Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Editor

Personal info

View

About

Terms

Javascript disabled

Please enable Javascript support in your browser to use this application.

Instructions on how to enable JavaScript on different browsers can be found here: http://www.google.com/support/bin/answer.py?answer=23852.

[edit this page]

Chemical Compound Review:

AC1NURHV (7S)-3-[(3S)-3-[[(2R)-2- acetamido-4-[(2R...

Synonyms: 16124-22-4, Udp-N-acetylmuramic acid pentapeptide, Udp-N-acetylmuramic acid pentapeptides

Hegde, S.S. et al., Weppner, W.A. et al., Jacobs, C. et al., Ishiguro, E.E. et al., David, V. et al., et al.

Branstrom, Midha, Goldman,

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of UDP-murnac-pentapeptide

Recombinant LvFemX exhibits Km values of 42 and 15 microm for UDP-MurNAc pentapeptide and Escherichia coli Ala-tRNAAla, respectively, and exhibited a kcat value of 660 min-1 [1].
The nascent peptidoglycan synthesizing system from Gaffkya homari utilized the dansylated nucleotide with a Vmax/Km of 0.05 and a Vmax of 0.10 times the values for UDP-MurNAc-pentapeptide [2].
We previously reported the identification of the femX gene from Lactobacillus viridescens and recombinant expression of active FemX (LvFemX) that catalyzes the transfer of l-Ala from Ala-tRNAAla to the epsilon-amino group of l-lysine of UDP-MurNAc pentapeptide (Hegde, S. S., and Shrader, T. E. (2001) J. Biol. Chem. 276, 6998-7003) [1].
Phospho-MurNAc-pentapeptide translocase in membrane fragments from Staphylococcus aureus Copenhagen catalyzed the transfer of phospho-MurNAc-Ala-DGlu-Lys(Nepsilon-Dns)-DAla-DAla to undecaprenyl phosphate with a Vmax/Km of 3.8 and a Vmax of 1.6 times the values for UDP-MurNAc-pentapeptide [2].
However, the expression of low-level resistance to vancomycin was observed only when both genes were cloned in E. faecalis JH2-2 together with the vanXYc gene from Enterococcus gallinarum BM4174 which encodes a d,d-peptidase which eliminates preferentially the high affinity vancomycin UDP-MurNAc-pentapeptide [D-Ala] precursors produced by the host [3].

High impact information on UDP-murnac-pentapeptide

Addition of the muropeptide, anhMurNAc-tripeptide, which accumulates in beta-lactamase-overproducing mutants, counteracts the negative effect of UDP-MurNAc-pentapeptide, restoring the innate ability of AmpR to induce ampC expression in vitro [4].
In the corresponding mutants, UDP-MurNAc-pentapeptide was extensively converted to UDP-MurNAc-tetrapeptide following hydrolysis of d-Ala(5), thereby providing the substrate of Ldt(fm) [5].
The UDP-MurNAc-pentapeptide, the major component of the cell wall precursor pool in vancomycin-sensitive cells was replaced by UDP-MurNAc-depsipeptide and UDP-MurNAc-tetrapeptide [6].
Nucleotide sequence of the murF gene encoding the UDP-MurNAc-pentapeptide synthetase of Escherichia coli [7].
Conditions were determined for an optimal accumulation of pentapeptide lipid II from UDP-MurNAc-pentapeptide in a cell-free system and for its isolation and purification [8].

Chemical compound and disease context of UDP-murnac-pentapeptide

The assay involves the preferential synthesis and accumulation of lipid II in a reaction mixture containing the cell wall membrane material isolated from Escherichia coli, exogenously supplied UDP-MurNAc-pentapeptide, and radiolabeled UDP-GlcNAc [9].

Biological context of UDP-murnac-pentapeptide

The murein precursor, UDP-MurNAc-pentapeptide, decreases AmpR-mediated transcriptional activation in vitro, but has no effect on an AmpR(G102E) mutant that mediates constitutive activation of ampC in vivo [4].
FemX consists of two structurally equivalent domains, separated by a cleft containing the binding site of the UDP-MurNAc-pentapeptide and a long channel that traverses one of the two domains [10].

Associations of UDP-murnac-pentapeptide with other chemical compounds

An isogenic relaxed (relA) strain deprived of lysine showed a 2.7-fold increase in UDP-MurNAc-pentapeptide [11].
D-Cycloserine treatment of rel+ and relA strains caused a depletion of intracellular UDP-MurNAc-pentapeptide [11].

Gene context of UDP-murnac-pentapeptide

The murein precursor, UDP-N-acetylmuramyl-L-Ala-gamma-D-Glu-meso-diaminopimelic acid-D-Ala-D-Ala (UDP-MurNAc-pentapeptide), has been shown to serve as a corepressor with AmpR to repress beta-lactamase expression in vitro [12].
Thus, UDP-MurNAc-pentapeptide synthesis is regulated by the relA gene [11].

Analytical, diagnostic and therapeutic context of UDP-murnac-pentapeptide

Structure-based site-directed mutagenesis of the UDP-MurNAc-pentapeptide-binding cavity of the FemX alanyl transferase from Weissella viridescens [13].

References

Kinetic and mechanistic characterization of recombinant Lactobacillus viridescens FemX (UDP-N-acetylmuramoyl pentapeptide-lysine N6-alanyltransferase). Hegde, S.S., Blanchard, J.S. J. Biol. Chem. (2003) [Pubmed]
Fluorescent substrate for nascent peptidoglycan synthesis. Uridine diphosphate-N-acetylmuramyl-(Nepsilon-5-dimethylaminonaphthalene-1-sulfonyl)pentapeptide. Weppner, W.A., Neuhaus, F.C. J. Biol. Chem. (1977) [Pubmed]
Mechanism of intrinsic resistance to vancomycin in Clostridium innocuum NCIB 10674. David, V., Bozdogan, B., Mainardi, J.L., Legrand, R., Gutmann, L., Leclercq, R. J. Bacteriol. (2004) [Pubmed]
Cytosolic intermediates for cell wall biosynthesis and degradation control inducible beta-lactam resistance in gram-negative bacteria. Jacobs, C., Frère, J.M., Normark, S. Cell (1997) [Pubmed]
Novel Mechanism of Resistance to Glycopeptide Antibiotics in Enterococcus faecium. Cremniter, J., Mainardi, J.L., Josseaume, N., Quincampoix, J.C., Dubost, L., Hugonnet, J.E., Marie, A., Gutmann, L., Rice, L.B., Arthur, M. J. Biol. Chem. (2006) [Pubmed]
High level oxacillin and vancomycin resistance and altered cell wall composition in Staphylococcus aureus carrying the staphylococcal mecA and the enterococcal vanA gene complex. Severin, A., Tabei, K., Tenover, F., Chung, M., Clarke, N., Tomasz, A. J. Biol. Chem. (2004) [Pubmed]
Nucleotide sequence of the murF gene encoding the UDP-MurNAc-pentapeptide synthetase of Escherichia coli. Parquet, C., Flouret, B., Mengin-Lecreulx, D., van Heijenoort, J. Nucleic Acids Res. (1989) [Pubmed]
Membrane intermediates in the peptidoglycan metabolism of Escherichia coli: possible roles of PBP 1b and PBP 3. van Heijenoort, Y., Gómez, M., Derrien, M., Ayala, J., van Heijenoort, J. J. Bacteriol. (1992) [Pubmed]
In situ assay for identifying inhibitors of bacterial transglycosylase. Branstrom, A.A., Midha, S., Goldman, R.C. FEMS Microbiol. Lett. (2000) [Pubmed]
Crystal structures of Weissella viridescens FemX and its complex with UDP-MurNAc-pentapeptide: insights into FemABX family substrates recognition. Biarrotte-Sorin, S., Maillard, A.P., Delettré, J., Sougakoff, W., Arthur, M., Mayer, C. Structure (Camb.) (2004) [Pubmed]
Involvement of the relA gene product and feedback inhibition in the regulation of DUP-N-acetylmuramyl-peptide synthesis in Escherichia coli. Ishiguro, E.E., Ramey, W.D. J. Bacteriol. (1978) [Pubmed]
Role of the murein precursor UDP-N-acetylmuramyl-L-Ala-gamma-D-Glu-meso-diaminopimelic acid-D-Ala-D-Ala in repression of beta-lactamase induction in cell division mutants. Uehara, T., Park, J.T. J. Bacteriol. (2002) [Pubmed]
Structure-based site-directed mutagenesis of the UDP-MurNAc-pentapeptide-binding cavity of the FemX alanyl transferase from Weissella viridescens. Maillard, A.P., Biarrotte-Sorin, S., Villet, R., Mesnage, S., Bouhss, A., Sougakoff, W., Mayer, C., Arthur, M. J. Bacteriol. (2005) [Pubmed]

Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenes Open Access Licence Privacy Policy Terms of Use apsburg

The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.