Hydrocarbon rulers in UDP-N-acetylglucosamine acyltransferases

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

doi:10.1074/jbc.273.49.32369

Hydrocarbon rulers in UDP-N-acetylglucosamine acyltransferases

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

School of Medicine

Research output: Contribution to journal › Article › peer-review

72 Scopus citations

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 language	English (US)
Pages (from-to)	32569-32372
Number of pages	198
Journal	Journal of Biological Chemistry
Volume	273
Issue number	49
DOIs	https://doi.org/10.1074/jbc.273.49.32369
State	Published - Dec 4 1998

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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title = "Hydrocarbon rulers in UDP-N-acetylglucosamine acyltransferases",

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.",

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AU - Wyckoff, Timna J.O.

AU - Lin, Shanhua

AU - Cotter, Robert J.

AU - Dotson, Garry D.

AU - Raetz, Christian R.H.

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AB - 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.

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Hydrocarbon rulers in UDP-N-acetylglucosamine acyltransferases

Abstract

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