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Mitochondrial one-carbon metabolism is adapted to the specific needs of yeast, plants and mammals.
The differences in the folate pathways of mitochondria depending on species, tissues and developmental stages, profoundly alter the nature of their metabolic contribution.
Structures of three inhibitor complexes provide insight into the reaction mechanism of the human methylenetetrahydrofolate dehydrogenase/cyclohydrolase.
The crystal structures of three ternary DC301/NADP/inhibitor complexes are determined and a reaction mechanism for both activities, the dehydrogenase and the cyclohydrolase is proposed.
The MTHFD1 p.Arg653Gln variant alters enzyme function and increases risk for congenital heart defects
The results indicate that the Arg653Gln polymorphism decreases enzyme stability and increases risk for CHD, and further evaluation of this polymorphism in folate related disorders and its potential interaction with folate status is warranted.
Methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase: a multifunctional protein from porcine liver.
The molecular basis of glutamate formiminotransferase deficiency
These mutations are the first identified in glutamate formiminotransferase deficiency and demonstrate that mutations in FTCD represent the molecular basis for the mild phenotype of this disease.
Mitochondrial methylenetetrahydrofolate dehydrogenase, methenyltetrahydrofolate cyclohydrolase, and formyltetrahydrofolate synthetases.
Binding and interconversion of tetrahydrofolates at a single site in the bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase.
The results of the binding and kinetic studies indicate that the bifunctional nature of the methyleneH4folate dehydrogenase/methenylH4 Folate cyclohdrolase domain is designed to optimize the overall reverse reactions in vivo.
Magnesium and Phosphate Ions Enable NAD Binding to Methylenetetrahydrofolate Dehydrogenase-Methenyltetrahydrofolate Cyclohydrolase*
- K. Christensen, I. Mirza, A. Berghuis, R. Mackenzie
- Biology, ChemistryJournal of Biological Chemistry
- 7 October 2005
A homology model of human NMDMC was constructed based on the structures of three homologous proteins and supports the hypothesis that the absolutely required Pi can bind in close proximity to the 2′-hydroxyl of NAD through interactions with Arg166 and Arg198.
Introduction to Differentiable Manifolds
Primary structure of a human trifunctional enzyme. Isolation of a cDNA encoding methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase.