EC Number   |
General Information |
Reference |
|---|
    1.5.1.5 | evolution |
the redox cofactor requirements of the isozymes from Mus musculus and Rattus norvegicus are quite similar, both exhibit lower Km values for NAD+ than for NADP+, their NAD+-dependent activities require phosphate and Mg2+, and their NADP+-dependent activities are inhibited by phosphate |
-, 742856 |
| 1.5.1.5 | metabolism |
cytosolic protein with role in cytosolic purine synthesis, ubiquitously expressed in all mammalian cells |
701402 |
| 1.5.1.5 | metabolism |
mitochondrial protein with role in cytosolic purine synthesis (main switch for format production in mitochondria) during embryonic development and in cells undergoing rapid growth, not expressed in differentiated cells |
701402 |
| 1.5.1.5 | metabolism |
product of the bifuncional enzyme, 10-formyl tetrahydrofolate, is not essential for de novo purine synthesis in Leishmania and other parasitic protozoans contrary to other organisms, it is utilized for methionyl-tRNA formulation in mitochondria, the bifunctional enzyme product is essential for Leishmania major and may even reveal novel pathways |
700281 |
| 1.5.1.5 | metabolism |
the dehydrogenase activity of FolD catalyses NADP+-dependent oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate. The 5,10-methenyltetrahydrofolate cyclohydrolase activity in Clostridium perfringens is provided by another protein, the 5,10-methylenetetrahydrofolate cyclohydrolase FchA, whose cyclohydrolase activity is 10 times more efficient than that of Eco FolD. Both Clostridium perfringens FolD and FchA are required to substitute for the single bifunctional FolD in Escherichia coli. The simultaneous presence of Clostridium perfringens FolD and FchA is also necessary to rescue an Escherichia coli K16 folD deletion strain for its formate and glycine auxotrophies, and to alleviate its susceptibility to trimethoprim (an antifolate drug) or UV light |
743250 |
| 1.5.1.5 | metabolism |
the enzyme is involved in folate pathway. It is involved in mitochondrial NADPH production. It is proposed that isoenzyme MTHFD2 may be expressed to boost flux through the mitochondrial folate pathway during early periods of embryogenesis when isoenzyme MTHFD2L alone is not sufficient to support high rates of cell proliferation |
756334 |
| 1.5.1.5 | metabolism |
the enzyme is involved in the folate recycling pathway |
-, 757625 |
| 1.5.1.5 | metabolism |
the enzyme plays a central role in folate homeostasis and serve as targets for antibacterials |
743250 |
| 1.5.1.5 | metabolism |
the mitochondrial methylenetetrahydrofolate dehydrogenase/cyclohydrolase(MTHFD2)-controlled cluster redirects metabolism to glycine synthesis to replenish purine nucleotides. Since endothelial cells secrete purines in response to oxPAPC, the MTHFD2-controlled response maintains endothelial ATP. Accordingly, MTHFD2-dependent glycine synthesis is a prerequisite for angiogenesis. It is proposed that endothelial cells undergo MTHFD2-mediated reprogramming toward serine-glycine and mitochondrial one-carbon metabolism to compensate for the loss of ATP in response to oxidized phospholipids during atherosclerosis |
757773 |
| 1.5.1.5 | more |
MTFHD2 isozyme has been named NAD+-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase but in fact exhibits dehydrogenase activity with NADP+, albeit with a much higher Km and lower Vmax |
-, 742856 |
