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A β-cyano-l-alanine (β-CNAla)-assimilating bacterium was isolated from soil samples, and was identified as belonging to the genus Pseudomonas. Under the growing conditions used, this strain consumed β-CNAla without accumulating any detectable metabolite. However, both intact cells and cell-free extracts of the strain formed aspartic acid from β-CNAla. By affinity chromatography using AHA (N-ω-aminohexyl-l-aspartic acid)-Sepharose 6B gel a β-CNAla-degrading enzyme was purified from the cell-free extract, and it was found that the enzyme was specific for the degradation of β-CNAla.The strain also utilized the aliphatic nitriles, aceto-, propio-, n-butyro- and succinonitrile, as the sole nitrogen source. Cell-free extracts from cells grown on various aliphatic nitriles possessed both nitrilase and amidase activity but not β-CNAla-degrading activity, and in this strain β-CNAla was found to be degraded via a pathway different from that for common nitriles.

Microbial utilization of .BETA.-cyano-L-alanine by Pseudomonas sp. 13.