EC Number   |
General Information |
Reference |
|---|
  3.1.4.60 | physiological function |
a Pde2 mutant strain displays a growth defect in the early growth phase. The mutant displays an increase in cellular c-di-AMP and 5'-O-phosphonoadenylyl-(3'->5')-adenosine levels and increased oxacillin resistance. A strain producing a high level of c-di-AMP has increased and a stain producing low levels has decreased acid resistance |
-, 751077 |
| 3.1.4.60 | 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 |
| 3.1.4.60 | 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 |
| 3.1.4.60 | 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 |
