3.4.13.22: D-Ala-D-Ala dipeptidase
This is an abbreviated version!
For detailed information about D-Ala-D-Ala dipeptidase, go to the full flat file.
Word Map on EC 3.4.13.22
-
3.4.13.22
-
dipeptide
-
enterococci
-
vancomycin-resistant
-
peptidoglycan
-
medicine
-
d-alanyl-d-lactate
-
d-ala-d-lactate
-
glycopeptide
-
faecium
-
carboxypeptidase
-
zinc-dependent
-
cell-wall
-
zinc-containing
-
toyocaensis
-
tetrahedral
-
depsipeptide
-
uv-vis
-
l-ala-l-ala
-
thiophenol
-
hedgehog
-
enterica
-
albus
-
vanhax
-
kinact
-
d,d-dipeptidase
-
phosphinate
-
synthesis
-
analysis
- 3.4.13.22
- dipeptide
-
enterococci
-
vancomycin-resistant
- peptidoglycan
- medicine
-
d-alanyl-d-lactate
- d-ala-d-lactate
- glycopeptide
- faecium
- carboxypeptidase
-
zinc-dependent
-
cell-wall
-
zinc-containing
- toyocaensis
-
tetrahedral
-
depsipeptide
-
uv-vis
- l-ala-l-ala
- thiophenol
-
hedgehog
- enterica
-
albus
-
vanhax
-
kinact
- d,d-dipeptidase
- phosphinate
- synthesis
- analysis
Reaction
Synonyms
AAD, D-, D-dipeptidase, D-Ala-D-Ala amino dipeptidase, D-Ala-D-Ala dipeptidase, D-Ala-D-Ala dipeptidase VanX, D-Ala-D-Ala-dipeptidase, D-alanyl-D-alanine dipeptidase, M15.011, MAB1843, Vancomycin B-type resistance protein vanX, VanX, VanXY, VanXYc
ECTree
Advanced search results
General Information
General Information on EC 3.4.13.22 - D-Ala-D-Ala dipeptidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
physiological function
-
exogenous D-Ala competes with D-Lac as a substrate for ligase VanA and reduces vancomycin resistance. The effect is augmented by several orders of magnitude in the absence of the D-Ala-D-Ala peptidase VanX. High concentrations of D-Ala lead to the production of a significant amount of wild-type cell wall precursors, while vanX-null mutants produce primarily wild-type precursors. This enhances the efficacy of vancomycin in the vancomycin-resistant model organism Streptomyces coelicolor, and the susceptibility of vancomycin-resistant clinical isolates of Enterococcus faecium increases by up to 100fold. The enhanced vancomycin sensitivity of Streptomyces coelicolor cells correlates directly to increased binding of the antibiotic to the cell wall
physiological function
Mycobacterium abscessus is an pulmonary pathogen in humans. The enzyme induces dendritic maturation via toll-like receptor 4 and its downstream signaling pathways, such as the mitogen-activated protein kinase and nuclear factor kappa B pathways. Enzyme-treated dendritic cells stimulate the proliferation of T cells and promote Th1 polarization
physiological function
-
Mycobacterium abscessus is an pulmonary pathogen in humans. The enzyme induces dendritic maturation via toll-like receptor 4 and its downstream signaling pathways, such as the mitogen-activated protein kinase and nuclear factor kappa B pathways. Enzyme-treated dendritic cells stimulate the proliferation of T cells and promote Th1 polarization
-
physiological function
-
exogenous D-Ala competes with D-Lac as a substrate for ligase VanA and reduces vancomycin resistance. The effect is augmented by several orders of magnitude in the absence of the D-Ala-D-Ala peptidase VanX. High concentrations of D-Ala lead to the production of a significant amount of wild-type cell wall precursors, while vanX-null mutants produce primarily wild-type precursors. This enhances the efficacy of vancomycin in the vancomycin-resistant model organism Streptomyces coelicolor, and the susceptibility of vancomycin-resistant clinical isolates of Enterococcus faecium increases by up to 100fold. The enhanced vancomycin sensitivity of Streptomyces coelicolor cells correlates directly to increased binding of the antibiotic to the cell wall
-
physiological function
-
exogenous D-Ala competes with D-Lac as a substrate for ligase VanA and reduces vancomycin resistance. The effect is augmented by several orders of magnitude in the absence of the D-Ala-D-Ala peptidase VanX. High concentrations of D-Ala lead to the production of a significant amount of wild-type cell wall precursors, while vanX-null mutants produce primarily wild-type precursors. This enhances the efficacy of vancomycin in the vancomycin-resistant model organism Streptomyces coelicolor, and the susceptibility of vancomycin-resistant clinical isolates of Enterococcus faecium increases by up to 100fold. The enhanced vancomycin sensitivity of Streptomyces coelicolor cells correlates directly to increased binding of the antibiotic to the cell wall
-