Hydrocarbon rulers in UDP-N-acetylglucosamine acyltransferases

Timna J.O. Wyckoff, Shanhua Lin, Robert J. Cotter, Garry D. Dotson, Christian R.H. Raetz

Research output: Contribution to journalArticle

Abstract

UDP-GlcNAc acyltransferase (LpxA), the first enzyme of lipid A biosynthesis, catalyzes the transfer of an acyl chain activated on acyl carrier protein (ACP) to UDP-GlcNAc. LpxAs are very selective for the lengths of their acyl donor substrates. Escherichia coli LpxA prefers R-3- hydroxymyristoyl-ACP to R-3-hydroxydecanoyl-ACP by a factor of ~1000, whereas Pseudomonas aeruginosa LpxA prefers the opposite. E. coli G173M LpxA and the reciprocal P. aeruginosa M169G LpxA show reversed substrate selectivity in vitro and in vivo, demonstrating the existence of precise hydrocarbon rulers in LpxAs.

Original languageEnglish (US)
Pages (from-to)32569-32372
Number of pages198
JournalJournal of Biological Chemistry
Volume273
Issue number49
StatePublished - Dec 4 1998

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Wyckoff, T. J. O., Lin, S., Cotter, R. J., Dotson, G. D., & Raetz, C. R. H. (1998). Hydrocarbon rulers in UDP-N-acetylglucosamine acyltransferases. Journal of Biological Chemistry, 273(49), 32569-32372.