Biosynthesis of monensins A and B: the role of isoleucine
Language English Country United States Media print
Document type Journal Article
PubMed
3957157
DOI
10.1007/bf02928674
Knihovny.cz E-resources
- MeSH
- Aminobutyrates pharmacology MeSH
- Butyrates metabolism MeSH
- Furans biosynthesis MeSH
- Isoleucine metabolism pharmacology MeSH
- Monensin analogs & derivatives biosynthesis MeSH
- Mutation MeSH
- Norleucine pharmacology MeSH
- Streptomyces genetics metabolism MeSH
- Valine biosynthesis MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- 2-amino-3-chlorobutyric acid MeSH Browser
- 2-methylbutanoic acid MeSH Browser
- Aminobutyrates MeSH
- Butyrates MeSH
- Furans MeSH
- Isoleucine MeSH
- monensin B MeSH Browser
- Monensin MeSH
- Norleucine MeSH
- Valine MeSH
Isoleucine added to the cultivation medium of Streptomyces cinnamonensis C-100-5 induced a relative increase of the production of monensin B at the expense of monensin A. U-14C-Isoleucine was found not to be a specific monensin B precursor. The incorporation of 1-13C-2-methylbutyrate into monensins A and B showed the label to be evenly incorporated in both products at carbon atoms originating from C(1) of propionate. In regulatory mutants insensitive to 2-amino-3-chlorobutyrate isoleucine influenced the production of monensins only slightly but strains resistant to 2-aminobutyrate and norleucine decreased their total production by 2-12% in the presence of isoleucine which was associated with a decrease of monensin A content by 14-52%. The inhibitory effect of isoleucine on the biosynthesis of valine, a specific precursor of the butyrate unit of monensin A, is discussed.
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