DAK (gene) explained
Triokinase/FMN cyclase is an enzyme that in humans is encoded by the DAK gene.[1]
Function
This gene is a member of the family of dihydroxyacetone kinases, which have a protein structure distinct from other kinases. The product of this gene phosphorylates dihydroxyacetone, and also catalyzes the formation of riboflavin 4',5'-phosphate (aka cyclic FMN) from FAD. Several alternatively spliced transcript variants have been identified, but the full-length nature of only one has been determined.
Further reading
- Diao F, Li S, Tian Y, Zhang M, Xu LG, Zhang Y, Wang RP, Chen D, Zhai Z, Zhong B, Tien P, Shu HB . Negative regulation of MDA5- but not RIG-I-mediated innate antiviral signaling by the dihydroxyacetone kinase . Proceedings of the National Academy of Sciences of the United States of America . 104 . 28 . 11706–11 . July 2007 . 17600090 . 1913852 . 10.1073/pnas.0700544104 . 2007PNAS..10411706D . free .
- Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S . Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes . Genome Research . 16 . 1 . 55–65 . January 2006 . 16344560 . 1356129 . 10.1101/gr.4039406 .
- Cabezas A, Costas MJ, Pinto RM, Couto A, Cameselle JC . Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as ATP-dependent dihydroxyacetone kinases . Biochemical and Biophysical Research Communications . 338 . 4 . 1682–9 . December 2005 . 16289032 . 10.1016/j.bbrc.2005.10.142 .
- Cheek S, Ginalski K, Zhang H, Grishin NV . A comprehensive update of the sequence and structure classification of kinases . BMC Structural Biology . 5 . 6 . 2006 . 15771780 . 1079889 . 10.1186/1472-6807-5-6 . free .
- Cabezas A, Pinto RM, Fraiz F, Canales J, González-Santiago S, Cameselle JC . Purification, characterization, and substrate and inhibitor structure-activity studies of rat liver FAD-AMP lyase (cyclizing): preference for FAD and specificity for splitting ribonucleoside diphosphate-X into ribonucleotide and a five-atom cyclic phosphodiester of X, either a monocyclic compound or a cis-bicyclic phosphodiester-pyranose fusion . Biochemistry . 40 . 45 . 13710–22 . November 2001 . 11695920 . 10.1021/bi0157159 .
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S . Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library . Gene . 200 . 1–2 . 149–56 . October 1997 . 9373149 . 10.1016/S0378-1119(97)00411-3 .
- Maruyama K, Sugano S . Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides . Gene . 138 . 1–2 . 171–4 . January 1994 . 8125298 . 10.1016/0378-1119(94)90802-8 .
Notes and References
- Web site: Entrez Gene: DAK dihydroxyacetone kinase 2 homolog (S. cerevisiae).