Crystallization (Comment) | Organism |
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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 | UniProt | Comment | Textmining |
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Enterococcus faecalis | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
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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 | ? | - |
? |
Synonyms | Comment | Organism |
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VanXY | - |
Enterococcus faecalis |