Information on EC 3.4.24.89 - Pro-Pro endopeptidase

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The expected taxonomic range for this enzyme is: Clostridioides difficile

EC NUMBER
COMMENTARY hide
3.4.24.89
-
RECOMMENDED NAME
GeneOntology No.
Pro-Pro endopeptidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
The enzyme catalyses the hydrolytic cleavage of peptide bonds between two proline residues
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-EVNPPVPD + H2O
acetyl-EVNP + PVPD
show the reaction diagram
adhesion molecule CD2831 + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
native CD2830, secreted by live cells, cleaves endogenous CD2831 and CD3246 molecules
-
?
collagen binding protein CD2831 + H2O
PAPPNTDEPIVNP + ?
show the reaction diagram
Dabcyl-Lys-EVNPPPPD-EdansGlu + H2O
Dabcyl-Lys-EVNP + PPPD-EdansGlu
show the reaction diagram
-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
fibrinogen beta-chain + H2O
?
show the reaction diagram
Fibronectin + H2O
?
show the reaction diagram
heat shock protein HSP90beta + H2O
?
show the reaction diagram
-
cleavage between resiudue A702 and A703
-
?
IgA2 heavy chain + H2O
?
show the reaction diagram
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cleavage within the hinge region PVP-PPPPC
-
?
KAAEEPNAAVPDEIK + H2O
KAAEEPNA + AVPDEIK
show the reaction diagram
peptide based on the cleacage site of HSP90beta
-
-
?
LPXTG cell surface protein CD2831 + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
native CD2830, secreted by live cells, cleaves endogenous CD2831 and CD3246 molecules
-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
adhesion molecule CD2831 + H2O
?
show the reaction diagram
Q183R7
-
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
?
show the reaction diagram
Q183R7
-
native CD2830, secreted by live cells, cleaves endogenous CD2831 and CD3246 molecules
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
partly substitutes for Zn2+
Ni2+
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partly substitutes for Zn2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
o-phenanthroline
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.077
Dabcyl-Lys-EVNPPPPD-EdansGlu
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pH 7.4, 3°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19
Dabcyl-Lys-EVNPPPPD-EdansGlu
Clostridioides difficile
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pH 7.4, 3°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Peptoclostridium difficile (strain 630)
Peptoclostridium difficile (strain 630)
Peptoclostridium difficile (strain 630)
Peptoclostridium difficile (strain 630)
Peptoclostridium difficile (strain 630)
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structures of Zmp1 in its unbound and peptide-bound forms. The structure analysis reveals a fold similar to Bacillus anthracis lethal factor. The structure consists of an upper N-terminal domain and a lower helical C-terminal domain with respect to the active-site helix aalpha4, which harbors two of the three zinc-binding residues His142 and His146 and the catalytic base Glu143 in the typical metalloprotease motif (H142E143TAH146)
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in all Peptoclostridium difficile strains tested the cd2830 gene is present
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E143A/Y178F
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complete loss of activity
H146A
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complete loss of the ability to bind Zn2+, highly reduced activity on fibronectin
Y178F
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41% of wild-type activity
E143A
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18% of wild-type activity; mutant displays highly reduced activity on fibronectin, binding of Zn2+ is similar to wild-type
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E143A/Y178F
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complete loss of activity
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H146A
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complete loss of the ability to bind Zn2+, highly reduced activity on fibronectin
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Y178F
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41% of wild-type activity
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