@article{mbs:/content/journal/micro/10.1099/00221287-17-3-620, author = "Shah, P. C. and King, H. K. and Hollis, B. and Fairhurst, A. S.", title = "Optical Activity of Amino Acids Formed by Reductive Amination in Bacillus subtilis", journal= "Microbiology", year = "1957", volume = "17", number = "3", pages = "620-624", doi = "https://doi.org/10.1099/00221287-17-3-620", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-17-3-620", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "SUMMARY: Suspensions of Bacillus subtilis form dl-alanine when incubated with pyruvate and ammonia. When leucine and valine are formed from the analogous keto acids, only the l-isomer is found. Since B. subtilis has a racemase active for alanine but not for valine or leucine, it is possible that the l-alanine may be the primary product and which is then racemized. Suspensions of Bacillus subtilis and of some other organisms can synthesize certain amino acids from ammonia and the corresponding keto-acids (Fair-hurst, King & Sewell, 1956). When alanine is formed from pyruvate by B. subtilis, the racemic dl-mixture is produced. The present paper gives evidence in support of this finding (mentioned by Fairhurst et al. 1956, but not in detail) and discusses the mechanism of the reaction.", }