Abstract
Summary: A stabilized L-form from Streptococcus pyogenes possessed alanine racemase and D-alanyl-D-alanine synthetase, and formed D-alanyl-D-alanine from L-alanine. Comparative rates of synthesis of this dipeptide by coccal and L-form cell-free preparations suggested that this pathway remained unaffected in the L-form, even after prolonged inhibition of wall formation. The terminal nucleotide precursor for wall biosynthesis (UDP-muramic acid-peptide) accumulated in this L-form organism; it probably contained D-alanyl-D-alanine. Lack of D-alanine in glycerol teichoic acid from the L-form only was not caused by a loss of alanine racemase activity.
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