Information on EC 6.3.2.35 - D-alanine-D-serine ligase

Word Map on EC 6.3.2.35
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Enterococcus

EC NUMBER
COMMENTARY hide
6.3.2.35
-
RECOMMENDED NAME
GeneOntology No.
D-alanine-D-serine ligase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-alanine + D-serine + ATP = D-alanyl-D-serine + ADP + phosphate
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
vancomycin resistance II
-
-
SYSTEMATIC NAME
IUBMB Comments
D-alanine:D-serine ligase (ADP-forming)
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain BM4518
-
-
Manually annotated by BRENDA team
isolated from a blood culture
-
-
Manually annotated by BRENDA team
isolated from a blood culture
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-alanine + D-2-aminobutanoate + ATP
D-alanyl-D-2-aminobutanoate + ADP + phosphate
show the reaction diagram
-
-
-
-
?
D-alanine + D-alanine + ATP
D-alanyl-D-alanine + ADP + phosphate
show the reaction diagram
-
formation of D-alanyl-D-serine is 400fold prefered over formation of D-alanyl-D-alanine
-
-
?
D-alanine + D-allo-threonine + ATP
D-alanyl-D-allo-threonine + ADP + phosphate
show the reaction diagram
-
-
-
-
?
D-alanine + D-asparagine + ATP
D-alanyl-D-asparagine + ADP + phosphate
show the reaction diagram
-
-
-
-
?
D-alanine + D-glutamine + ATP
D-alanyl-D-glutamine + ADP + phosphate
show the reaction diagram
-
-
-
-
?
D-alanine + D-homoserine + ATP
D-alanyl-D-homoserine + ADP + phosphate
show the reaction diagram
-
-
-
-
?
D-alanine + D-serine + ATP
D-alanyl-D-serine + ADP + phosphate
show the reaction diagram
D-alanine + D-threonine + ATP
D-alanyl-D-threonine + ADP + phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
amino acid preference in decreasing order: D-Ser, D-Asn, D-Thr, D-Gln, D-homoserine, D-aminobutanoate, D-allo-Thr
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-alanine + D-serine + ATP
D-alanyl-D-serine + ADP + phosphate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.2
D-asparagine
-
pH 7.5
1.8
D-serine
-
pH 7.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.87
D-asparagine
Enterococcus casseliflavus
-
pH 7.5
8.17
D-serine
Enterococcus casseliflavus
-
pH 7.5
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.23
D-asparagine
Enterococcus casseliflavus
-
pH 7.5
2194
4.5
D-serine
Enterococcus casseliflavus
-
pH 7.5
481
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39932
-
x * 39947, MALDI-TOF, x * 39932, calculated for His-tagged protein
39947
-
x * 39947, MALDI-TOF, x * 39932, calculated for His-tagged protein
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 2.35 A resolution, P3121 or P3221, with unit-cell parameters a and b 116.1, c 177.2 A
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant protein
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
vanL, chromosomal localization, belongs to the vanN operon, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons with VanN-type proteins, phylogenetic analysis
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the vanE operon comprises five genes, with three of them, VanE, VanXYE, and VanTE being sufficient to confer vancomycin resistance whereas the last two encode a two-component system postulated to regulate expression of the operon
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
of 7271 Enterococcus-containing clinical samples collected between 2004 and 2009, 16 vancomycin resistant enterococci were identified. The vanC1 resistance gene was found in 14 Enterococcus gallinarum and the vanC2 resistance gene in two Enterococcus casseliflavus strains. Except for two samples, the isolates have different pulsed-field gel electrophoresis types, suggesting sporadic emergence of the resistant bacteria