排序方式: 共有9条查询结果,搜索用时 15 毫秒
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Scharf DH Remme N Habel A Chankhamjon P Scherlach K Heinekamp T Hortschansky P Brakhage AA Hertweck C 《Journal of the American Chemical Society》2011,133(32):12322-12325
Gliotoxin is a virulence factor of the human pathogen Aspergillus fumigatus , the leading cause of invasive aspergillosis. Its toxicity is mediated by the unusual transannular disulfide bridge of the epidithiodiketopiperazine (ETP) scaffold. Here we disclose the critical role of a specialized glutathione S-transferase (GST), GliG, in enzymatic sulfurization. Furthermore, we show that bishydroxylation of the diketopiperazine by the oxygenase GliC is a prerequisite for glutathione adduct formation. This is the first report of the involvement of a GST in enzymatic C-S bond formation in microbial secondary metabolism. 相似文献
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Regioselective Dichlorination of a Non‐Activated Aliphatic Carbon Atom and Phenolic Bismethylation by a Multifunctional Fungal Flavoenzyme 下载免费PDF全文
Pranatchareeya Chankhamjon Dr. Yuta Tsunematsu Dr. Mie Ishida‐Ito Yuzuka Sasa Florian Meyer Dr. Daniela Boettger‐Schmidt Barbara Urbansky Klaus‐Dieter Menzel Dr. Kirstin Scherlach Prof. Dr. Kenji Watanabe Prof. Dr. Christian Hertweck 《Angewandte Chemie (International ed. in English)》2016,55(39):11955-11959
The regioselective functionalization of non‐activated carbon atoms such as aliphatic halogenation is a major synthetic challenge. A novel multifunctional enzyme catalyzing the geminal dichlorination of a methyl group was discovered in Aspergillus oryzae (Koji mold), an important fungus that is widely used for Asian food fermentation. A biosynthetic pathway encoded on two different chromosomes yields mono‐ and dichlorinated polyketides (diaporthin derivatives), including the cytotoxic dichlorodiaporthin as the main product. Bioinformatic analyses and functional genetics revealed an unprecedented hybrid enzyme (AoiQ) with two functional domains, one for halogenation and one for O‐methylation. AoiQ was successfully reconstituted in vivo and in vitro, unequivocally showing that this FADH2‐dependent enzyme is uniquely capable of the stepwise gem‐dichlorination of a non‐activated carbon atom on a freestanding substrate. Genome mining indicated that related hybrid enzymes are encoded in cryptic gene clusters in numerous ecologically relevant fungi. 相似文献
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Cover Picture: Biosynthesis of the Halogenated Mycotoxin Aspirochlorine in Koji Mold Involves a Cryptic Amino Acid Conversion (Angew. Chem. Int. Ed. 49/2014) 下载免费PDF全文
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Biosynthesis of the Halogenated Mycotoxin Aspirochlorine in Koji Mold Involves a Cryptic Amino Acid Conversion 下载免费PDF全文
Pranatchareeya Chankhamjon Dr. Daniela Boettger‐Schmidt Dr. Kirstin Scherlach Barbara Urbansky Dr. Gerald Lackner Daniel Kalb Hans‐Martin Dahse Prof. Dr. Dirk Hoffmeister Prof. Dr. Christian Hertweck 《Angewandte Chemie (International ed. in English)》2014,53(49):13409-13413
Aspirochlorine ( 1 ) is an epidithiodiketopiperazine (ETP) toxin produced from koji mold (Aspergillus oryzae), which has been used in the oriental cuisine for over two millennia. Considering its potential risk for food safety, we have elucidated the molecular basis of aspirochlorine biosynthesis. By a combination of genetic and chemical analyses we found the acl gene locus and identified the key role of AclH as a chlorinase. Stable isotope labeling, biotransformation, and mutational experiments, analysis of intermediates and an in vitro adenylation domain assay gave totally unexpected insights into the acl pathway: Instead of one Phe and one Gly, two Phe units are assembled by an iterative non‐ribosomal peptide synthetase (NRPS, AclP), followed by halogenation and an unprecedented Phe to Gly amino acid conversion. Biological assays showed that both amino acid transformations are required to confer cytotoxicity and antifungal activity to the mycotoxin. 相似文献
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