The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

EC 6.1.2.1     
Accepted name: D-alanine—(R)-lactate ligase
Reaction: D-alanine + (R)-lactate + ATP = D-alanyl-(R)-lactate + ADP + phosphate
Glossary: (R)-lactate = D-lactate
D-alanyl-(R)-lactate = D-alanyl-D-lactate = (2R)-2-(D-alanyloxy)propanoic acid = (R)-2-((R)-2-aminopropanoyloxy)propanoic acid
Other name(s): VanA; VanB; VanD
Systematic name: D-alanine:(R)-lactate ligase (ADP-forming)
Comments: The product of this enzyme, the depsipeptide D-alanyl-(R)-lactate, can be incorporated into the peptidoglycan pentapeptide instead of the usual D-alanyl-D-alanine dipeptide, which is formed by EC 6.3.2.4, D-alanine—D-alanine ligase. The resulting peptidoglycan does not bind the glycopeptide antibiotics vancomycin and teicoplanin, conferring resistance on the bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bugg, T.D., Wright, G.D., Dutka-Malen, S., Arthur, M., Courvalin, P. and Walsh, C.T. Molecular basis for vancomycin resistance in Enterococcus faecium BM4147: biosynthesis of a depsipeptide peptidoglycan precursor by vancomycin resistance proteins VanH and VanA. Biochemistry 30 (1991) 10408–10415. [PMID: 1931965]
2.  Meziane-Cherif, D., Badet-Denisot, M.A., Evers, S., Courvalin, P. and Badet, B. Purification and characterization of the VanB ligase associated with type B vancomycin resistance in Enterococcus faecalis V583. FEBS Lett. 354 (1994) 140–142. [PMID: 7957913]
3.  Perichon, B., Reynolds, P. and Courvalin, P. VanD-type glycopeptide-resistant Enterococcus faecium BM4339. Antimicrob. Agents Chemother. 41 (1997) 2016–2018. [PMID: 9303405]
[EC 6.1.2.1 created 2010]
 
 


Data © 2001–2017 IUBMB
Web site © 2005–2017 Andrew McDonald