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
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3.4.24.89
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difficile
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metalloprotease
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diarrhea
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toxin
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flagellar
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scissile
- 3.4.24.89
- difficile
- metalloprotease
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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
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Natural Substrates Products
Natural Substrates Products on EC 3.4.24.89 - Pro-Pro endopeptidase
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REACTION DIAGRAM
Ac-SLRPAPP-CONH2 + H2O
Ac-SLRP + APP-CONH2
fibrinogen beta-derived peptide
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?
Ac-EPNA + AVP-CONH2
heat shock protein 90-derived peptide
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?
Ac-EPNAAVP-CONH2 + H2O
Ac-EPNA + AVP-CONH2
heat shock protein 90-derived peptide
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?
Ac-HLLP + PPS-CONH2
immunoglobulin A1-derived peptide
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?
Ac-HLLPPPS-CONH2 + H2O
Ac-HLLP + PPS-CONH2
immunoglobulin A1-derived peptide
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adhesion molecule CD2831 + H2O
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native CD2830, secreted by live cells, cleaves endogenous CD2831 and CD3246 molecules. Enzyme efficiently cleaves CD2831 between two prolines at all predicted cleavage sites
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adhesion molecule CD3246 + H2O
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native CD2830, secreted by live cells, cleaves endogenous CD2831 and CD3246 molecules
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?
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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
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additional information
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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
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-
?
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
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-
?
additional information
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the enzyme cleaves between two prolines in a PLPPVP motif
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additional information
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the enzyme cleaves between two prolines in a PLPPVP motif
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?
additional information
?
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the enzyme cleaves between two prolines in a PLPPVP motif
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?