New insights into the catalytic mechanism of vitamin K epoxide reductase (VKORC1) - The catalytic properties of the major mutations of rVKORC1 explain the biological cost associated to mutations

▸ L120Q and Y139C/F/S mutations of rVKORC1 dramatically affect VKOR activity. ▸ Y139C/F/S mutations lead to the production of 3-hydroxyvitamin K. ▸ Tyr-139 residue is involved in the dehydration of vitamin K epoxide. ▸ VKORC1 mutations in position 139 lead to increase in vitamin K requirements. ▸ Rat carriers for Y139C/F/S are models to study consequences of vitamin K deficiency.