Biology:D-alanine—D-serine ligase

From HandWiki
Short description: Class of enzymes
D-Alanine—D-serine ligase
Identifiers
EC number6.3.2.35
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

D-Alanine—D-serine ligase (EC 6.3.2.35, VanC, VanE, VanG) is an enzyme with systematic 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 [math]\displaystyle{ \rightleftharpoons }[/math] 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. "Sequence of the vanC gene of Enterococcus gallinarum BM4174 encoding a D-alanine:D-alanine ligase-related protein necessary for vancomycin resistance". Gene 112 (1): 53–8. March 1992. doi:10.1016/0378-1119(92)90302-6. PMID 1551598. 
  2. "Bacterial resistance to vancomycin: overproduction, purification, and characterization of VanC2 from Enterococcus casseliflavus as a D-Ala-D-Ser ligase". Proceedings of the National Academy of Sciences of the United States of America 94 (19): 10040–4. September 1997. doi:10.1073/pnas.94.19.10040. PMID 9294159. Bibcode1997PNAS...9410040P. 
  3. "VanE, a new type of acquired glycopeptide resistance in Enterococcus faecalis BM4405". Antimicrobial Agents and Chemotherapy 43 (9): 2161–4. September 1999. doi:10.1128/aac.43.9.2161. PMID 10471558. 
  4. "The vanG glycopeptide resistance operon from Enterococcus faecalis revisited". Molecular Microbiology 50 (3): 931–48. November 2003. doi:10.1046/j.1365-2958.2003.03737.x. PMID 14617152. 
  5. "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". Microbial Drug Resistance 15 (1): 1–9. March 2009. doi:10.1089/mdr.2009.0856. PMID 19216682. 

External links