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Gene Review

murC  -  UDP-N-acetylmuramate:L-alanine ligase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK0092, JW0089
 
 
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Disease relevance of murC

 

High impact information on murC

  • Viability of the E. coliDeltaddlADeltaddlB mutant in the absence of exogenous D-Ala-D-Ala dipeptide became dependent on the expression of the chlamydial murC-ddl thus demonstrating functional ligase activity [3].
  • The N-terminal sequence of the purified protein correlated with the nucleotide sequence of the murC gene [1].
  • Plasmid pAM1005, in which the promoter and ribosome-binding site region of murC were removed and in which the gene was directly under the control of promoter trc, led to a 2000-fold amplification of the L-alanine-adding activity after induction by isopropyl-thio-beta-D-galactopyranoside [1].
  • These results suggest that P. gingivalis contains a homologue of the E. coli peptidoglycan synthesis gene murC and indicate the possibility of a cluster of genes responsible for cell division and cell growth, as in the E. coli mra region [2].

References

  1. Over-production, purification and properties of the uridine-diphosphate-N-acetylmuramate:L-alanine ligase from Escherichia coli. Liger, D., Masson, A., Blanot, D., van Heijenoort, J., Parquet, C. Eur. J. Biochem. (1995) [Pubmed]
  2. A murC gene in Porphyromonas gingivalis 381. Ansai, T., Yamashita, Y., Awano, S., Shibata, Y., Wachi, M., Nagai, K., Takehara, T. Microbiology (Reading, Engl.) (1995) [Pubmed]
  3. Characterization of Chlamydia MurC-Ddl, a fusion protein exhibiting D-alanyl-D-alanine ligase activity involved in peptidoglycan synthesis and D-cycloserine sensitivity. McCoy, A.J., Maurelli, A.T. Mol. Microbiol. (2005) [Pubmed]
 
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