One-carbon metabolism is usually represented as having three canonical functions: purine synthesis, thymidylate synthesis and methylation reactions. There is however a fourth major function: the metabolism of some amino acids (serine, glycine, tryptophan and histidine), as well as choline. These substrates can provide cells with more one-carbon groups than they need for these three canonical functions. Therefore, there must be mechanisms for the disposal of these one-carbon groups (when in excess) which maintain the complement of these groups required for the canonical functions. The key enzyme for these mechanisms is 10-formyl-THF (tetrahydrofolate) dehydrogenase (both mitochondrial and cytoplasmic isoforms) which oxidizes the formyl group to CO2 with the attendant reduction of NADP+ to NADPH and release of THF. In addition to oxidizing the excess of these compounds, this process can reduce substantial quantities of NADP+ to NADPH.
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December 2015
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Review Article|
November 13 2015
Division of labour: how does folate metabolism partition between one-carbon metabolism and amino acid oxidation?
Margaret E. Brosnan
;
Margaret E. Brosnan
*Department of Biochemistry, Memorial University of Newfoundland, St. John's, NL, Canada A1B 3X9
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Luke MacMillan
;
Luke MacMillan
*Department of Biochemistry, Memorial University of Newfoundland, St. John's, NL, Canada A1B 3X9
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Jennifer R. Stevens
;
Jennifer R. Stevens
*Department of Biochemistry, Memorial University of Newfoundland, St. John's, NL, Canada A1B 3X9
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John T. Brosnan
John T. Brosnan
1
*Department of Biochemistry, Memorial University of Newfoundland, St. John's, NL, Canada A1B 3X9
1To whom correspondence should be addressed (email jbrosnan@mun.ca).
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Biochem J (2015) 472 (2): 135–146.
Article history
Received:
July 27 2015
Revision Received:
July 27 2015
Accepted:
September 09 2015
Citation
Margaret E. Brosnan, Luke MacMillan, Jennifer R. Stevens, John T. Brosnan; Division of labour: how does folate metabolism partition between one-carbon metabolism and amino acid oxidation?. Biochem J 1 December 2015; 472 (2): 135–146. doi: https://doi.org/10.1042/BJ20150837
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