Function
Galactokinase (GALK) is the enzyme which catalyzes the second step in the Leloir pathway which converts β-D-galactose to glucose 1-phosphate. GALK catalyzes the conversion of α-D-galactose to galactose 1-phosphate[1].
Disease
Hereditary GALK deficiency is called galactosemia. The symptoms are early onset of cataract and impairment of galactose (gal) metabolism[2]..
Structural highlights
The 3D structure of human GALK shows the sugar binding active site wedged between the N- and C-termini of the enzyme. The galactose forms with GALK termini residues and in [3].
3D structures of galactokinase
Updated on 07-March-2023
6gr2 - hGALK + ADP + gal - human
7rcl, 7rcm - hGALK (mutant) + ADP + gal
1wuu - hGALK + Mg + AMPPNP + gal
6q3w, 6q8z - hGALK + pyrazine derivative + gal
6q91 - hGALK + benzamide derivative + gal
6q90, 6zgw - hGALK + pyridine derivative + gal
6q3x, 6zfh, 7s49 - hGALK + quinazoline derivative + gal
6zgv, 6zgx, 6zgz, 6zgy, 6zh0 - hGALK + pyrimidine derivative + gal
7s4c - hGALK (mutant) + pyrimidine derivative + gal
6qje - hGALK + imidazole derivative + gal
7ozx - hGALK + inhibitor + gal
2aj4 - GALK + Mg + AMPPNP + gal - yeast
1s4e - GALK + Mg + ADP + gal - Pyrococcus furiosus
2dej, 2dei - GALK + AMPPN derivative + gal - Pyrococcus horikoshii
1pie - GALK + gal - Lactococcus lactis
6tep - BiGALK + Mg + ADP - Bifidobacterium infantis
6ter, 6teq - BiGALK + gal derivative