Summary for peptidase M15.011: vanX D-Ala-D-Ala dipeptidase

Summary Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates


MEROPS NamevanX D-Ala-D-Ala dipeptidase
Other namesVanX g.p. (Enterococcus faecium)
Domain architecture
MEROPS Classification
Classification Clan MD >> Subclan (none) >> Family M15 >> Subfamily D >> M15.011
HolotypevanX D-Ala-D-Ala dipeptidase (Enterococcus faecium), Uniprot accession Q06241 (peptidase unit: 50-189), MERNUM MER0001602
History Identifier created: MEROPS 5.5 (16 June 2001)
Catalytic typeMetallo
PeplistIncluded in the Peplist with identifier PL00219
NC-IUBMBSubclass 3.4 (Peptidases) >> Sub-subclass 3.4.13 (Dipeptidases) >> Peptidase
EnzymologyBRENDA database
Pharmaceutical relevanceNecessary for the resistance of some pathogenic bacteria to vancomycin, and hence a target for antibacterial drugs (Arthur et al., 1998).