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Literature summary for 3.4.13.22 extracted from

  • Meziane-Cherif, D.; Stogios, P.J.; Evdokimova, E.; Savchenko, A.; Courvalin, P.
    Structural basis for the evolution of vancomycin resistance D,D-peptidases (2014), Proc. Natl. Acad. Sci. USA, 111, 5872-5877.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structures of VanXY mutant D59S and VanXY wild-type in apo and transition state analog-bound forms and of the mutant in complex with the D-Ala-D-Ala substrate and D-Ala product. Structural and biochemical analysis identifies the molecular determinants of VanXY dual specificity acting on dipeptide D-Ala-D-Ala or pentapeptide UDP-MurNac-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala, respectively. VanXY residues 110-115 form a mobile cap over the catalytic site, whose flexibility is involved in the switch between di- and pentapeptide hydrolysis. VanY pentapeptidases lack this element, which promotes binding of the penta- rather than that of the dipeptide Enterococcus faecalis

Organism

Organism UniProt Comment Textmining
Enterococcus faecalis Q9JN36
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information bifunctional enzyme catalyzing the reactions of D-Ala-D-Ala-carboxypeptidase EC 3.4.16.4 and D-Ala-D-Ala-dipeptidase EC 3.4.13.22 Enterococcus faecalis ?
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Synonyms

Synonyms Comment Organism
VanXY
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Enterococcus faecalis