D-alanine—D-serine ligase

D-alanine—D-serine ligase
Identifiers
EC number 6.3.2.35
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-alanine—D-serine ligase (EC 6.3.2.35, VanC, VanE, VanG) is an enzyme with system name D-alanine:D-serine ligase (ADP-forming).[1][2][3][4][5] This enzyme catalyses the following chemical reaction

D-alanine + D-serine + ATP \rightleftharpoons D-alanyl-D-serine + ADP + phosphate

The product of this enzyme, D-alanyl-D-serine, can be incorporated into the peptidoglycan pentapeptide instead of the usual D-alanyl-D-alanine dipeptide.

References

  1. ↑ Dutka-Malen, S., Molinas, C., Arthur, M. and Courvalin, P. (1992). "Sequence of the vanC gene of Enterococcus gallinarum BM4174 encoding a D-alanine:D-alanine ligase-related protein necessary for vancomycin resistance". Gene 112: 53–58. doi:10.1016/0378-1119(92)90302-6. PMID 1551598.
  2. ↑ Park, I.S., Lin, C.H. and Walsh, C.T. (1997). "Bacterial resistance to vancomycin: overproduction, purification, and characterization of VanC2 from Enterococcus casseliflavus as a D-Ala-D-Ser ligase". Proc. Natl. Acad. Sci. USA 94: 10040–10044. doi:10.1073/pnas.94.19.10040. PMID 9294159.
  3. ↑ Fines, M., Perichon, B., Reynolds, P., Sahm, D.F. and Courvalin, P. (1999). "VanE, a new type of acquired glycopeptide resistance in Enterococcus faecalis BM4405". Antimicrob. Agents Chemother. 43: 2161–2164. PMID 10471558.
  4. ↑ Depardieu, F., Bonora, M.G., Reynolds, P.E. and Courvalin, P. (2003). "The vanG glycopeptide resistance operon from Enterococcus faecalis revisited". Mol. Microbiol. 50: 931–948. doi:10.1046/j.1365-2958.2003.03737.x. PMID 14617152.
  5. ↑ Watanabe, S., Kobayashi, N., Quinones, D., Hayakawa, S., Nagashima, S., Uehara, N. and Watanabe, N. (2009). "Genetic diversity of the low-level vancomycin resistance gene vanC-2/vanC-3 and identification of a novel vanC subtype (vanC-4) in Enterococcus casseliflavus". Microb. Drug Resist. 15: 1–9. doi:10.1089/mdr.2009.0856. PMID 19216682.

External links