NAD- and NADP-dependent mitochondrially targeted methylenetetrahydrofolate dehydrogenase-cyclohydrolases can rescue mthfd2 null fibroblasts

Archives of Biochemistry and Biophysics

Volumn 442, Issue 1, 2005, Pages 133-139

  Patel, Harshila ^a   Di Pietro, Erminia ^a   Mejia, Narciso ^a   MacKenzie, Robert E ^a  

^a MCGILL UNIVERSITY   (Canada)

Author keywords

Bifunctional; Folate; Formate; Glycine auxotrophy; Methylenetetrahydrofolate dehydrogenase; Mitochondria; mthfd2 null fibroblasts; NAD; Purine synthesis; Serine; Trifunctional

Indexed keywords

COMPLEMENTARY DNA; GLYCINE; HYDROLASE; METHYLENETETRAHYDROFOLATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

ANIMAL CELL; ARTICLE; AUXOTROPHY; CELL FRACTIONATION; ENZYME ACTIVITY; ENZYME INACTIVATION; FIBROBLAST; ISOTOPE LABELING; MITOCHONDRION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN TARGETING; WILD TYPE;

AMINOHYDROLASES; ANIMALS; BLOTTING, WESTERN; CARBON RADIOISOTOPES; CELL LINE; DNA, COMPLEMENTARY; EMBRYONIC DEVELOPMENT; FIBROBLASTS; GLYCINE; KINETICS; LEUCOVORIN; METHYLENETETRAHYDROFOLATE DEHYDROGENASE (NADP); MICE; MITOCHONDRIA; MUTATION; NAD; NADP;

EID: 24944526674     PISSN: 00039861     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.abb.2005.07.022     Document Type: Article

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