D-Ala-D-Ala dipeptidase

D-Ala-D-Ala dipeptidase
Identifiers
EC number 3.4.13.22
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

D-Ala-D-Ala dipeptidase (EC 3.4.13.22, D-alanyl-D-alanine dipeptidase, vanX D-Ala-D-Ala dipeptidase, VanX) is an enzyme.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction

D-Ala-D-Ala + H2O 2 D-Ala

This enzyme is Zn2+-dependent.

References

  1. Reynolds, P.E.; Depardieu, F.; Dutka-Malen, S.; Arthur, M.; Courvalin, P. (1994). "Glycopeptide resistance mediated by enterococcal transposon Tn1546 requires production of VanX for hydrolysis of D-alanyl-D-alanine". Mol. Microbiol. 13: 1065–1070. doi:10.1111/j.1365-2958.1994.tb00497.x. PMID 7854121.
  2. Wu, Z.; Wright, G.D.; Walsh, C.T. (1995). "Overexpression, purification, and characterization of VanX, a D-, D-dipeptidase which is essential for vancomycin resistance in Enterococcus faecium BM4147". Biochemistry. 34: 2455–2463. doi:10.1021/bi00008a008. PMID 7873524.
  3. McCafferty, D.G.; Lessard, I.A.; Walsh, C.T. (1997). "Mutational analysis of potential zinc-binding residues in the active site of the enterococcal D-Ala-D-Ala dipeptidase VanX". Biochemistry. 36: 10498–10505. doi:10.1021/bi970543u. PMID 9265630.
  4. Bussiere, D.E.; Pratt, S.D.; Katz, L.; Severin, J.M.; Holzman, T.; Park, C.H. (1998). "The structure of VanX reveals a novel amino-dipeptidase involved in mediating transposon-based vancomycin resistance". Mol. Cell. 2: 75–84. doi:10.1016/s1097-2765(00)80115-x. PMID 9702193.
  5. Tan, A.L.; Loke, P.; Sim, T.S. (2002). "Molecular cloning and functional characterisation of VanX, a D-alanyl-D-alanine dipeptidase from Streptomyces coelicolor A3(2)". Res. Microbiol. 153: 27–32. doi:10.1016/s0923-2508(01)01282-7. PMID 11881895.
  6. Matthews, M.L.; Periyannan, G.; Hajdin, C.; Sidgel, T.K.; Bennett, B.; Crowder, M.W. (2006). "Probing the reaction mechanism of the D-ala-D-ala dipeptidase, VanX, by using stopped-flow kinetic and rapid-freeze quench EPR studies on the Co(II)-substituted enzyme". J. Am. Chem. Soc. 128: 13050–13051. doi:10.1021/ja0627343. PMID 17017774.

External links

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