D-Ala-D-Ala dipeptidase
| D-Ala-D-Ala dipeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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
[edit]- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
External links
[edit]- D-Ala-D-Ala+dipeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
