyme cleaves between two prolines in a PLPPVP motif
-
-
?
additional information
?
-
the enzyme poorly cleaves the VNPPVP peptide
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ac-EPNAAVP-CONH2 + H2O
Ac-EPNA + AVP-CONH2
Ac-HLLPPPS-CONH2 + H2O
Ac-HLLP + PPS-CONH2
Ac-SLRPAPP-CONH2 + H2O
Ac-SLRP + APP-CONH2
fibrinogen beta-derived peptide
-
-
?
adhesion molecule CD2831 + H2O
?
adhesion molecule CD3246 + H2O
?
additional information
?
-
Ac-EPNAAVP-CONH2 + H2O
Ac-EPNA + AVP-CONH2
heat shock protein 90-derived peptide
-
-
?
Ac-EPNAAVP-CONH2 + H2O
Ac-EPNA + AVP-CONH2
heat shock protein 90-derived peptide
-
-
?
Ac-HLLPPPS-CONH2 + H2O
Ac-HLLP + PPS-CONH2
immunoglobulin A1-derived peptide
-
-
?
Ac-HLLPPPS-CONH2 + H2O
Ac-HLLP + PPS-CONH2
immunoglobulin A1-derived peptide
-
-
?
adhesion molecule CD2831 + H2O
?
-
-
-
?
adhesion molecule CD2831 + H2O
?
-
-
-
-
?
adhesion molecule CD2831 + H2O
?
-
native CD2830, secreted by live cells, cleaves endogenous CD2831 and CD3246 molecules. Enzyme efficiently cleaves CD2831 between two prolines at all predicted cleavage sites
-
?
adhesion molecule CD2831 + H2O
?
-
-
-
?
adhesion molecule CD3246 + H2O
?
-
-
-
?
adhesion molecule CD3246 + H2O
?
-
-
-
-
?
adhesion molecule CD3246 + H2O
?
-
native CD2830, secreted by live cells, cleaves endogenous CD2831 and CD3246 molecules
-
?
adhesion molecule CD3246 + H2O
?
-
-
-
?
additional information
?
-
the enzyme exhibits a unique specificity for Pro-Pro peptide bonds within the consensus sequence VNP-PVP. The enzyme prefers proline residues at P1'. The residues Lys-101, Trp-103, and Glu-184 are crucial for proteolytic activity
-
-
?
additional information
?
-
-
the enzyme exhibits a unique specificity for Pro-Pro peptide bonds within the consensus sequence VNP-PVP. The enzyme prefers proline residues at P1'. The residues Lys-101, Trp-103, and Glu-184 are crucial for proteolytic activity
-
-
?
additional information
?
-
the enzyme exhibits a unique specificity for Pro-Pro peptide bonds within the consensus sequence VNP-PVP. The enzyme prefers proline residues at P1'. The residues Lys-101, Trp-103, and Glu-184 are crucial for proteolytic activity
-
-
?
additional information
?
-
the enzyme cleaves between two prolines in a PLPPVP motif
-
-
?
additional information
?
-
-
the enzyme cleaves between two prolines in a PLPPVP motif
-
-
?
additional information
?
-
the enzyme cleaves between two prolines in a PLPPVP motif
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0436
Abz-DVVNAPVPPSKDD-CONH2
wild type enzyme, at pH 7.5 and 20°C
0.0825
Abz-DVVNPAVPPSKDD-CONH2
wild type enzyme, at pH 7.5 and 20°C
0.1366 - 0.137
Abz-DVVNPPVPPSKDD-CONH2
0.077
Dabcyl-Lys-EVNPPPPD-EdansGlu
pH 7.4, 3°C
0.07 - 0.33
YPSSKPLPPVPPVQPLPPVPKLETS
-
0.1366
Abz-DVVNPPVPPSKDD-CONH2
mutant enzyme E184A, at pH 7.5 and 20°C
0.137
Abz-DVVNPPVPPSKDD-CONH2
wild type enzyme, at pH 7.5 and 20°C
0.07
YPSSKPLPPVPPVQPLPPVPKLETS
wild type enzyme PPEP-2, at pH 7.0 and 37°C
-
0.33
YPSSKPLPPVPPVQPLPPVPKLETS
recombinant enzyme PPEP-2GGST, where residues 112-115 of the wild type enzyme (SERV) are replaced by residues 91-94 of Pro-Pro endopeptidase-1 (GGST), at pH 7.0 and 37°C
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
E184A
the mutant shows reduced activity for Abz-DVVNPPVPPSKDD-CONH2 (15%) and Abz-DVVNAPVPPSKDD-CONH2 (9%) and residual activity for Abz-DVVNPAVPPSKDD-CONH2 (1.2%) compared to the wild type enzyme
E184K
the mutant shows residual activity compared to the wild type enzyme
H146A
complete loss of the ability to bind Zn2+, highly reduced activity on fibronectin
K101A
the mutant shows dramatically reduced activity compared to the wild type enzyme
K101E
the mutant shows dramatically reduced activity compared to the wild type enzyme
K101R
the mutant shows about wild type activity
W103F
the mutant shows residual activity for Abz-DVVNPPVPPSKDD-CONH2 compared to the wild type enzyme
W103H
the mutant shows residual activity for Abz-DVVNPPVPPSKDD-CONH2 compared to the wild type enzyme
W103Y
the mutant shows severely reduced activity for Abz-DVVNPPVPPSKDD-CONH2 and residual activity for Abz-DVVNPAVPPSKDD-CONH2 and Abz-DVVNAPVPPSKDD-CONH2 compared to the wild type enzyme
Y178F
41% of wild-type activity
E184A
-
the mutant shows reduced activity for Abz-DVVNPPVPPSKDD-CONH2 (15%) and Abz-DVVNAPVPPSKDD-CONH2 (9%) and residual activity for Abz-DVVNPAVPPSKDD-CONH2 (1.2%) compared to the wild type enzyme
-
E184K
-
the mutant shows residual activity compared to the wild type enzyme
-
H146A
-
complete loss of the ability to bind Zn2+, highly reduced activity on fibronectin
-
K101R
-
the mutant shows about wild type activity
-
Y178F
-
41% of wild-type activity
-
E143A
18% of wild-type activity
E143A
mutant displays highly reduced activity on fibronectin, binding of Zn2+ is similar to wild-type
E143A/Y178F
inactive
E143A/Y178F
complete loss of activity
E143A
-
mutant displays highly reduced activity on fibronectin, binding of Zn2+ is similar to wild-type
-
E143A
-
18% of wild-type activity
-
E143A/Y178F
-
complete loss of activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Hensbergen, P.; Klychnikov, O.; Bakker, D.; Van Winden, V.; Ras, N.; Kemp, A.; Cordfunke, R.; Dragan, I.; Deelder, A.; Kuijper, E.; Corver, J.; Drijfhout, J.; Van Leeuwen, H.
A novel secreted metalloprotease (CD2830) from Clostridium difficile cleaves specific proline sequences in LPXTG cell surface Proteins
Mol. Cell. Proteomics
13
1231-1244
2014
Clostridioides difficile (Q183R7)
-
brenda
Cafardi, V.; Biagini, M.; Martinelli M.; Leuzzi, R.; Rubino, J.T.; Cantini, F.; Norais, N.; Scarselli, M.; Serruto, D.; Unnikrishnan, M.
Identification of a novel zinc metalloprotease through a global analysis of Clostridium difficile extracellular proteins
PLoS One
8
e81306
2013
Clostridioides difficile (Q183R7), Clostridioides difficile, Clostridioides difficile 630 (Q183R7)
brenda
Hensbergen, P.J.; Klychnikov, O.I.; Bakker, D.; Dragan, I., Kelly, M.L.; Minton, N.P.; Corver, J.; Kuijper, E.J.; Drijfhout, J.W.; van Leeuwen, H.C.
Clostridium difficile secreted Pro-Pro endopeptidase PPEP-1 (ZMP1/CD2830) modulates adhesion through cleavage of the collagen binding protein CD2831
FEBS Lett.
589
3952-3958
2015
Clostridioides difficile (Q183R7), Clostridioides difficile, Clostridioides difficile 630 (Q183R7)
brenda
Schacherl, M.; Pichlo, C.; Neundorf, I.; Baumann, U.
Structural basis of proline-proline peptide bond specificity of the metalloprotease Zmp1 implicated in motility of Clostridium difficile
Structure
23
1632-1642
2015
Clostridioides difficile (Q183R7), Clostridioides difficile 630 (Q183R7)
brenda
Klychnikov, O.I.; Shamorkina, T.M.; Weeks, S.D.; van Leeuwen, H.C.; Corver, J.; Drijfhout, J.W.; van Veelen, P.A.; Sluchanko, N.N.; Strelkov, S.V.; Hensbergen, P.J.
Discovery of a new Pro-Pro endopeptidase, PPEP-2, provides mechanistic insights into the differences in substrate specificity within the PPEP family
J. Biol. Chem.
293
11154-11165
2018
Paenibacillus alvei (K4ZRC1), Paenibacillus alvei, Paenibacillus alvei ATCC 6344 (K4ZRC1)
brenda
Pichlo, C.; Juetten, L.; Wojtalla, F.; Schacherl, M.; Diaz, D.; Baumann, U.
Molecular determinants of the mechanism and substrate specificity of Clostridium difficile proline-proline endopeptidase-1
J. Biol. Chem.
294
11525-11535
2019
Clostridioides difficile (Q183R7), Clostridioides difficile, Clostridioides difficile 630 (Q183R7)
brenda
Corver, J.; Cordo, V.; van Leeuwen, H.C.; Klychnikov, O.I.; Hensbergen, P.J.
Covalent attachment and Pro-Pro endopeptidase (PPEP-1)-mediated release of Clostridium difficile cell surface proteins involved in adhesion
Mol. Microbiol.
105
663-673
2017
Clostridioides difficile (Q183R7), Clostridioides difficile, Clostridioides difficile 630 (Q183R7)
brenda