The MurE synthetase from thermotoga maritima is endowed with an unusual D-lysine-adding activity

doi:10.1074/jbc.M506311200

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Papers In Press, published online ahead of print April 4, 2006
J. Biol. Chem, 10.1074/jbc.M506311200
Submitted on June 9, 2005
Revised on April 3, 2006
Accepted on April 4, 2006

The MurE synthetase from thermotoga maritima is endowed with an unusual D-lysine-adding activity

Audrey Boniface, Ahmed Bouhss, Dominique Mengin-Lecreulx, and Didier Blanot

Enveloppes Bactériennes et Antibiotiques, IBBMC, UMR 8619 CNRS, Université de Paris-Sud, Orsay 91405

Corresponding Author: didier.blanot{at}ebp.u-psud.fr

The peptidoglycan of Thermotoga maritima, an extremely thermophilic eubacterium, was shown to contain no diaminopimelic acid and approximate amounts of both enantiomers of lysine (Huber, R., et al., (1986) Arch. Microbiol. 144, 324-333). In order to assess the possible involvement of the MurE activity in the incorporation of D-lysine, the murE gene from this organism was cloned in Escherichia coli and the corresponding protein was purified as the C-terminal His₆-tagged form. In vitro assays showed that D-lysine and meso-diaminopimelic acid were added to UDP-N-acetylmuramoyl-dipeptide with 25% and 10% efficiencies, respectively, relative to L-lysine. The purified enzyme was used to synthesize the L- and D-lysine-containing UDP-N-acetylmuramoyl-tripeptides ; chemical analysis revealed an unusual structure for the D-lysine-containing nucleotide, namely acylation of the $epsilon$ -amino function of D-lysine by the D-glutamyl residue. In vitro assays with MurF and MraY enzymes from T. maritima showed that this novel nucleotide was not a substrate for MurF, but that it could be directly processed into tripeptide lipid I by MraY, thereby substantiating the role of MurE in the incorporation of D-lysine into peptidoglycan.

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