We revealed nitrogen isotopic hetero- and homogeneity for D-α-alanine and L-α-alanine in terms of microbial processes in domain Bacteria and chemical processes in organic symmetric synthesis. D-alanine is a physiologically essential enantiomer for microbial growth and metabolic maintenance. The nitrogen isotopic difference of amino acids in peptidoglycan in bacteria, representative gram-positive phylum Firmicutes and Actinobacteria (Enterococcus faecalis, Staphylococcus aureus, Staphylococcus staphylolyticus, Lactobacillus acidophilus, Bacillus subtilis, Micrococcus luteus and Streptomyces sp.), tended to be 15N-depleted in D-alanine, suggesting that isotopically heterogeneous components are mainly controlled by enzymatic pathways prior to formation of the bacterial cell wall. In contrast, the δ15N of racemic alanine in the chemical pathway during the typical nucleophilic substitution reaction (SN1 type) between 2-bromopropionic acid and ammonia showed infinitely homogeneous components for each enantiomer. The novel method of enantiomer-specific isotopic analysis (ESIA) is useful for distinguishing the origin of biogenic and abiogenic processes and is applicable to enantiomer studies.
View full abstract