On the stereochemistry of 2-hydroxyethylphosphonate dioxygenase

John T. Whitteck, Petra Malova, Spencer C. Peck, Robert M. Cicchillo, Friedrich Hammerschmidt, Wilfred A. Van Der Donk

Research output: Contribution to journalArticle

Abstract

Stereochemical investigations have shown that the conversion of 2-hydroxyethylphosphonate to hydroxymethylphosphonate by the enzyme HEPD involves removal of the pro-S hydrogen at C2 and, surprisingly, the loss of stereochemical information at C1. As a result, the mechanisms previously proposed for HEPD must be re-evaluated.

Original languageEnglish (US)
Pages (from-to)4236-4239
Number of pages4
JournalJournal of the American Chemical Society
Volume133
Issue number12
DOIs
StatePublished - Mar 30 2011

ASJC Scopus subject areas

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

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  • Cite this

    Whitteck, J. T., Malova, P., Peck, S. C., Cicchillo, R. M., Hammerschmidt, F., & Van Der Donk, W. A. (2011). On the stereochemistry of 2-hydroxyethylphosphonate dioxygenase. Journal of the American Chemical Society, 133(12), 4236-4239. https://doi.org/10.1021/ja1113326