Deamination and Degradation of Amino Acids by Streptomycetes
- 1 March 1956
- journal article
- research article
- Published by Taylor & Francis in Mycologia
- Vol. 48 (2), 253-263
- https://doi.org/10.2307/3755473
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.This publication has 3 references indexed in Scilit:
- THE METABOLISM OF SPECIES OF STREPTOMYCES VIIJournal of Bacteriology, 1953
- THE METABOLISM OF SPECIES OF STREPTOMYCES VJournal of Bacteriology, 1952
- Observations on Streptomyces griseusJournal of Bacteriology, 1948