Mechanisms of β-amino acid incorporation in polyketide macrolactam biosynthesis
| Autor: | Tadashi Eguchi, Akimasa Miyanaga, Fumitaka Kudo |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Lactams Stereochemistry Biology 01 natural sciences Biochemistry Analytical Chemistry 03 medical and health sciences Polyketide chemistry.chemical_compound Biosynthesis Moiety Vicenistatin Amino Acid Sequence Amino Acids Adenylylation chemistry.chemical_classification Dipeptide 010405 organic chemistry 0104 chemical sciences Amino acid Acyl carrier protein 030104 developmental biology chemistry Polyketides biology.protein bacteria |
| Zdroj: | Current Opinion in Chemical Biology. 35:58-64 |
| ISSN: | 1367-5931 |
| DOI: | 10.1016/j.cbpa.2016.08.030 |
| Popis: | Macrolactam antibiotics are an important class of macrocyclic polyketides. In recent years, the number of identified β-amino acid-containing macrolactams and their biosynthetic gene clusters have greatly expanded. Functional analyses of vicenistatin biosynthetic enzymes have revealed conserved biosynthetic machinery that incorporates a β-amino acid starter unit into the polyketide skeleton. A VinN-type adenylation enzyme recognizes a specific β-amino acid starter unit and ligates it with a standalone acyl carrier protein (ACP). The resulting β-aminoacyl-ACP is further aminoacylated to yield dipeptidyl-ACP, whose terminal aminoacyl moiety is a characteristic feature of polyketide biosynthetic intermediates. Structural and mechanistic analyses of enzymes that selectively recognize β-amino acids and dipeptide moieties of polyketide intermediates are reviewed. |
| Databáze: | OpenAIRE |
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