[HTML][HTML] Two enzymes catalyze vitamin K 2, 3-epoxide reductase activity in mouse: VKORC1 is highly expressed in exocrine tissues while VKORC1L1 is highly …
M Caspers, KJ Czogalla, K Liphardt, J Müller… - Thrombosis …, 2015 - Elsevier
Abstract VKORC1 and VKORC1L1 are enzymes that both catalyze the reduction of vitamin
K2, 3-epoxide via vitamin K quinone to vitamin K hydroquinone. VKORC1 is the key enzyme
of the classical vitamin K cycle by which vitamin K-dependent (VKD) proteins are γ-
carboxylated by the hepatic γ-glutamyl carboxylase (GGCX). In contrast, the VKORC1
paralog enzyme, VKORC1L1, is chiefly responsible for antioxidative function by reduction of
vitamin K to prevent damage by intracellular reactive oxygen species. To investigate tissue …
K2, 3-epoxide via vitamin K quinone to vitamin K hydroquinone. VKORC1 is the key enzyme
of the classical vitamin K cycle by which vitamin K-dependent (VKD) proteins are γ-
carboxylated by the hepatic γ-glutamyl carboxylase (GGCX). In contrast, the VKORC1
paralog enzyme, VKORC1L1, is chiefly responsible for antioxidative function by reduction of
vitamin K to prevent damage by intracellular reactive oxygen species. To investigate tissue …