Sterochemical Analysis of the Methyl Transfer Catalyzed by Cobalamin-Dependent Methionine Synthase from Escherichia coli B

T. M. Zydowsky, L. F. Courtney, V. Frasca, R. G. Matthews, L. D. Yuen, H. Shimizu, K. Kobayashi, S. J. Benkovic, H. G. Floss

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Abstract

The last step in the biosynthesis of methionine involves transfer of the methyl group of TV5-methyltetrahydrofolate (5-CH3-H4-folate) or its polyglutamate analogue to the sulfur of homocysteine.

Original languageEnglish (US)
Pages (from-to)3152-3153
Number of pages2
JournalJournal of the American Chemical Society
Volume108
Issue number11
DOIs
StatePublished - Jan 1 1986

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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    Zydowsky, T. M., Courtney, L. F., Frasca, V., Matthews, R. G., Yuen, L. D., Shimizu, H., Kobayashi, K., Benkovic, S. J., & Floss, H. G. (1986). Sterochemical Analysis of the Methyl Transfer Catalyzed by Cobalamin-Dependent Methionine Synthase from Escherichia coli B. Journal of the American Chemical Society, 108(11), 3152-3153. https://doi.org/10.1021/ja00271a081