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EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.155,10-methylenetetrahydrofolate + NAD+ the bifunctional enzyme also shows N5,N10-methenyltetrahydrofolate cyclohydrolase activity EC 3.5.4.9. with NADP+ (1 mM), the enzyme shows less than 0.1% of the activity obtained with NAD+ (1 mM). The purified enzyme shows no activity with methylene-tetrahydromethanopterin or with 5,10-methylenetetrahydrosarcinapterin either in the presence of NAD+ or NADP+ or in the presence of F420 Methanosarcina barkeri DSM 804 5,10-methenyltetrahydrofolate + NADH + H+ - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.155,10-methylenetetrahydrofolate + NADP+ - Homo sapiens 5,10-methenyltetrahydrofolate + NADPH + H+ - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.155,10-methylenetetrahydrofolate + NADP+ - Homo sapiens 5,10-methenyltetrahydrofolate + NADPH + H+ ? -
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.155,10-methylenetetrahydrofolate + NADP+ about 15% of the rate with NAD+ Homo sapiens 5,10-methenyltetrahydrofolate + NADPH + H+ - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.155,10-methylenetetrahydropteroylglutamate + NAD+ NAD+-dependent dehydrogenase activity of MTHFD2 is 8.5fold higher than its NADP+-dependent activity Homo sapiens 5,10-methenyltetrahydropteroylglutamate + NADH + H+ - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.155,10-methylenetetrahydropteroylglutamate + NAD+ NAD+-dependent dehydrogenase activity of MTHFD2L is 3.4fold higher than its NADP+-dependent activity under saturating substrate conditions Homo sapiens 5,10-methenyltetrahydropteroylglutamate + NADH + H+ - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.155,10-methylenetetrahydropteroylglutamate + NADP+ NAD+-dependent dehydrogenase activity of MTHFD2 is 8.5fold higher than its NADP+-dependent activity Homo sapiens 5,10-methenyltetrahydropteroylglutamate + NADPH + H+ - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.155,10-methylenetetrahydropteroylglutamate + NADP+ NAD+-dependent dehydrogenase activity of MTHFD2L is 3.4fold higher than its NADP+-dependent activity under saturating substrate conditions Homo sapiens 5,10-methenyltetrahydropteroylglutamate + NADPH + H+ - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.155,10-methylenetetrahydropteroylpentaglutamate + 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 Homo sapiens 5,10-methenyltetrahydropteroylpentaglutamate + NADH + H+ - ?
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.155,10-methylenetetrahydropteroylpentaglutamate + 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 Homo sapiens 5,10-methenyltetrahydropteroylpentaglutamate + NADH + H+ - ?
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