KEGG   ENZYME: 6.3.2.35Help
Entry
EC 6.3.2.35                 Enzyme                                 

Name
D-alanine---D-serine ligase;
VanC;
VanE;
VanG
Class
Ligases;
Forming carbon-nitrogen bonds;
Acid-D-amino-acid ligases (peptide synthases)
BRITE hierarchy
Sysname
D-alanine:D-serine ligase (ADP-forming)
Reaction(IUBMB)
D-alanine + D-serine + ATP = D-alanyl-D-serine + ADP + phosphate [RN:R09595]
Reaction(KEGG)
Substrate
D-alanine [CPD:C00133];
D-serine [CPD:C00740];
ATP [CPD:C00002]
Product
D-alanyl-D-serine [CPD:C19719];
ADP [CPD:C00008];
phosphate [CPD:C00009]
Comment
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, 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.
History
EC 6.3.2.35 created 2010
Orthology
K18856  D-alanine---D-serine ligase
Genes
BBE: BBR47_05870
BFM: BP422_28590(vanB)
PBJ: VN24_01315(vanB)
SANS: DK43_03860(vanB)
ECAS: ECBG_02849
EGA: AL523_09465
CLB: Clo1100_2030
CACE: CACET_c25480(vanA)
CFM: BJL90_20410(vanB)
CARG: RSJ17_11295(vanB)
AOE: Clos_2860
FPLA: A4U99_10115(vanB)
CLE: Clole_1511
CSO: CLS_04660
HSD: SD1D_0541(ddl2)
CDF: CD630_16260(vanG)
PDC: CDIF630_01803(vanG)
CDC: CD196_1549(vanG)
CDL: CDR20291_1524(vanG)
PDF: CD630DERM_16260(vanG)
DGI: Desgi_1749
OVA: OBV_09510
IBU: IB211_01760
CAD: Curi_c05060(vanG)
EUC: EC1_04100
AARG: Aargi30884_01290(vanG)
ABSI: A9CBEGH2_02850(vanG)
 » show all
Taxonomy
Reference
1  [PMID:1551598]
  Authors
Dutka-Malen S, Molinas C, Arthur M, Courvalin P
  Title
Sequence of the vanC gene of Enterococcus gallinarum BM4174 encoding a D-alanine:D-alanine ligase-related protein necessary for vancomycin resistance.
  Journal
Gene 112:53-8 (1992)
DOI:10.1016/0378-1119(92)90302-6
  Sequence
Reference
2  [PMID:9294159]
  Authors
Park IS, Lin CH, Walsh CT
  Title
Bacterial resistance to vancomycin: overproduction, purification, and characterization of VanC2 from Enterococcus casseliflavus as a D-Ala-D-Ser ligase.
  Journal
Proc Natl Acad Sci U S A 94:10040-4 (1997)
DOI:10.1073/pnas.94.19.10040
Reference
3  [PMID:10471558]
  Authors
Fines M, Perichon B, Reynolds P, Sahm DF, Courvalin P
  Title
VanE, a new type of acquired glycopeptide resistance in Enterococcus faecalis BM4405.
  Journal
Antimicrob Agents Chemother 43:2161-4 (1999)
Reference
4  [PMID:14617152]
  Authors
Depardieu F, Bonora MG, Reynolds PE, Courvalin P
  Title
The vanG glycopeptide resistance operon from Enterococcus faecalis revisited.
  Journal
Mol Microbiol 50:931-48 (2003)
DOI:10.1046/j.1365-2958.2003.03737.x
Reference
5  [PMID:19216682]
  Authors
Watanabe S, Kobayashi N, Quinones D, Hayakawa S, Nagashima S, Uehara N, Watanabe N
  Title
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.
  Journal
Microb Drug Resist 15:1-9 (2009)
DOI:10.1089/mdr.2009.0856
Other DBs
ExplorEnz - The Enzyme Database: 6.3.2.35
IUBMB Enzyme Nomenclature: 6.3.2.35
ExPASy - ENZYME nomenclature database: 6.3.2.35
BRENDA, the Enzyme Database: 6.3.2.35
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