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Literature summary for 3.2.1.B37 extracted from

  • Dhalluin, A.; Bourgeois, I.; Pestel-Caron, M.; Camiade, E.; Raux, G.; Courtin, P.; Chapot-Chartier, M.P.; Pons, J.L.
    Acd, a peptidoglycan hydrolase of Clostridium difficile with N-acetylglucosaminidase activity (2005), Microbiology, 151, 2343-2351.
    View publication on PubMed
Search for more literature for 3.2.1.B37

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Clostridioides difficile

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
64000
-
 x * 65852, calculated, x * 64000, SDS-PAGE Clostridioides difficile
65852
-
 x * 65852, calculated, x * 64000, SDS-PAGE Clostridioides difficile

Organism

Organism UniProt Comment Textmining
Clostridioides difficile Q5S4P9
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification first 22 N-terminal residues of the protein encode a putative signal sequence or an N-terminal signal anchor sequence Clostridioides difficile

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Bacillus subtilis 168 HR cell wall + H2O enzyme hydrolyses peptidoglycan bonds between N-acetylglucosamine and N-acetylmuramic acid. Enzyme does not possess muraminidase activity Clostridioides difficile soluble muropeptides
-
 ?

Subunits

Subunits Comment Organism
? x * 65852, calculated, x * 64000, SDS-PAGE Clostridioides difficile
More deduced amino acid sequence of Acd shows a modular structure with an N-terminal domain exhibiting repeated sequences and a C-terminal catalytic domain Clostridioides difficile

Synonyms

Synonyms Comment Organism
ACD
-
 Clostridioides difficile
Autolysin
-
 Clostridioides difficile
N-acetylglucosaminidase
-
 Clostridioides difficile

pI Value

Organism Comment pI Value Maximum pI Value
Clostridioides difficile calculated
-
 9.5

Expression

Organism Comment Expression
Clostridioides difficile transcription of the Acd gene increases during vegetative cellular growth up

General Information

General Information Comment Organism
physiological function enzyme is a cell-wall hydrolase with lytic activity on the peptidoglycan of several Gram-positive bacteria, including Clostridium difficile. Enzyme hydrolyses peptidoglycan bonds between N-acetylglucosamine and N-acetylmuramic acid Clostridioides difficile