{"title":"Fatty acyl-AMP ligases in bacterial natural product biosynthesis.","authors":"Anne Liong, Pedro N Leão","doi":"10.1039/d4np00073k","DOIUrl":null,"url":null,"abstract":"<p><p>Covering: covering up to 2024Fatty Acyl-AMP Ligases (FAALs) belong to the family of adenylate-forming enzymes and activate fatty acyl substrates through adenylation. FAALs were discovered as key players in various natural product biosynthetic pathways, particularly in the assembly of polyketides and non-ribosomal peptides. These enzymes exhibit a conserved structural architecture that distinguishes them from their close relatives, the Fatty Acyl-CoA Ligases. FAALs display the starter unit in the biosynthesis of diverse natural products where they shuttle fatty acyl substrates into secondary metabolism for further chain elongation and/or modification. In this review, we cover the discovery, distribution and structure of FAALs as well as their role in natural product biosynthesis. In addition, we provide an overview about their genomic and biosynthetic contexts and summarize approaches used to analyze FAAL activity, predict their substrate specificity and to discover new compounds whose biosyntheses involve these enzymes.</p>","PeriodicalId":94,"journal":{"name":"Natural Product Reports","volume":" ","pages":""},"PeriodicalIF":10.2000,"publicationDate":"2025-02-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Natural Product Reports","FirstCategoryId":"92","ListUrlMain":"https://doi.org/10.1039/d4np00073k","RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Covering: covering up to 2024Fatty Acyl-AMP Ligases (FAALs) belong to the family of adenylate-forming enzymes and activate fatty acyl substrates through adenylation. FAALs were discovered as key players in various natural product biosynthetic pathways, particularly in the assembly of polyketides and non-ribosomal peptides. These enzymes exhibit a conserved structural architecture that distinguishes them from their close relatives, the Fatty Acyl-CoA Ligases. FAALs display the starter unit in the biosynthesis of diverse natural products where they shuttle fatty acyl substrates into secondary metabolism for further chain elongation and/or modification. In this review, we cover the discovery, distribution and structure of FAALs as well as their role in natural product biosynthesis. In addition, we provide an overview about their genomic and biosynthetic contexts and summarize approaches used to analyze FAAL activity, predict their substrate specificity and to discover new compounds whose biosyntheses involve these enzymes.
期刊介绍：
Natural Product Reports (NPR) serves as a pivotal critical review journal propelling advancements in all facets of natural products research, encompassing isolation, structural and stereochemical determination, biosynthesis, biological activity, and synthesis.
With a broad scope, NPR extends its influence into the wider bioinorganic, bioorganic, and chemical biology communities. Covering areas such as enzymology, nucleic acids, genetics, chemical ecology, carbohydrates, primary and secondary metabolism, and analytical techniques, the journal provides insightful articles focusing on key developments shaping the field, rather than offering exhaustive overviews of all results.
NPR encourages authors to infuse their perspectives on developments, trends, and future directions, fostering a dynamic exchange of ideas within the natural products research community.
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