{"title":"Frontispiece: Cyclochlorotine Hydroxylase CctR Reveals DUF3328 as a Family of Copper-Dependent Metalloenzymes","authors":"","doi":"10.1002/ange.202583802","DOIUrl":null,"url":null,"abstract":"<p>The copper-dependent hydroxylase CctR from <i>Talaromyces islandicus</i> catalyzes selective C(sp<sup>3</sup>)─H hydroxylation of the fungal cyclic peptide cyclochlorotine, as reported by Jing-Ke Weng et al. in their Coomunication (e202512449). The image highlights CctR's homodimeric structure and the binuclear copper active site, which enables the oxidative formation of hydroxycyclochlorotine by this newly defined DUF3328 metalloenzyme family.\n\n <figure>\n <div><picture>\n <source></source></picture><p></p>\n </div>\n </figure></p>","PeriodicalId":7803,"journal":{"name":"Angewandte Chemie","volume":"137 38","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2025-09-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/ange.202583802","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Angewandte Chemie","FirstCategoryId":"1085","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1002/ange.202583802","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
Abstract
The copper-dependent hydroxylase CctR from Talaromyces islandicus catalyzes selective C(sp3)─H hydroxylation of the fungal cyclic peptide cyclochlorotine, as reported by Jing-Ke Weng et al. in their Coomunication (e202512449). The image highlights CctR's homodimeric structure and the binuclear copper active site, which enables the oxidative formation of hydroxycyclochlorotine by this newly defined DUF3328 metalloenzyme family.
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