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• W2150449715 abstract "The subcellular distributions of folate and folate-synthesizing enzymes were investigated in pea leaves. It was observed that the mitochondrial folate pool (˜400 μM) represented ˜50% of the total pool. Furthermore, all the enzymes involved in tetrahydrofolate polyglutamate synthesis were present in the mitochondria. In marked contrast, we failed to detect any significant activity of these enzymes in chloroplasts, cytosol, and nuclei. The presence of the tetrahydrofolate synthesis pathway in mitochondria is apparently a general feature in plants since potato tuber mitochondria also contained a high folate concentration (˜200 μM) and all the enzymes required for tetrahydrofolate polyglutamate synthesis.The specific activities of tetrahydrofolate-synthesizing enzymes were rather low (1.5-15 nmol h-1 mg-1 matrix protein), except for dihydrofolate reductase (180-500 nmol h-1 mg-1 matrix protein). Dihydrofolate reductase was purified to homogeneity. The enzyme had a native molecular mass of ˜140 kDa and was constituted of two identical 62-kDa subunits. Interestingly, this mitochondrial protein appeared to be a bifunctional enzyme, also supporting thymidylate synthesis. The cell distribution of thymidylate synthase was also investigated. No significant activity was observed in cell fractions other than mitochondria, indicating that plant cell mitochondria are also a major site for thymidylate synthesis. The subcellular distributions of folate and folate-synthesizing enzymes were investigated in pea leaves. It was observed that the mitochondrial folate pool (˜400 μM) represented ˜50% of the total pool. Furthermore, all the enzymes involved in tetrahydrofolate polyglutamate synthesis were present in the mitochondria. In marked contrast, we failed to detect any significant activity of these enzymes in chloroplasts, cytosol, and nuclei. The presence of the tetrahydrofolate synthesis pathway in mitochondria is apparently a general feature in plants since potato tuber mitochondria also contained a high folate concentration (˜200 μM) and all the enzymes required for tetrahydrofolate polyglutamate synthesis. The specific activities of tetrahydrofolate-synthesizing enzymes were rather low (1.5-15 nmol h-1 mg-1 matrix protein), except for dihydrofolate reductase (180-500 nmol h-1 mg-1 matrix protein). Dihydrofolate reductase was purified to homogeneity. The enzyme had a native molecular mass of ˜140 kDa and was constituted of two identical 62-kDa subunits. Interestingly, this mitochondrial protein appeared to be a bifunctional enzyme, also supporting thymidylate synthesis. The cell distribution of thymidylate synthase was also investigated. No significant activity was observed in cell fractions other than mitochondria, indicating that plant cell mitochondria are also a major site for thymidylate synthesis." @default.
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• W2150449715 date "1996-04-01" @default.
• W2150449715 modified "2023-10-15" @default.
• W2150449715 title "Mitochondria Are a Major Site for Folate and Thymidylate Synthesis in Plants" @default.
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• W2150449715 doi "https://doi.org/10.1074/jbc.271.16.9466" @default.
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