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 (Engineering
Engineering on EC 3.4.24.89 - Pro-Pro endopeptidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E143A
E143A/Y178F
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
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
E143A
E143A/Y178F
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
-
E143A
mutant displays highly reduced activity on fibronectin, binding of Zn2+ is similar to wild-type
E143A
-
mutant displays highly reduced activity on fibronectin, binding of Zn2+ is similar to wild-type
-
