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Lysine 190 is the catalytic base in MenF, the menaquinone-specific isochorismate synthase from Escherichia coli: Implications for an enzyme family

  • Subramaniapillai Kolappan
  • , Jacque Zwahlen
  • , Rong Zhou
  • , James J. Truglio
  • , Peter J. Tonge
  • , Caroline Kisker
  • Stony Brook University
  • Simon Fraser University
  • University of Würzburg

Research output: Contribution to journalArticlepeer-review

51 Scopus citations

Abstract

Menaquinone biosynthesis is initiated by the conversion of chorismate to isochorismate, a reaction that is catalyzed by the menaquinone-specific isochorismate synthase, MenF. The catalytic mechanism of MenF has been probed using a combination of structural and biochemical studies, including the 2.5 Å structure of the enzyme, and Lys190 has been identified as the base that activates water for nucleophilic attack at the chorismate C2 carbon. MenF is a member of a larger family of Mg2+ dependent chorismate binding enzymes catalyzing distinct chorismate transformations. The studies reported here extend the mechanism recently proposed for this enzyme family by He et al.: He, Z., Stigers Lavoie, K. D., Bartlett, P. A., and Toney, M. D. (2004) J. Am. Chem. Soc. 126, 2378-85.

Original languageEnglish
Pages (from-to)946-953
Number of pages8
JournalBiochemistry
Volume46
Issue number4
DOIs
StatePublished - Jan 30 2007

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