Deamination and Degradation of Amino Acids by Streptomycetes

Abstract

Streptomyces venezuelae and S. lavendulae deaminated glycine, alanine, serine, threonine, glutamic acid, histidine, arginine, and proline, but not tyrosine, leucine, norleucine, cysteine, or tryptophan in a salt solution buffered at pH 6.9. In addition, S. venezuelae deaminated phenylalanine. The optimum pH was near neutrality. Histidine was degraded through a pathway involving glutamic acid, while arginine was transformed by way of ornithine. When amino acids were used as the sole source of nitrogen, the ability to support growth was correlated with the susceptibility to deamination by S. venezuelae. Phenylalanine was an exception, since it could be deaminated, though to a lesser extent than other amino acids, but did not support growth.