Biology:D-Ala-D-Ala dipeptidase
From HandWiki
| 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 | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] 2 D-Ala
This enzyme is Zn2+-dependent.
References
- ↑ "Glycopeptide resistance mediated by enterococcal transposon Tn1546 requires production of VanX for hydrolysis of D-alanyl-D-alanine". Molecular Microbiology 13 (6): 1065–70. September 1994. doi:10.1111/j.1365-2958.1994.tb00497.x. PMID 7854121.
- ↑ "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. February 1995. doi:10.1021/bi00008a008. PMID 7873524.
- ↑ "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. August 1997. doi:10.1021/bi970543u. PMID 9265630.
- ↑ "The structure of VanX reveals a novel amino-dipeptidase involved in mediating transposon-based vancomycin resistance". Molecular Cell 2 (1): 75–84. July 1998. doi:10.1016/s1097-2765(00)80115-x. PMID 9702193.
- ↑ "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. 2002. doi:10.1016/s0923-2508(01)01282-7. PMID 11881895.
- ↑ "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. October 2006. doi:10.1021/ja0627343. PMID 17017774.
External links
- D-Ala-D-Ala+dipeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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