Flavokinase
| Flavokinase | ||
|---|---|---|
| Properties of human protein | ||
| Mass / length primary structure | 155 amino acids | |
| Secondary to quaternary structure | Monomer | |
| Cofactor | Zinc or magnesium | |
| Identifier | ||
| Gene name | RFK | |
| External IDs | ||
| Enzyme classification | ||
| EC, category | 2.7.1.26 , kinase | |
| Response type | Phosphorylation | |
| Substrate | Riboflavin + ATP | |
| Products | FMN + ADP | |
| Occurrence | ||
| Homology family | Riboflavin kinase | |
| Parent taxon | Eukaryotes | |
Flavokinase (also riboflavin kinase ) is the enzyme in the vitamin B 2 - metabolism which riboflavin in the flavin converts (FMN) and therefore essential for the synthesis of the coenzyme flavin adenine dinucleotide (FAD) are. Flavokinase is produced by all living things, but the archaea enzyme is very different from that of bacteria and eukaryotes . In humans, flavokinase is localized in the cytoplasm of the cells of the brain , placenta and urinary bladder .
Catalyzed reaction
+ XTP →
+ XDP
The catalyzed reaction is a phosphorylation in which a phosphoric acid residue is transferred from a nucleotide triphosphate to the 5'-hydroxy group of the riboflavin.
In bacterial and eukaryotic riboflavin kinases ( ATP-riboflavin-5'-phosphotransferases , EC 2.7.1.26 ) the catalyzed reaction is ATP- specific:
- Riboflavin + ATP - (flavokinase, T 3 -stimulated) FMN + ADP
In archaeal riboflavin kinases ( CTP-riboflavin-5′-phosphotransferases , EC 2.7.1.161 ) it is CTP- specific:
- Riboflavin + CTP - (Flavokinase) FMN + CDP
Web links
Individual evidence
- ↑ M. Ammelburg, MD Hartmann, S. Djuranovic, V. Alva, KK Koretke, J. Martin, G. Sauer, V. Truffault, K. Zeth, AN Lupas, M. Coles: A CTP-Dependent Archaeal Riboflavin Kinase Forms a Bridge in the Evolution of Cradle-Loop Barrels. In: Structure. (12), 2007, pp. 1577-1590. PMID 18073108 .