the enzyme exhibits dual redox cofactor specificity, utilizing either NADP+ or NAD+. NAD+-dependent dehydrogenase activity of MTHFD2 with the substrate 5,10-methylenetetrahydropteroylglutamate is 8.5fold higher than its NADP+-dependent activity. While the NAD+-dependent activity of MTHFD2 slightly decreases, its maximal NADP+-dependent activity considerably increases with 5,10-methylenetetrahydropteroylpentaglutamate compared to 5,10-methylenetetrahydropteroylglutamate
the enzyme exhibits dual redox cofactor specificity, utilizing either NADP+ or NAD+. NAD+-dependent dehydrogenase activity of MTHFD2L with the substrate 5,10-methylenetetrahydropteroylglutamat is 3.4fold higher than its NADP+-dependent activity under saturating substrate conditions. While the NAD+-dependent activity of MTHFD2 slightly decreases, its maximal NADP+-dependent activity considerably increases with 5,10-methylenetetrahydropteroylpentaglutamate compared to 5,10-methylenetetrahydropteroylglutamate
the enzyme exhibits dual redox cofactor specificity, utilizing either NADP+ or NAD+. NAD+-dependent dehydrogenase activity of MTHFD2 with the substrate 5,10-methylenetetrahydropteroylglutamate is 8.5fold higher than its NADP+-dependent activity. While the NAD+-dependent activity of MTHFD2 slightly decreases, its maximal NADP+-dependent activity considerably increases with 5,10-methylenetetrahydropteroylpentaglutamate compared to 5,10-methylenetetrahydropteroylglutamate
the enzyme exhibits dual redox cofactor specificity, utilizing either NADP+ or NAD+. NAD+-dependent dehydrogenase activity of MTHFD2L with the substrate 5,10-methylenetetrahydropteroylglutamate is 3.4fold higher than its NADP+-dependent activity under saturating substrate conditions. While the NAD+-dependent activity of MTHFD2 slightly decreases, its maximal NADP+-dependent activity considerably increases with 5,10-methylenetetrahydropteroylpentaglutamate compared to 5,10-methylenetetrahydropteroylglutamate
the recombinant Bombyx mori MTHFD (bmMTHFD) recognizes 5,10-methylenetetrahydrofolate and 5,10-methenyltetrahydrofolate as substrates in the presence of NADP+ as well as NAD+