KEGG   ENZYME: 6.3.2.35
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)
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)
R09595
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
CGOTJ1899_06180(vanG)
BBEBBR47_05870
BFMBP422_28590(vanB)
PBJVN24_01315(vanB)
PSOPKP014_14540(vanG)
CHEBHH215_23270(vanG)
SANSDK43_03860(vanB)
ECASECBG_02849
EGAAL523_09465
EIEENLAB_26750(ddlA_2)
VCPH9L18_13855(vanC)
VFVK5K99_04105(vanC)
CLBClo1100_2030
CACECACET_c25480(vanA)
CFMBJL90_20410(vanB)
CARGRSJ17_11295(vanB)
AOEClos_2860
FPLAA4U99_10115(vanB)
RGVNQ502_15010(vanG)
OVAOBV_09510
PFAAMM59RIKEN_12790(vanG)
VCOPMM50RIKEN_08120(vanG)
CFEMHCR03_19250(vanG)
LASAL9O85_05970
CLEClole_1511
CSOCLS_04660
HSDSD1D_0541(ddl2)
ACELacsn021_25810(vanG)
ACHTbsdcttw_22890(vanG)
QDOH9Q78_03830(vanG)
WHJH9Q79_01750(vanG)
CDFCD630_16260(vanG)
PDCCDIF630_01803(vanG)
CDCCD196_1549(vanG)
CDLCDR20291_1524(vanG)
PDFCD630DERM_16260(vanG)
CALKHUE98_13540(vanG)
DGIDesgi_1749
VGUHYG85_23280(vanG)
IBUIB211_01760
ABUTAmi103574_02975(vanG) Ami103574_07960(vanG)
ETMCE91St48_02960(vanG)
CADCuri_c05060(vanG)
SEDZJYG23_10725
EUCEC1_04100
AARGAargi30884_01290(vanG)
ABSIA9CBEGH2_02850(vanG)
CIUG4D55_13020
ERMEYR00_02855(vanG)
LCGL3BBH23_19070(vanG)
ERBA4V01_15880
RTSCE91St31_07130(vanG)
TPERIWA51_01115
 » show all
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)
DOI:10.1128/AAC.43.9.2161
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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