1. L-lysine epsilon-aminotransferase involved in cephamycin C synthesis in Streptomyces lactamdurans.
- Author
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Kern BA, Hendlin D, and Inamine E
- Subjects
- 2-Aminoadipic Acid biosynthesis, Fermentation, Pipecolic Acids analysis, Stereoisomerism, Streptomyces enzymology, Cephalosporins biosynthesis, Cephamycins biosynthesis, Lysine metabolism, Streptomyces metabolism, Transaminases metabolism
- Abstract
In Streptomyces lactamdurans, the precursor of the alpha-aminoadipoyl side-chain of cephamycin C is L-lysine. In this regard, streptomycetes differ strikingly from the fungi, which produce alpha-aminoadipic acid during the synthesis, rather than the breakdown, of L-lysine. Studies using a cell-free system showed that an aminoadipic acid. The product of this reaction was trapped and subsequently purified by ion-exchange chromatography. Thin-layer chromatography, spectrophotometry, and amino acid oxidase digestion studies identified the reaction product as L-1-piperideine-6-carboxylate, implying enzymatic removal of the epsilon amino group of L-lysine. This enzymatic activity (E.C. 2.6.1.36; L-lysine: 2-oxoglutarate 6-aminotransferase) is highly unusual and was previously conclusively demonstrated only in the genus Flavobacterium. In S. lactamdurans, the specific activity of this enzyme reaches a peak early in the fermentation (approximately 20 h) and decreases as the antibiotic begins to appear.
- Published
- 1980
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