Biosynthetic Studies of Phomopsins Unveil Posttranslational Installation of Dehydroamino Acids by UstYa Family Proteins
| Autor: | Chengwei Liu, Atsushi Minami, Taro Ozaki, Yuya Igarashi, Yuka Naganuma, Kaho Sogahata, Hideaki Oikawa |
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| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
natural products
Aspergillus oryzae enzymes Sequence (biology) Catalysis Fungal Proteins chemistry.chemical_compound Biosynthesis halogenation Amino Acids Gene knockout chemistry.chemical_classification Oxidative cyclization Molecular Structure Chemistry General Medicine General Chemistry Mycotoxins Amino acid Enzyme Biochemistry peptides Genome mining biosynthesis Protein Processing Post-Translational Function (biology) |
| Zdroj: | Angewandte chemie-international edition. 60(49):25729-25734 |
| ISSN: | 1433-7851 |
| Popis: | UstYa family proteins (DUF3328) are widely and specifically distributed in fungi. They are known to be involved in the biosynthesis of ribosomally synthesized and posttranslationally modified peptides (RiPPs) and nonribosomal peptides, and possibly catalyze various reactions, including oxidative cyclization and chlorination. In this study, we focused on phomopsin A, a fungal RiPP consisting of unique nonproteinogenic amino acids. Gene knockout experiments demonstrated that three UstYa homologues, phomYc, phomYd, and phomYe, are essential for the desaturation of amino acid moieties, showing unprecedented function among UstYa family proteins. Sequence similarity network analysis indicated that their amino acid sequences are highly diverged and that most remain uncharacterized, paving the way for genome mining of fungal metabolites with unique modifications. |
| Databáze: | OpenAIRE |
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