Characterization of peptidoglycan stem lengths by solid-state 13C and 15N NMR.
Lyophilized whole cells of Aerococcus viridans (Gaffkya homari) grown on a synthetic medium containing D-[2-13C, 15N]Ala, or containing both L-[1-13C]Lys and D-[15N]Ala, have been examined by double cross-polarization magic-angle spinning 13C and 15N nuclear magnetic resonance. Results from the double-labeled alanine experiment confirm the absence of metabolic scrambling of alanine by A. viridans. Results from the combined single-label experiment can be used to count directly the number of adjacent L-Lys and D-Ala units in peptide chains of cell-wall peptidoglycan. This count leads to the conclusion that there are no terminal D-Ala or D-Ala-D-Ala units in uncross-linked chains of the peptidoglycan of A. viridans.
D000409:Alanine / Q000096:biosynthesis; D000411:Alanine Racemase / Q000378:metabolism; D000595:Amino Acid Sequence; D002247:Carbon Isotopes; D002473:Cell Wall / Q000032:analysis; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D009587:Nitrogen Isotopes; D010446:Peptide Fragments / Q000032:analysis; D010457:Peptidoglycan / Q000032:analysis* / Q000378:metabolism; D013289:Streptococcaceae / Q000032:analysis
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D010446:Peptide Fragments; D010457:Peptidoglycan; D000411:Alanine Racemase; D000409:Alanine