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
Search PMC articles PubMed articles NCBI proteins

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 $\rightleftharpoons$ 2 D-Ala

This enzyme is Zn²⁺-dependent.

References

1. Reynolds, P.E., Depardieu, F., Dutka-Malen, S., Arthur, M. and 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. and 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. and 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. and 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. and 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. and 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

• D-Ala-D-Ala dipeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)