Table 3.
Rates of enzymatic hydrolysis for c-di-AMP and its nucleotide analogs by phosphodiesterase protein GdpPa
| Modification | Analog | Rate [mol min−1 (mol of enzyme)−1]b |
Fold Change |
|---|---|---|---|
| c-di-AMP | 4.1 ± 0.2 | - | |
| Base | c-AMP-GMP | 2.4 ± 0.3 | 1.7 |
| c-di-GMP | 0.8 ± 0.1 | 5.1 | |
| c-AMP-IMP | 1.3 ± 0.2 | 3.3 | |
| c-di-IMP | ≤ 0.001 c | ≥ 4100 | |
| c-AMP-Purine | 1.1 ± 0.1 | 3.8 | |
| c-di-Purine | 0.11 ± 0.01 | 36 | |
| c-di-N6m,N6mAMP | ≤ 0.001 | ≥ 4100 | |
| c-AMP-DAP | 1.8 ± 0.3 | 2.2 | |
| c-di-DAP | ≤ 0.001 | ≥ 4100 | |
| c-di-2AP | 1.7 ± 0.2 | 2.4 | |
| c-di-c7AMP | 2.3 ± 0.2 | 1.8 | |
| Ribose | c-dA-AMP | 3.5 ± 0.3 | 1.2 |
| c-di-dAMP | ≤ 0.001 | ≥ 4100 | |
| c-2’F-A-AMP | 0.17 ± 0.01 | 24 | |
| c-di-2’F-AMP | ≤ 0.001 | ≥ 4100 | |
| c-dA-2’F-A | ≤ 0.001 | ≥ 4100 | |
| c-2’OMe-A-AMP | 0.14 ± 0.01 | 30 | |
| c-di-2’OMe-AMP | ≤ 0.001 | ≥ 4100 | |
| Phosphate | c-(RpRp)-di-Aps | ≤ 0.001 | ≥ 4100 |
| c-(RpSp)-di-Aps | ≤ 0.001 | ≥ 4100 |
a
All data are the average of at least three independent trials.
b
Rates measured under multiple-turnover conditions with 100 µM substrate and 1 µM enzyme.
c
No degradation under the conditions tested after incubation with GdpP for 24 h. Rates were estimated using a detection limit of 2%.