Lysine catabolism in Streptomyces ambofaciens producer of macrolide antibiotic, spiramycin

Spiramycin production was highly stimulated when lysine was used as the sole nitrogen source. This amino acid was catabolized by the alpha -transaminase pathway characterized by dosage of cadaverine aminotransferase (CAT) enzyme. The Km sub(cadaverine) was of 57 mM. CAT was highly induced by lysine...

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Bibliographic Details
Published in:Current microbiology 1992-12, Vol.25 (6), p.313-318
Main Authors: UNTRAU, S, LEBRIHI, A, GERMAIN, P, LEFEBVRE, G
Format: Article
Language:English
Subjects:
Biological and medical sciences
Biology of microorganisms of confirmed or potential industrial interest
Biotechnology
Fundamental and applied biological sciences. Psychology
Mission oriented research
Physiology and metabolism
Streptomyces ambofaciens
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Summary:Spiramycin production was highly stimulated when lysine was used as the sole nitrogen source. This amino acid was catabolized by the alpha -transaminase pathway characterized by dosage of cadaverine aminotransferase (CAT) enzyme. The Km sub(cadaverine) was of 57 mM. CAT was highly induced by lysine (634% in comparison with ammonium). Addition of 40 mM of ammonium in a culture begun with 20 mM of lysine as the sole initial nitrogen source repressed CAT biosynthesis by 24% but did not affect spiramycin production seriously. Addition of 20 mM of lysine in a culture started with 40 mM ammonium induced CAT biosynthesis of 425%, but did not allow spiramycin production. In these two cases, spiramycin production seems to be conditioned by the nitrogen source initially present in the culture medium. CAT activity was inhibited by ammonium ions (33% at 20 mM), whereas lysine had no effects.
ISSN:0343-8651
1432-0991
DOI:10.1007/BF01577227