EC Number   |
Application |
Reference |
|---|
    3.4.13.22 | analysis |
although catalytically ineffecient, the VanX substrate D-leucine-p-nitroanilide is an alternative substrate for VanX because it can be monitored directly and assayed spectrophotometrically which facilitates the routine analysis of enzyme catalysis and the screening discovery of potential VanX inhibitors. In addition, it is with leucine in its D form that possible activities from other contaminated species (other than VanX) in Escherichia coli JM109 are greatly reduced. Moreover, D-leucine-p-nitroanilide needs essentially no sophisticated synthetic chemistry for preparation |
667195 |
| 3.4.13.22 | analysis |
continuous assay of VanX in vitro and in vivo from hydrolysis of D-Ala-D-Ala, based on the heat-rate changes measured with isothermal titration calorimetry |
752475 |
| 3.4.13.22 | medicine |
Enterecoccus faecium carrying plasmid pHVH-V1511 is capable of nosocomial transmission and may develop clinical resistance to vancomycin. Strains may not be detected using standard culture methods for vancomycin-resistant enterococci |
753985 |
| 3.4.13.22 | medicine |
enzyme may be a target for drug design to reverse clinical vancomycin resistance |
36315 |
| 3.4.13.22 | medicine |
key drug target in circumventing clinical vancomycin resistance |
653196 |
| 3.4.13.22 | medicine |
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 |
-, 753076 |
| 3.4.13.22 | medicine |
VanX is an excellent target for the generation of inhibitors |
683586 |
| 3.4.13.22 | synthesis |
novel cell breakage method based on VanX. The D-Ala-D-Ala dipeptidase encoded in a vancomycin-resistant VanA gene cluster, exhibits a strong cell lysis activity when expressed in isolation in Escherichia coli. Coexpression of VanX with the target protein causes cell autolysis and release of the cellular content into the culture medium. Application of this strategy for two model proteins, a green fluorescent protein variant and Gaussia luciferase, and optimization of the autolysis conditions and coexpression vectors shows that the fluorescence activity of green fluorescent protein variant collected from the medium is identical to that of green fluorescent protein variant purified by conventional methods. Cell breakage by VanX-mediated autolysis is very simple to implement and will efficiently complement traditional methods |
731122 |
| 3.4.13.22 | synthesis |
strong bacteriolysis occurrs when isolated VanX is expressed in Escherichia coli at temperatures lower than 30°C. No cell lysis is observed when VanX is expressed, even in large quantities, in the cell inclusion bodies at 37°C, suggesting that a natively folded VanX is required for lysis. In addition, VanX mutants with suppressed dipeptidase activity do not lyse Escherichia coli cells, confirming that bacteriolysis originates from the dipeptidase activity of VanX. There are also shape changes in Escherichia coli cells undergoing VanX-mediated lysis, these changes may be classified into three classes: bursting, deformation, and leaking fluid |
732161 |
