“DAK (gene)”的意思、由来-开放百科全书

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.^[1]

1. ^¹{{cite web | title = Entrez Gene: DAK dihydroxyacetone kinase 2 homolog (S. cerevisiae)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=26007| accessdate = }}

Further reading

{{cite journal | vauthors = Diao F, Li S, Tian Y, Zhang M, Xu LG, Zhang Y, Wang RP, Chen D, Zhai Z, Zhong B, Tien P, Shu HB | title = Negative regulation of MDA5- but not RIG-I-mediated innate antiviral signaling by the dihydroxyacetone kinase | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 104 | issue = 28 | pages = 11706–11 | date = July 2007 | pmid = 17600090 | pmc = 1913852 | doi = 10.1073/pnas.0700544104 }}

{{cite journal | vauthors = 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 | title = Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes | journal = Genome Research | volume = 16 | issue = 1 | pages = 55–65 | date = January 2006 | pmid = 16344560 | pmc = 1356129 | doi = 10.1101/gr.4039406 }}

{{cite journal | vauthors = Cabezas A, Costas MJ, Pinto RM, Couto A, Cameselle JC | title = Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as ATP-dependent dihydroxyacetone kinases | journal = Biochemical and Biophysical Research Communications | volume = 338 | issue = 4 | pages = 1682–9 | date = December 2005 | pmid = 16289032 | doi = 10.1016/j.bbrc.2005.10.142 }}

{{cite journal | vauthors = Cheek S, Ginalski K, Zhang H, Grishin NV | title = A comprehensive update of the sequence and structure classification of kinases | journal = BMC Structural Biology | volume = 5 | pages = 6 | year = 2006 | pmid = 15771780 | pmc = 1079889 | doi = 10.1186/1472-6807-5-6 }}

{{cite journal | vauthors = Cabezas A, Pinto RM, Fraiz F, Canales J, González-Santiago S, Cameselle JC | title = 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 | journal = Biochemistry | volume = 40 | issue = 45 | pages = 13710–22 | date = November 2001 | pmid = 11695920 | doi = 10.1021/bi0157159 }}

{{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1-2 | pages = 149–56 | date = October 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}

{{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1-2 | pages = 171–4 | date = January 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}

Function

References

Further reading