3.4.24.89: Pro-Pro endopeptidase
This is an abbreviated version!
For detailed information about Pro-Pro endopeptidase, go to the full flat file.
Word Map on EC 3.4.24.89
-
3.4.24.89
-
difficile
-
metalloprotease
-
diarrhea
-
toxin
-
flagellar
-
scissile
- 3.4.24.89
- difficile
- metalloprotease
-
diarrhea
- toxin
-
flagellar
-
scissile
Reaction
The enzyme catalyses the hydrolytic cleavage of peptide bonds between two proline residues =
Synonyms
CD2830, CD630_28300, PPEP-1, PPEP-2, Pro-Pro endopeptidase, Pro-Pro endopeptidase 1, proline-proline endopeptidase-1, Zmp1
ECTree
3.4.24.89 Pro-Pro endopeptidaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.24.89 - Pro-Pro endopeptidase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-SLRPAPP-CONH2 + H2O
Ac-SLRP + APP-CONH2
fibrinogen beta-derived peptide
-
-
?
Dabcyl-Lys-EVNPPPPD-EdansGlu + H2O
Dabcyl-Lys-EVNP + PPPD-EdansGlu
-
-
-
?
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
-
?
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
?
-
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 CD3246 + H2O
?
-
native CD2830, secreted by live cells, cleaves endogenous CD2831 and CD3246 molecules
-
?
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
?
in vitro assay, presence of Zn2+ required
-
-
?
Fibronectin + H2O
?
in vitro assay, presence of Zn2+ required
-
-
?
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
-
-
?
