• [1]
    Rogers, H.J., Perkins, H.R. and Ward, J.B. (1980) Biosynthesis of peptidoglycan. In: Microbial Cell Walls and Membranes (Rogers, H.J., Ed.), pp. 239–297. Chapman and Hall, London.
  • [2]
    van Heijenoort, J. (1994) Biosynthesis of the bacterial peptidoglycan unit. In: Bacterial Cell Wall (Ghuysen, J.-M. and Hakenbeck, R., Eds.), pp. 39–54. Elsevier, Amsterdam.
  • [3]
    Christensen, B.G., Leanza, W.J., Beatties, T.R., Patchett, A.A., Arison, B.H., Ormond, R.E. F.A. Kuehl Jr. Albers-Schonberg, G., Jardetzky, O. (1969) Phosphonomycin: structure and synthesis. Science 166, 123125.
  • [4]
    Bouhss, A., Mengin-Lecreulx, D., Blanot, D., van Heijenoort, J., Parquet, C. (1997) Invariant amino acids in the Mur peptide synthetases of bacterial peptidoglycan synthesis and their modification by site-directed mutagenesis in the UDP-MurNAc: l-alanine ligase from Escherichia coli. Biochemistry 36, 1155611563.
  • [5]
    Eveland, S.S., Pompliano, D.L., Anderson, M.S. (1997) Conditionally lethal Escherichia coli murein mutants contain point defects that map to regions conserved among murein and folyl poly-γ-glutamate ligases: Identification of a ligase superfamily. Biochemistry 36, 62236229.
  • [6]
    El Zoeiby, A., Sanschagrin, F., Lamoureux, J., Darveau, A., Levesque, R.C. (2000) Cloning, over-expression and purification of Pseudomonas aeruginosa murC encoding uridine diphosphate N-acetylmuramate:l-alanine ligase. FEMS Microbiol. Lett. 183, 281288.
  • [7]
    Falk, P.J., Ervin, K.M., Volk, K.S., Ho, H.T. (1996) Biochemical evidence for the formation of a covalent acyl-phosphate linkage between UDP-N-acetylmuramate and ATP in the Escherichia coli UDP-N-acetylmuramate: l-alanine ligase-catalyzed reaction. Biochemistry 35, 14171422.
  • [8]
    Liger, D., Masson, A., Blanot, D., van Heijenoort, J., Parquet, C. (1996) Study of the overproduced uridine-diphosphate-N-acetylmuramate: l-alanine ligase from Escherichia coli. Microb. Drug Resist. 2, 2527.
  • [9]
    Tanner, M., Vaganay, S., van Heijenoort, J., Blanot, D. (1996) Phosphinate inhibitors of the d-glutamic acid-adding enzyme of peptidoglycan biosynthesis. J. Org. Chem. 61, 17561760.
  • [10]
    Vaganay, S., Tanner, M., van Heijenoort, J., Blanot, D. (1996) Study of the reaction mechanism of the d-glutamic acid-adding enzyme from Escherichia coli. Microb. Drug Resist. 2, 5154.
  • [11]
    Bertrand, J.A., Auger, G., Martin, L., Fanchon, E., Blanot, D., Le Beller, D., van Heijenoort, J., Dideberg, O. (1999) Determination of the MurD mechanism through crystallographic analysis of enzyme complexes. J. Mol. Biol. 289, 579590.
  • [12]
    Anderson, M.S., Eveland, S.S., Onishi, H.R., Pompliano, D.L. (1996) Kinetic mechanism of the Escherichia coli UDPMurNAc-Tripeptide d-alanyl-d-alanine-adding enzyme: Use of a glutathione S-Transferase fusion. Biochemistry 35, 1626416269.
  • [13]
    Pratviel-Sosa, F., Acher, F., Trigalo, F., Blanot, D., Azerad, R., van Heijenoort, J. (1994) Effect of various analogues of d-glutamic acid on the d-glutamate-adding enzyme from Escherichia coli. FEMS Microbiol. Lett. 115, 223228.
  • [14]
    Auger, G., van Heijenoort, J., Blanot, D. (1995) Synthesis of N-Acetylmuramic acid derivatives as potential inhibitors of the d-glutamic acid-adding enzyme. J. Prakt. Chem. 337, 351357.
  • [15]
    Gegnas, L.D., Waddell, S.T., Chabin, R.M., Reddy, S., Wong, K.K. (1998) Inhibitors of the bacterial cell wall biosynthesis enzyme MurD. Bioorg. Med. Chem. Lett. 8, 16431648.
  • [16]
    Zeng, B., Wong, K.K., Pompliano, D.L., Reddy, S., Tanner, M.E. (1998) A phosphinate inhibitor of the meso-diaminopimelic acid-adding enzyme (MurE) of peptidoglycan biosynthesis. J. Org. Chem. 63, 1008110086.
  • [17]
    Auger, G., van Heijenoort, J., Vederas, J.C., Blanot, D. (1996) Effect of analogues of diaminopimelic acid on the meso-diaminopimelate-adding enzyme from Escherichia coli. FEBS Lett. 391, 171174.
  • [18]
    Bugg, T.D., Walsh, C.T. (1992) Intracellular steps of bacterial cell wall peptidoglycan biosynthesis: Enzymology, antibiotics, and antibiotic resistance. Nat. Prod. Rep. 9, 199215.
  • [19]
    Auger, G., Martin, L., Bertrand, J., Ferrari, P., Fanchon, E., Vaganay, S., Pétillot, Y., van Heijenoort, J., Blanot, D., Dideberg, O. (1998) Large-scale preparation, purification, and crystallization of UDP-N-Acetylmuramoyl-l-alanine:d-glutamate ligase from Escherichia coli. Protein Expr. Purif. 13, 2329.
  • [20]
    Sambrook, J., Fritch, E.F. and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, 2nd edn. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
  • [21]
    Stover, C.K., Pham, X.Q., Erwin, A.L., Mizoguchi, S.D., Warrener, P., Hickey, M.J., Brinkman, F.S., Hufnagle, W.O., Kowalik, D.J., Lagrou, M., Garber, R.L., Goltry, L., Tolentino, E., Westbrock-Wadman, S., Yuan, Y., Brody, L.L., Coulter, S.N., Folger, K.R., Kas, A., Larbig, K., Lim, R., Smith, K., Spencer, D., Wong, G.K., Wu, Z., Paulsen, I.T., Reizer, J., Saier, M.H., Hancock, R.E.W., Lory, S., Olson, M.V. (2000) Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen. Nature 406, 959964.
  • [22]
    El-Sherbeini, M., Geissler, W.M., Pittman, J., Yuan, X., Wong, K.K., Pompliano, D.L. (1998) Cloning and expression of Staphylococcus aureus and Streptococcus pyogenes murD genes encoding uridine diphosphate N-acetylmuramoyl-l-alanine:d-glutamate ligases. Gene 210, 117125.
  • [23]
    Wong, K.K., Kuo, D.W., Chabin, R.M., Fournier, C., Gegnas, L.D., Waddell, S.T., Marsilio, F., Leiting, B., Pompliano, D.L. (1998) Engineering a cell-free murein biosynthetic pathway: Combinatorial enzymology in drug discovery. J. Am. Chem. Soc. 120, 1352713528.
  • [24]
    Reddy, S.G., Waddell, S.T., Kuo, D.W., Wong, K.K., Pompliano, D.L. (1999) Preparative enzymatic synthesis and characterization of the cytoplasmic intermediates of murein biosynthesis. J. Am. Chem. Soc. 121, 11751178.
  • [25]
    Wulfing, C., Lombardero, J., Pluckthun, A. (1994) An Echerichia coli protein consisting of a domain homologous to FK506-binding proteins (FKBP) and a new metal binding motif. J. Biol. Chem. 269, 28952901.