{"title":"来自铜绿微囊藻 NIES-4285 蓝藻的双同源含酪氨酸肽及其生物合成。","authors":"Chin-Soon Phan, Zhengyi Ling, Jakia Jerin Mehjabin, Kenichi Matsuda, Nurcahyo Iman Prakoso, Taiki Umezawa, Toshiyuki Wakimoto, Tatsufumi Okino","doi":"10.1021/acs.jnatprod.4c00972","DOIUrl":null,"url":null,"abstract":"<p><p>Chemical investigation of the cyanobacterium <i>Microcystis aeruginosa</i> NIES-4285 led to the isolation of six new natural products, microginins 705 (<b>1</b>), 719 (<b>2</b>), 733A (<b>3</b>), 733B (<b>4</b>), and 733C (<b>5</b>), and anabaenopeptin 885 (<b>7</b>), and three known compounds, anabaenopeptins 871 (<b>6</b>), B (<b>8</b>), and F (<b>9</b>). Planar structures and absolute configurations for <b>1</b>-<b>7</b> were determined by 2D NMR, HRMS, and Marfey's analyses. Microginin 733C (<b>5</b>), and anabaenopeptins 871 (<b>6</b>) and 885 (<b>7</b>) contained a unique residue of 2-amino-5-(4-hydroxyphenyl)pentanoic acid (Ahppa): doubly homologated tyrosine (di-hTyr). The biosynthetic origin of this nonproteinogenic amino acid di-hTyr was investigated, and it was found that MaHphABCDE are involved in the production of di-hTyr. In addition, biochemical characterization of aminotransferase MaHphE showed that it is a promiscuous enzyme. This result expanded the biocatalytic toolbox for amino acid homologation.</p>","PeriodicalId":47,"journal":{"name":"Journal of Natural Products ","volume":" ","pages":"2629-2639"},"PeriodicalIF":3.3000,"publicationDate":"2024-11-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Doubly Homologated Tyrosine-Containing Peptides from the Cyanobacterium <i>Microcystis aeruginosa</i> NIES-4285 and Their Biosynthesis.\",\"authors\":\"Chin-Soon Phan, Zhengyi Ling, Jakia Jerin Mehjabin, Kenichi Matsuda, Nurcahyo Iman Prakoso, Taiki Umezawa, Toshiyuki Wakimoto, Tatsufumi Okino\",\"doi\":\"10.1021/acs.jnatprod.4c00972\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Chemical investigation of the cyanobacterium <i>Microcystis aeruginosa</i> NIES-4285 led to the isolation of six new natural products, microginins 705 (<b>1</b>), 719 (<b>2</b>), 733A (<b>3</b>), 733B (<b>4</b>), and 733C (<b>5</b>), and anabaenopeptin 885 (<b>7</b>), and three known compounds, anabaenopeptins 871 (<b>6</b>), B (<b>8</b>), and F (<b>9</b>). Planar structures and absolute configurations for <b>1</b>-<b>7</b> were determined by 2D NMR, HRMS, and Marfey's analyses. Microginin 733C (<b>5</b>), and anabaenopeptins 871 (<b>6</b>) and 885 (<b>7</b>) contained a unique residue of 2-amino-5-(4-hydroxyphenyl)pentanoic acid (Ahppa): doubly homologated tyrosine (di-hTyr). The biosynthetic origin of this nonproteinogenic amino acid di-hTyr was investigated, and it was found that MaHphABCDE are involved in the production of di-hTyr. In addition, biochemical characterization of aminotransferase MaHphE showed that it is a promiscuous enzyme. This result expanded the biocatalytic toolbox for amino acid homologation.</p>\",\"PeriodicalId\":47,\"journal\":{\"name\":\"Journal of Natural Products \",\"volume\":\" \",\"pages\":\"2629-2639\"},\"PeriodicalIF\":3.3000,\"publicationDate\":\"2024-11-22\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Natural Products \",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1021/acs.jnatprod.4c00972\",\"RegionNum\":2,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2024/10/30 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"Q2\",\"JCRName\":\"CHEMISTRY, MEDICINAL\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Natural Products ","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1021/acs.jnatprod.4c00972","RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2024/10/30 0:00:00","PubModel":"Epub","JCR":"Q2","JCRName":"CHEMISTRY, MEDICINAL","Score":null,"Total":0}
Doubly Homologated Tyrosine-Containing Peptides from the Cyanobacterium Microcystis aeruginosa NIES-4285 and Their Biosynthesis.
Chemical investigation of the cyanobacterium Microcystis aeruginosa NIES-4285 led to the isolation of six new natural products, microginins 705 (1), 719 (2), 733A (3), 733B (4), and 733C (5), and anabaenopeptin 885 (7), and three known compounds, anabaenopeptins 871 (6), B (8), and F (9). Planar structures and absolute configurations for 1-7 were determined by 2D NMR, HRMS, and Marfey's analyses. Microginin 733C (5), and anabaenopeptins 871 (6) and 885 (7) contained a unique residue of 2-amino-5-(4-hydroxyphenyl)pentanoic acid (Ahppa): doubly homologated tyrosine (di-hTyr). The biosynthetic origin of this nonproteinogenic amino acid di-hTyr was investigated, and it was found that MaHphABCDE are involved in the production of di-hTyr. In addition, biochemical characterization of aminotransferase MaHphE showed that it is a promiscuous enzyme. This result expanded the biocatalytic toolbox for amino acid homologation.
期刊介绍：
The Journal of Natural Products invites and publishes papers that make substantial and scholarly contributions to the area of natural products research. Contributions may relate to the chemistry and/or biochemistry of naturally occurring compounds or the biology of living systems from which they are obtained.
Specifically, there may be articles that describe secondary metabolites of microorganisms, including antibiotics and mycotoxins; physiologically active compounds from terrestrial and marine plants and animals; biochemical studies, including biosynthesis and microbiological transformations; fermentation and plant tissue culture; the isolation, structure elucidation, and chemical synthesis of novel compounds from nature; and the pharmacology of compounds of natural origin.
When new compounds are reported, manuscripts describing their biological activity are much preferred.
Specifically, there may be articles that describe secondary metabolites of microorganisms, including antibiotics and mycotoxins; physiologically active compounds from terrestrial and marine plants and animals; biochemical studies, including biosynthesis and microbiological transformations; fermentation and plant tissue culture; the isolation, structure elucidation, and chemical synthesis of novel compounds from nature; and the pharmacology of compounds of natural origin.
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