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Gene Review:

murE - UDP-N-acetylmuramoyl-L-alanyl-D...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK0086, JW0083

Boniface, A. et al., Tao, J.S. et al., Liao, X. et al., Mengin-Lecreulx, D. et al., Michaud, C. et al., et al.

Mengin-Lecreulx, Falla, Blanot, van Heijenoort, Adams, Chopra,

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Disease relevance of murE

Nucleotide sequence of the murE gene of Escherichia coli [1].
DNA sequence of the murE-murD region of Bacillus subtilis 168 [2].

High impact information on murE

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 [3].
The pbpB gene was located upstream of a gene homologous to the E. coli murE gene, which encodes uridine diphosphate-N-acetyl muramic acid-tripeptide synthetase [4].
The murE gene from S. aureus encoding the UDP-N-acetylmuramoyl-L-alanyl-D-glutamate: L-lysine ligase was identified and cloned into plasmid vectors [5].
The N-terminal sequence of the protein was determined and correlated with the nucleotide sequence of the murE gene [6].

Chemical compound and disease context of murE

The nucleotide sequence of the murE gene encoding the diaminopimelic acid adding enzyme of Escherichia coli is reported [1].

References

Nucleotide sequence of the murE gene of Escherichia coli. Tao, J.S., Ishiguro, E.E. Can. J. Microbiol. (1989) [Pubmed]
DNA sequence of the murE-murD region of Bacillus subtilis 168. Daniel, R.A., Errington, J. J. Gen. Microbiol. (1993) [Pubmed]
The MurE synthetase from Thermotoga maritima is endowed with an unusual D-lysine adding activity. Boniface, A., Bouhss, A., Mengin-Lecreulx, D., Blanot, D. J. Biol. Chem. (2006) [Pubmed]
Cloning and characterization of the Pseudomonas aeruginosa pbpB gene encoding penicillin-binding protein 3. Liao, X., Hancock, R.E. Antimicrob. Agents Chemother. (1995) [Pubmed]
Expression of the Staphylococcus aureus UDP-N-acetylmuramoyl- L-alanyl-D-glutamate:L-lysine ligase in Escherichia coli and effects on peptidoglycan biosynthesis and cell growth. Mengin-Lecreulx, D., Falla, T., Blanot, D., van Heijenoort, J., Adams, D.J., Chopra, I. J. Bacteriol. (1999) [Pubmed]
Over-production, purification and properties of the uridine-diphosphate-N-acetylmuramoyl-L-alanyl-D-glutamate: meso-2,6-diaminopimelate ligase from Escherichia coli. Michaud, C., Mengin-Lecreulx, D., van Heijenoort, J., Blanot, D. Eur. J. Biochem. (1990) [Pubmed]

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