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Literature summary for 3.4.17.13 extracted from

  • Frirdich, E.; Vermeulen, J.; Biboy, J.; Soares, F.; Taveirne, M.E.; Johnson, J.G.; DiRita, V.J.; Girardin, S.E.; Vollmer, W.; Gaynor, E.C.
    Peptidoglycan LD-carboxypeptidase Pgp2 influences Campylobacter jejuni helical cell shape and pathogenic properties and provides the substrate for the DL-carboxypeptidase Pgp1 (2014), J. Biol. Chem., 289, 8007-8018.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Campylobacter jejuni

Organism

Organism UniProt Comment Textmining
Campylobacter jejuni
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information isoform Pgp2 is a LD-carboxypeptidase cleaving monomeric and cross-linked disaccharide tetrapeptides to tripeptides Campylobacter jejuni ?
-
?
muropeptides + H2O
-
Campylobacter jejuni ? incubation of isoform Pgp2 with peptidglucan from the Pgp2 mutant strain results in a 94% reduction of monomeric tetrapeptides, a 68% reduction in dimeric tetrapeptides, and a 47% reduction in trimeric tetrapeptides ?

Subunits

Subunits Comment Organism
? x *37800, calculated Campylobacter jejuni

Synonyms

Synonyms Comment Organism
cjj81176_0915
-
Campylobacter jejuni
Pgp2
-
Campylobacter jejuni

General Information

General Information Comment Organism
physiological function a LD-carboxypeptidase isoform Pgp2 mutant shows an increase in tetrapeptide-containing muropeptides and a complete absence of tripeptides in the peptidoglycan structure, consistent with LD-carboxypeptidase activity. An isoform Pgp1Pgp2 double mutant demonstrates that Pgp2 activity is required to generate the tripeptide substrate for Pgp1. Loss of Pgp2 affects several pathogenic properties, the deletion strain is defective for motility in semisolid agar, biofilm formation, and fluorescence on calcofluor white. Isoform Pgp2 peptidoglucan also causes decreased stimulation of the human nucleotide-binding oligomerization domain 1 (Nod1) proinflammatory mediator in comparison with wild type, these changes do not alter the ability of the Pgp2 mutant strain to survive within human epithelial cells or to elicit secretion of IL-8 from epithelial cells after infection. The Pgp2 mutant also shows significantly reduced fitness in a chick colonization model Campylobacter jejuni