Table 4.
Some important characteristics of metabolite probes.
| Name | Analyte | Range Max | Kd | Reference |
|---|---|---|---|---|
| MaLionB | ATP | 1.9 | Kd = 0.46 mM | [193] |
| QUEEN-7μ | ATP | ~6 | Kd = 7.2 μM (25 °C) | [191] |
| QUEEN-2m | ATP | ~5 | Kd = 4.5 mM (25 °C) | [191] |
| iATPSnFR1.0 | ATP | ~3.4 | EC50 ~ 120 μM | [192] |
| iATPSnFR1.1 | ATP | ~2.9 | EC50 ~ 50 μM | [192] |
| mRuby-iATPSnFR1.0 | ATP | Same as for iATPSnFR1.0 | Same as for iATPSnFR1.0 | [192] |
| MaLionG | ATP | 4.9 | Kd = 1.1 mM | [193] |
| Perceval | [ATP]:[ADP] | ~2 | KR~0.5 | [197] |
| PercevalHR | [ATP]:[ADP] | ~8 | KR~3.5 | [198] |
| MaLionR | ATP | 4.5 | Kd = 0.34 mM | [193] |
| ATeam1.03 | ATP | ~2.3 | Kd = 3.3 mM (37 °C) | [194] |
| ATeam3.10 | ATP | ~2 | Kd = 7.4 μM (37 °C) | [194] |
| GO-ATeam1 | ATP | ~2 | Kd = 7.1 mM (37 °C) | [195] |
| GO-ATeam2 | ATP | ~3 | Kd = 2.3 mM (37 °C) | [195] |
| BTeam (BRET) | ATP | ~3 | K0.5 = 1.7 mM (25 °C) | [196] |
| Laconic | Lactate | ~1.2 (in vitro) ~1.4 (in living cells) |
NM | [200] |
Kd—dissociation constant; range max—maximal dynamic range of the probe (N-fold); EC50—half maximal effective concentration; KR—ratio of analytes at which the sensor response is half-maximal; K0.5—the concentration at which half of the protein molecules are bound to the analyte; NM—not measured. Background colors correspond to the color of FPs used as reporter domains. Colorless lines correspond to Förster resonance energy transfer (FRET) or bioluminescence resonance energy transfer (BRET) probes.