Triokinase/FMN cyclase is an
enzyme that in humans is encoded by the DAKgene.[5]
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.[5]
Cabezas A, Costas MJ, Pinto RM, Couto A, Cameselle JC (December 2005). "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.
doi:
10.1016/j.bbrc.2005.10.142.
PMID16289032.
Cabezas A, Pinto RM, Fraiz F, Canales J, González-Santiago S, Cameselle JC (November 2001). "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.
doi:
10.1021/bi0157159.
PMID11695920.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56.
doi:
10.1016/S0378-1119(97)00411-3.
PMID9373149.
Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4.
doi:
10.1016/0378-1119(94)90802-8.
PMID8125298.
Triokinase/FMN cyclase is an
enzyme that in humans is encoded by the DAKgene.[5]
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.[5]
Cabezas A, Costas MJ, Pinto RM, Couto A, Cameselle JC (December 2005). "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.
doi:
10.1016/j.bbrc.2005.10.142.
PMID16289032.
Cabezas A, Pinto RM, Fraiz F, Canales J, González-Santiago S, Cameselle JC (November 2001). "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.
doi:
10.1021/bi0157159.
PMID11695920.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56.
doi:
10.1016/S0378-1119(97)00411-3.
PMID9373149.
Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4.
doi:
10.1016/0378-1119(94)90802-8.
PMID8125298.