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The FASEB Journal, Vol 5, 2645-2651, Copyright © 1991 by The Federation of American Societies for Experimental Biology
REVIEWS |
DR Appling
Department of Chemistry and Biochemistry, University of Texas, Austin 78712.
Folate coenzymes supply the activated one-carbon units required in nucleic acid biosynthesis, mitochondrial and chloroplast protein biosynthesis, amino acid metabolism, methyl group biogenesis, and vitamin metabolism. Because of its central role in purine and thymidylate biosynthesis, folate-mediated one-carbon metabolism has been the target of many anticancer drug therapies. This review is a summary of recent results that suggest that folate-mediated one-carbon metabolism is highly compartmentalized in eukaryotic cells. Evidence exists for compartmentation of folate coenzymes and their one-carbon units between intracellular organelles, for substrate channeling of folate coenzymes, and for compartmentation by intracellular folate- binding proteins. Metabolic, regulatory, and therapeutic implications of these processes are discussed.
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J. R. Suh, E. W. Oppenheim, S. Girgis, and P. J. Stover Purification and Properties of a Folate-catabolizing Enzyme J. Biol. Chem., November 3, 2000; 275(45): 35646 - 35655. [Abstract] [Full Text] [PDF] |
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E. W. Oppenheim, C. Adelman, X. Liu, and P. J. Stover Heavy Chain Ferritin Enhances Serine Hydroxymethyltransferase Expression and de Novo Thymidine Biosynthesis J. Biol. Chem., June 1, 2001; 276(23): 19855 - 19861. [Abstract] [Full Text] [PDF] |
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