Table 1.
Kinetic properties of wild-type and modified luciferases in the present study.
| Luciferase | Amino acid length | Mutation sites | λmax (in vitro) | λmax (in cell) | Km (luciferin μM) | Km (ATP μM) | DDBJ Accession No | BRC catalog No |
|---|---|---|---|---|---|---|---|---|
| Pmat (wt) | 548 | wild type | 560 | – | 14.2 | 104 | LC495923 | |
| Pmat | 548 | E355R, V367A, I424L, K446Q | 560 | 568 | 62.2 | 98.1 | LC495924 | RDB14359 |
| Pmat (Dro) | 548 | E355R, V367A, I424L, K446Q | – | – | – | – | LC495925 | |
| Dkum (wt) | 547 | wild type | 557 | – | 60.1 | 127.3 | LC495926 | |
| Dkum | 547 | N2D, I424L | 558 | 560 | 19.4 | 26.8 | LC495927 | RDB14360 |
| MALuci2 (wt) | 544 | wild type | 557 | – | 4.25 | 188 | LC495928 | |
| MALuci2 | 544 | N2D | 556 | 557 | 1.2 | 88.9 | LC495929 | RDB14363* |
| Sfla (wt) | 555 | wild type | 559 | – | 16.6 | 21.5 | LC495930 | |
| Sfla | 555 | P2A, S293F, N387S, C400Y, I432V, V451I, A486D, S517C, K520R | 609 | 612 | 6.6 | 9.0 | LC495931 | RDB14362 |
| Psag (wt) | 545 | wild type | 583 | – | 4.9 | 194 | LC495932 | |
| Psag | 545 | I148V, S283L, V401 M, F464I, G503R | 605 | 609 | 221.7 | 281.7 | LC495933 | RDB14361 |
| Luc2 | 550 | 562 | 605 | 27.1 | 72.6 |
The position numbers of mutation sites are indicated as amino acid sequence position for the length of each luciferase. Maximum wavelength (λmax) in vitro (at pH 8.0) and in the cell was measured at 25 °C and 37 °C, respectively. These materials were deposited at RIKEN BioResource Research Center (Tsukuba, Japan), and the deposition numbers are also listed. However, it is to be noted that amino acid position at 2 of MALuci2 (RDB14363*) was not altered to N2D (N2N). –: not determined.