Biosynthesis of the fungal nonribosomal peptide penilumamide A and biochemical characterization of a pterin-specific adenylation domain.

Biosynthesis of the fungal nonribosomal peptide penilumamide A and biochemical characterization of a pterin-specific adenylation domain.
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DOI:
10.1039/d3cb00088e
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发表时间:
2023-10-04
影响因子:
4.1
通讯作者:
--
中科院分区:
其他
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我们报告了黄足曲霉CNL-338的青霉胺生物合成簇的表征。在体外重建实验表明,三个非核糖体肽合成酶是必需的构建三肽和解剖的腺苷酸化结构域的研究允许的第一个生化表征的域,选择一个蝶呤衍生的积木。第一个生物合成表征的鲁马嗪含非核糖体肽和生化调查各自的腺苷酸化结构域进行了描述。
We report the characterization of the penilumamide biosynthetic cluster from Aspergillus flavipes CNL-338. In vitro reconstitution experiments demonstrated that three nonribosomal peptide synthetases are required for constructing the tripeptide and studies with dissected adenylation domains allowed for the first biochemical characterization of a domain that selects a pterin-derived building block. The first biosynthetic characterization of a lumazine-containing nonribosomal peptide and the biochemical investigation of the respective adenylation domains is described.
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