Table 1.
The enzymatic properties of NADKs in different organisms.
| Species | Gene | Accession No. | Substrate | Phosphate donor | Multimerization | MW (subunits) | Km (mM) | Vmax | Subcellular localization | References |
|---|---|---|---|---|---|---|---|---|---|---|
| Mycobacterium tuberculosis H37Rv | ppnk | Z98268-16 | NAD | ATP or poly(P) | Tetramer | 35 kDa | ATP: 1.80 Poly(P)4: 1.60 | ATP: 1.40 A Poly (P)4: 1.60 A | – | Kawai et al., 2000 |
| Micrococcus flavus | ppnk | – | NAD | ATP or poly(P) | Dimer | 34 kDa | ATP: 0.13 Poly(P)4: 1.04 | ATP: 1.09 A Poly (P)4: 1.58 A | – | Kawai et al., 2000 |
| Escherichia coli MG1655 | yfjB | D90888-18 | NAD | ATP or other nucleoside triphosphates | Hexamer | 30 kDa | ATP:2.50 NAD: 2.00 | – | – | Kawai et al., 2001a |
| Archaeoglobus fulgidus | Afnk | GI NO. 2650718 | NAD | ATP | Tetramers or dimers | – | – | – | – | Liu et al., 2005 |
| Synechocystis sp. PCC 6803 | SLr0400 | NP_441852 | – | – | – | 34 kDa | – | – | – | Gao and Xu, 2012 |
| SLl1415 | NP_441342 | – | – | – | 34 kDa | – | – | – | Gao and Xu, 2012 | |
| Fusarium oxysporum | FoNADHK | FOXG_01647 | NADH | ATP | Homodimer | 72 kDa | ATP: 2.59 NADH: 0.13 | – | Panagiotou et al., 2008 | |
| Salmonella enterica | NadK | 16421206 | NAD | ATP and other nucleoside triphosphates | Dimers and tetramers | 36 kDa | ATP:2.7± 0.2 NAD: 2.1 ± 0.14 | – | – | Grose et al., 2006 |
| Saccharomyces cerevisiae | UTR1 | NM_001181707 | NAD | ATP, dATP, or CTP | Hexamer | 60 kDa | ATP: 0.60 NAD: 0.50 NADH: 3.9 | ATP: 1.2 B NAD: 1.2 B NADH: 3.5 B | Cytosol | Kawai et al., 2001b |
| POS5 | NM_001184002 | NADH | ATP | – | 46.3 kDa | – | – | Mitochondrial matrix | Outten and Culotta, 2003 | |
| YEF1 | NM_001178856 | NADH | ATP | Homooctamer | 60 kDa | ATP: 0.17 NAD: 1.9 NADH: 2.0 | NADH: 1.9 B NAD: 1.7 B | Cytosol | Shi et al., 2005 | |
| Strongylocentrotus purpuratus | SpNADK1 | ABY58956 | NAD | ATP | – | – | NAD: 0.54 ATP: 0.397 | 2.27 D | – | Love et al., 2015 |
| SpNADK2 | ABY58957 | NAD | ATP | – | – | NAD:0.212 ATP: 0.263 | 1.38 D | – | Love et al., 2015 | |
| Xenopus tropicalis | XtNADK | IMAGE clone no. 7003620 | NAD | ATP | – | – | NAD:0.756 ATP: 1.586 | 2.66 D | – | Love et al., 2015 |
| Pyrococcus horikoshii | PH1074 (PhNADK) | AB055976 | NAD | GTP, CTP, UTP, ITP, and ATP/poly (P) | Tetramer | 37 kDa | poly[27]: 0.30 ATP: 0.40 | – | – | Sakuraba et al., 2005 |
| Corynebacterium glutamicum | CljPpnK | 1019388 | NAD | ATP or poly(P) | Homotetramer | 35.8 kDa | NAD: 4.02 ATP: 1.95 | – | – | Shi et al., 2012 |
| ClPpnK | – | NAD | ATP or poly(P) | Homotetramer | 35.8 kDa | NAD: 1.40 ATP: 2.12 | – | – | Shi et al., 2012 | |
| Aspergillus nidulans | AnNADHK | AN8837 | NADH | ATP | – | 49 kDa | – | – | – | Panagiotou et al., 2009 |
| Sphingomonas sp. A1 | SNADK | AB127931 | NAD | ATP or other nucleoside triphosphates | Homodimer | 32 kDa | ATP: 1.92 NAD:0.43 | – | – | Ochiai et al., 2004 |
| Thermococcus kodakarensis | ANKtk | TK2124 | NADH | – | – | 40 kDa | – | – | – | Jia et al., 2010 |
| Bacillus subtilis | BsNADK | C663_1189 | NAD | poly(P), ATP, or other nucleoside triphosphates | Dimer | 30 kDa | NAD: 1.0 ± 0.09 | NAD: 2.6 ± 0.075 C ATP: 0.65 ± 0.08 C poly(P): 0.032 ± 0.09 C | – | Garavaglia et al., 2003 |
| Homo sapiens | C5orf33 (MNADK) | NM_001085411 | NAD | ATP or poly(P) | Homodimer | 45 kDa | ATP: 1.7 ± 0.3 NAD: 0.022 ± 0.001 | 0.091 ± 0.001 C | Mitochondria | Ohashi et al., 2012; Zhang, 2013 |
| HuNADK | NM_001198993 | NAD | ATP | Homotetramer | 49 kDa | ATP:3.3 NAD:0.54 | 6.7 D | Cytosol | Lerner et al., 2001; Pollak et al., 2007b | |
| Arabidopsis thaliana | AtNADK1 | AT3G21070 | NAD | UTP or ATP | – | 58.2 kDa | NAD: 0.52± 0.03 Mg2+·ATP: 0.73 ± 0.040 | Mg2+·ATP: 11.1 ± 0.61 C | Cytosol | Turner et al., 2004; Waller et al., 2010 |
| AtNADK2 | AT1G21640 | NAD | UTP or ATP | – | 109.2 kDa | NAD: 0.43 ± 0.017 Mg2+·ATP: 0.74 ± 0.012 | Mg2+·ATP: 14.3 ± 0.30 C | Chloroplasts | Turner et al., 2004; Chai et al., 2005; Waller et al., 2010 | |
| AtNADK3 | AT1G78590 | NADH | ATP,UTP, GTP and CTP | Dimer | 35 kDa | ATP:0.062 Mg2+:1.16 NAD:2.39 NADH:0.042 | ATP:39.5 ± 0.9 C Mg2+:40.3 ± 1.2 C NAD:23.2 ± 0.6 C NADH:41.2 ± 0.9 C | Peroxisomes | Turner et al., 2005; Waller et al., 2010 | |
| Triticum aestivum | TaNADK1 | KP165048 | – | – | – | – | – | – | Cytosol | Wang et al., 2016 |
| TaNADK2 | KP165049 | – | – | – | – | – | – | Cytosol | Wang et al., 2016 | |
| TaNADK3 | KP165050 | – | – | – | – | – | – | Chloroplasts | Wang et al., 2016 | |
| TaNADK4 | KP165051 | – | – | – | – | – | – | Peroxisomes | Wang et al., 2016 |
NADKs were identified and cloned from different organisms. The enzymatic properties of these NADKs were summarized here, including the preferable substrates, phosphate donors, multimerization, subunit molecular weight, Km and Vmax. To keep consistent with the original data, the units of Vmax were presented as follows: A, μmol/unit/h; B, mM min−1 U−1; C, U/mg; D, μm∙(min∙mg)−1.