D-alanine—(R)-lactate ligase
Appearance
D-Alanine—(R)-lactate ligase | |||||||||
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Identifiers | |||||||||
EC no. | 6.1.2.1 | ||||||||
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-alanine—(R)-lactate ligase (EC 6.1.2.1, VanA, VanB, VanD) is an enzyme with systematic name D-alanine:(R)-lactate ligase (ADP-forming).[1][2][3] This enzyme catalyses the following chemical reaction
The product of this enzyme can be incorporated into the peptidoglycan pentapeptide instead of the usual D-alanyl-D-alanine dipeptide.
References
[edit]- ^ Bugg TD, Wright GD, Dutka-Malen S, Arthur M, Courvalin P, Walsh CT (October 1991). "Molecular basis for vancomycin resistance in Enterococcus faecium BM4147: biosynthesis of a depsipeptide peptidoglycan precursor by vancomycin resistance proteins VanH and VanA". Biochemistry. 30 (43): 10408–15. doi:10.1021/bi00107a007. PMID 1931965.
- ^ Meziane-Cherif D, Badet-Denisot MA, Evers S, Courvalin P, Badet B (November 1994). "Purification and characterization of the VanB ligase associated with type B vancomycin resistance in Enterococcus faecalis V583". FEBS Letters. 354 (2): 140–2. doi:10.1016/0014-5793(94)01096-x. PMID 7957913.
- ^ Perichon B, Reynolds P, Courvalin P (September 1997). "VanD-type glycopeptide-resistant Enterococcus faecium BM4339". Antimicrobial Agents and Chemotherapy. 41 (9): 2016–8. doi:10.1128/aac.41.9.2016. PMC 164056. PMID 9303405.
External links
[edit]- D-alanine---(R)-lactate+ligase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)