EC Number   |
General Information |
Reference |
|---|
   3.1.4.59 | physiological function |
a Pde2 mutant strain displays a growth defect in the early growth phase. Mutation leads to an increase in cellular c-di-AMP and 5'-O-phosphonoadenylyl-(3'->5')-adenosine levels and increased resistance to oxacillin |
-, 751077 |
| 3.1.4.59 | physiological function |
both phosphodiesterases, GdpP and PgpH, contribute to the degradation of cyclic di-AMP. Accumulation of cyclic di-AMP in a GdpP PgpH double mutant is toxic for the cells, and the cells respond to accumulation by inactivation of the diadenylate cyclase CdaA |
-, 750959 |
| 3.1.4.59 | physiological function |
both phosphodiesterases, GdpP and PgpH, contribute to the degradation of cyclic di-AMP. Accumulation of cyclic di-AMP in a GdpP PgpH double mutant is toxic for the cells, and the cells respond to this accumulation by inactivation of the diadenylate cyclase CdaA |
-, 750959 |
| 3.1.4.59 | physiological function |
deficiency of Pde significantly enhances intracellular C12-C20 fatty acid accumulation. Superfluous c-di-AMP in Mycobacterium smegmatis may lead to abnormal colonial morphology |
-, 750844 |
| 3.1.4.59 | physiological function |
deletion of either isoform Pde1 or Pde2 results in a moderate increase of the c-di-AMP levels compared with the parental strain. Deletion of both genes results in an up to 4fold increase in c-di-AMP levels compared to that of the parental strain. Both Pde1 and Pde2 play a role in pneumococcal growth. Deletion of either isoform Pde1 or Pde2 reduces the growth rate slightly, and the double mutant synergizes the reduction |
750954 |
| 3.1.4.59 | physiological function |
deletion of the GdpP gene impairs the processing of cysteine protease SpeB, decreases sensitivity to the antibiotic ampicillin, and attenuates virulence in a murine model of subcutaneous infection |
751991 |
| 3.1.4.59 | physiological function |
DhhP is essential for Borrelia burgdorferi growth both in vitro and in the mammalian host. The conditional DhhP mutant has a dramatic increase in intracellular c-di-AMP level in comparison to the isogenic wild-type strain. Elevated cellular c-di-AMP in Borrelia burgdorferi does not result in an increased resistance to beta-lactamase antibiotics. The DhhP mutant is defective in induction of the sigmaS factor, RpoS, and the RpoS-dependent outer membrane virulence factor OspC |
-, 750731 |
| 3.1.4.59 | physiological function |
disruption of gdpP increases intracellular c-di-AMP level and affects growth and increases biofilm formation. The GdpP mutant strain exhibits a significant decrease in hemolytic activity and adherence to and invasion of HEp-2 cells compared with the parental strain. Virulence genes cps2,sly, fpbs, mrp, ef and gdh display reduced expression in the gdpP mutant. In murine infection models, the GdpP mutant strain is attenuated, and impaired bacterial growth is observed in specific organs |
-, 751490 |
| 3.1.4.59 | physiological function |
GdpP mutant bacteria contain extra-membranous material at the division sites and in the form of vesicles in the cytoplasm. Expression of superoxide dismutase SodM is 5fold downregulated in the mutant, while no significant differences in the susceptibility to H2O2 or in peroxide levels are observed |
751056 |
| 3.1.4.59 | physiological function |
inactivation of GdpP confers tolerance to inhibitors of peptidoglycan biosynthesis |
-, 749591 |
