Ribokinase (RK)

Ribokinase is an **enzyme** (EC 2.7.1.15) that catalyzes the phosphorylation of **D-ribose** to **D-ribose-5-phosphate** using **ATP** and magnesium as cofactors. This reaction is the **first step in ribose catabolism**, facilitating the entry of ribose into the **pentose phosphate pathway** and supporting the synthesis of nucleotides and histidine. Ribokinase belongs to the **phosphofructokinase B (PfkB) family**, also known as the RK family, which shares conserved sequence motifs and structural features. In humans, ribokinase (abbreviation: RK) is encoded by the RBKS gene. The enzyme's activity is essential for trapping ribose within the cell following uptake and for the metabolic recycling of ribose derived from nucleoside catabolism[1][2][3][4][5][6][8]. There are no well-established direct therapeutic drugs targeting ribokinase, nor are there clear safety issues or biomarker roles reported in current biomedical literature.

Other names

d-RibokinaseATP:d-ribose 5-phosphotransferasedeoxyribokinaseribokinase (phosphorylating)

Substrate phosphorylation (transfers a phosphate group from ATP to D-ribose, producing D-ribose-5-phosphate)[1][2][5][8] - Magnesium ion dependence for activity[2][8]