Stereochemistry of Methylene Transfer Involving 5,10-Methylenetetrahydrofolate

Charles M. Tatum, Patricia A. Benkovic, Stephen J. Benkovic, Rowell Potts, Erwin Schleicher, Eleinz G. Floss

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Abstract

The stereochemistry of the transfer catalyzed by rabbit liver serine transhydroxymethylase (EC 2.1.2.1) of the prochiral hydroxymethyl group from serine to tetrahydrofolate to form 5,10-methylenetetrahydrofolate was studied. Initial kinetic studies on labeled 5,10-methylenetetrahydrofolate showed that nonenzymatic racemization of the prochiral methylene center was buffer dependent and was slow under the conditions employed. Specifically tritiated (3R)- and (3S)-serines were employed to study the transfer reaction. Reactions were carried out under various conditions and the stereochemistry of the methylene carbon of the 5,10-methylenetetrahydrofolate produced was determined. The enzyme was shown to be partially stereospecific for this transfer reaction, proceeding with a loss of about 50% of the stereochemical purity of the transferred carbon center. Possible mechanistic interpretations of this finding are discussed.

Original languageEnglish (US)
Pages (from-to)1093-1102
Number of pages10
JournalBiochemistry
Volume16
Issue number6
DOIs
Publication statusPublished - Mar 1 1977

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All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Tatum, C. M., Benkovic, P. A., Benkovic, S. J., Potts, R., Schleicher, E., & Floss, E. G. (1977). Stereochemistry of Methylene Transfer Involving 5,10-Methylenetetrahydrofolate. Biochemistry, 16(6), 1093-1102. https://doi.org/10.1021/bi00625a010