Structural basis for the sugar nucleotide and acyl-chain selectivity of Leptospira interrogans LpxA.

@article{Robins2009StructuralBF,
  title={Structural basis for the sugar nucleotide and acyl-chain selectivity of Leptospira interrogans LpxA.},
  author={Lori I Robins and Allison H. Williams and Christian R. H. Raetz},
  journal={Biochemistry},
  year={2009},
  volume={48 26},
  pages={6191-201}
}
The first step of lipid A biosynthesis is catalyzed by LpxA in Escherichia coli (EcLpxA), an acyltransferase selective for UDP-GlcNAc and R-3-hydroxymyristoyl-acyl carrier protein (ACP). Leptospira interrogans LpxA (LiLpxA) is extremely selective for R-3-hydroxylauroyl-ACP and an analogue of UDP-GlcNAc, designated UDP-GlcNAc3N, in which NH(2) replaces the GlcNAc 3-OH group. EcLpxA does not discriminate between UDP-GlcNAc and UDP-GlcNAc3N; however, E. coli does not make UDP-GlcNAc3N. With LiLpxA… CONTINUE READING

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