D-Ala-D-Ala dipeptidase

D-Ala-D-Ala dipeptidase
Identifiers
EC no.3.4.13.22
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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NCBIproteins

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 PE, Depardieu F, Dutka-Malen S, Arthur M, Courvalin P (September 1994). "Glycopeptide resistance mediated by enterococcal transposon Tn1546 requires production of VanX for hydrolysis of D-alanyl-D-alanine". Molecular Microbiology. 13 (6): 1065–70. doi:10.1111/j.1365-2958.1994.tb00497.x. PMID 7854121.
  2. ^ Wu Z, Wright GD, Walsh CT (February 1995). "Overexpression, purification, and characterization of VanX, a D-, D-dipeptidase which is essential for vancomycin resistance in Enterococcus faecium BM4147". Biochemistry. 34 (8): 2455–63. doi:10.1021/bi00008a008. PMID 7873524.
  3. ^ McCafferty DG, Lessard IA, Walsh CT (August 1997). "Mutational analysis of potential zinc-binding residues in the active site of the enterococcal D-Ala-D-Ala dipeptidase VanX". Biochemistry. 36 (34): 10498–505. doi:10.1021/bi970543u. PMID 9265630.
  4. ^ Bussiere DE, Pratt SD, Katz L, Severin JM, Holzman T, Park CH (July 1998). "The structure of VanX reveals a novel amino-dipeptidase involved in mediating transposon-based vancomycin resistance". Molecular Cell. 2 (1): 75–84. doi:10.1016/s1097-2765(00)80115-x. PMID 9702193.
  5. ^ Tan AL, Loke P, Sim TS (2002). "Molecular cloning and functional characterisation of VanX, a D-alanyl-D-alanine dipeptidase from Streptomyces coelicolor A3(2)". Research in Microbiology. 153 (1): 27–32. doi:10.1016/s0923-2508(01)01282-7. PMID 11881895.
  6. ^ Matthews ML, Periyannan G, Hajdin C, Sidgel TK, Bennett B, Crowder MW (October 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". Journal of the American Chemical Society. 128 (40): 13050–1. doi:10.1021/ja0627343. PMC 2547881. PMID 17017774.