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alr  -  alanine racemase

Staphylococcus aureus RF122

 
 
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High impact information on alr

  • Solid-state NMR has been used to examine the cell walls of intact whole cells of Staphyloccus aureus grown on media containing D-[1-(13)C]alanine, [(15)N]glycine, and the alanine racemase inhibitor, alaphosphin [1].
  • Full-echo REDOR spectra of cell-wall complexes from cells labeled by d-[1-(13)C]alanine (in the presence of an alanine racemase inhibitor) reveal three different carbonyl carbon chemical-shift environments, arising from the d-Ala-d-Ala binding site and the d-Ala-Gly-1 cross-link site [2].
  • A set of dipeptides containing the amino acid residues beta-chloroalanine and propargylglycine, which are mechanism-based inactivators of purified microbial enzymes (alanine racemase and cystathionine gamma-synthase, respectively), have been synthesized, and their antibacterial properties in vitro have been evaluated [3].

References

  1. Conformational and quantitative characterization of oritavancin-peptidoglycan complexes in whole cells of Staphylococcus aureus by in vivo 13C and 15N labeling. Cegelski, L., Steuber, D., Mehta, A.K., Kulp, D.W., Axelsen, P.H., Schaefer, J. J. Mol. Biol. (2006) [Pubmed]
  2. Structures of Staphylococcus aureus cell-wall complexes with vancomycin, eremomycin, and chloroeremomycin derivatives by 13C{19F} and 15N{19F} rotational-echo double resonance. Kim, S.J., Cegelski, L., Preobrazhenskaya, M., Schaefer, J. Biochemistry (2006) [Pubmed]
  3. Chloralanyl and propargylglycyl dipeptides. Suicide substrate containing antibacterials. Cheung, K.S., Wasserman, S.A., Dudek, E., Lerner, S.A., Johnston, M. J. Med. Chem. (1983) [Pubmed]
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