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Literature summary for 3.1.4.52 extracted from

  • Bordeleau, E.; Fortier, L.; Malouin, F.; Burrus, V.
    c-di-GMP turn-over in Clostridium difficile is controlled by a plethora of diguanylate cyclases and phosphodiesterases (2011), PLoS Genet., 7, e1002039.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.4.52

Activating Compound

Activating Compound Comment Organism Structure
GTP required by PDE CD0757 Clostridioides difficile

Cloned(Commentary)

Cloned (Comment) Organism
ectopic expression of 31 of the conserved genes from 20 genomes of Clostridium difficile for comparison of their effect on motility and biofilm formation. Most of the PDEs are active in a Vibrio cholerae model Clostridioides difficile

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cyclic di-3',5'-guanylate + H2O Clostridioides difficile
-
 5'-phosphoguanylyl(3'-5')guanosine
-
 ?

Organism

Organism UniProt Comment Textmining
Clostridioides difficile
-
 sveral strains
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cyclic di-3',5'-guanylate + H2O
-
 Clostridioides difficile 5'-phosphoguanylyl(3'-5')guanosine
-
 ?
additional information CD0522 has dual enzymatic activity, as cyclic di-GMP phosphodiestrase and as diguanylate cyclase Clostridioides difficile ?
-
 ?

Synonyms

Synonyms Comment Organism
CD0757
-
 Clostridioides difficile
PDE
-
 Clostridioides difficile

General Information

General Information Comment Organism
physiological function Clostridium difficile encodes a large assortment of functional DGCs and PDEs, revealing that cyclic di-GMP signalling is an important and well-conserved signal transduction system in the human pathogen. The second messenger cyclic di-3',5'-guanylate is degraded by phosphodiesterases that contain either an EAL or an HD-GYP conserved domain Clostridioides difficile