Table 1. Physical and kinetic properties of prokaryotic and eukaryotic NADKs.
Activities using either NAD+ or NADH as substrate are presented. The values are given as μmol of product (NADP+ or NADPH respectively) formed per min per mg of protein. −, not detectable; poly(P) designates polyphosphate as the substrate instead of ATP.
| Organism | Subunit mass and number | Activity NAD+/NADH | Km NAD+ | Km NADH | Km ATP | Reference |
|---|---|---|---|---|---|---|
| Homo sapiens | ||||||
| hNADK | 49 kDa tetramer | 6.7/− | 0.54 | − | 3.3 | [127] |
| S. cerevisiae | ||||||
| ScNADK-1b (Utr1p) | 60 kDa hexamer | 16.2-51.5/∼2 | 0.5 | 3.9 | 0.6 | [102,126,129,152] |
| ScNADK-2b (Yef1p) | 56 kDa octamer | 3.3–9.5/∼1 | 1.9 | 2 | 0.17 | [102,126,129] |
| ScNADK-3b (Pos5p) | 46 kDa | 0.2/0.4, but see [151] | a | a | a | [151,155] |
| A. thaliana | ||||||
| AtNADK-1 | 58 kDa | <0.2/<0.1 | 0.52 | a | 0.73 | [122,125] |
| AtNADK-2 | 109 kDa | 0.2/− | 0.43 | − | 0.74 | [122] |
| AtNADK-3 | 35 kDa dimer | 41.2/23.2 | 2.39 | 0.042 | NAD+: 0.19 | [160] |
| NADH: 0.06 | ||||||
| E. coli | ||||||
| YfjB | 30 kDa hexamer | 13/− | 2 | − | 2.5 | [126,128] |
| M. tuberculosis | ||||||
| Ppnk | 33 kDa tetramer | 0.5–4.3/0.7 | 0.9–3.3 | a | 1.8–2.5 | [113,117,126] |
| (poly(P): 1.7/0.2) | (poly(P): 1.2–2.9) | (poly(P): 1.3–1.6) | ||||
| Micrococcus flavus | ||||||
| Mfnk | 34 kDa dimer | 18.3/8.7 | 0.53–0.83 | 0.45 | NAD+: 0.23 | [113,126] |
| (poly(P): 7.4/3.0) | (poly(P): 0.26–0.58) | (poly(P): 0.35) | NADH: 0.32 | |||
| (poly(P): NAD+: 0.33 | ||||||
| NADH: 0.58) |
aNot reported.
bProposed name.