Deamination and Degradation of Amino Acids by Streptomycetes

Abstract

S. venezuelae, in a saline solution buffered at pH 6.9, deaminated glycine, alanine, serine, threonine, glutamic acid, histidine, arginine, proline and phenylalanine. Under these conditions the organism was not able to deaminate tyrosine, leucine, norleucine, cysteine or tryptophan. A similar pattern was shown by S. lavendulae for all the amino acids but phenylalanine. The deamination was influenced by the pH of the solution with an optimum near neutrality. The deamination of acidic amino acids was easily inhibited in slightly basic solutions and that of basic amino acids in acidic solutions. The pathway of dissimilation of histidine by S. venezuelae was through glutamic acid and of arginine through ornithine. The amino acids that were deaminated by S. venesuelae in pH 6.9 buffer were the same ones that were able to support growth when used as sole nitrogen sources in a synthetic medium. The amino acids that were not deaminated were not able to support growth.