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Literature summary for 3.4.24.89 extracted from

  • 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 (2013), PLoS One, 8, e81306.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.89

Cloned(Commentary)

Cloned (Comment) Organism
-
 Clostridioides difficile

Protein Variants

Protein Variants Comment Organism
E143A mutant displays highly reduced activity on fibronectin, binding of Zn2+ is similar to wild-type Clostridioides difficile
H146A complete loss of the ability to bind Zn2+, highly reduced activity on fibronectin Clostridioides difficile

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ partly substitutes for Zn2+ Clostridioides difficile
Ni2+ partly substitutes for Zn2+ Clostridioides difficile
Zn2+ required Clostridioides difficile

Organism

Organism UniProt Comment Textmining
Clostridioides difficile Q183R7
-
-
Clostridioides difficile 630 Q183R7
-
-

Source Tissue

Source Tissue Comment Organism Textmining
culture fluid
-
 Clostridioides difficile
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Fibrinogen + H2O in vitro assay, presence of Zn2+ required Clostridioides difficile ?
-
 ?
Fibrinogen + H2O in vitro assay, presence of Zn2+ required Clostridioides difficile 630 ?
-
 ?
Fibronectin + H2O in vitro assay, presence of Zn2+ required Clostridioides difficile ?
-
 ?
Fibronectin + H2O in vitro assay, presence of Zn2+ required Clostridioides difficile 630 ?
-
 ?

Synonyms

Synonyms Comment Organism
CD630_28300
-
 Clostridioides difficile
Zmp1
-
 Clostridioides difficile

General Information

General Information Comment Organism
physiological function enzyme destabilizes the fibronectin network produced by human fibroblast Clostridioides difficile