Lichens

Grube, Martin

doi:10.1007/978-3-031-41648-4_6

Cited by 2 publications

(2 citation statements)

References 154 publications

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“…In contrast, nitrogen-containing secondary metabolites in lichen are rare and, to the best of our knowledge, indole alkaloids have never been isolated from lichens thus far. This is attributed to the fact that nitrogen is a limiting nutrient for lichen-forming fungi and therefore mostly restricted to primary metabolism [19]. Indeed, our SSN analysis shows that only one out of 67 lichen PTs— from the organism Usnea florida —localizes in the prototype DMATS cluster.…”

Section: Resultsmentioning

confidence: 98%

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Discovery and heterologous expression of functional 4-O-dimethylallyl-L-tyrosine synthases from lichen-forming fungi

Iacovelli,

He,

Sokolova

et al. 2024

Preprint

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Fungal DMATS-type aromatic prenyltransferases are a family of biosynthetic enzymes that catalyze the prenylation of a range of aromatic substrates during the biosynthesis of bioactive indole alkaloids, diketopiperazines, and meroterpenoids. Together with their broad substrate scope and soluble nature, this makes DMATS-type prenyltransferases particularly adept for applications in biocatalysis, for example to derivatize aromatic drug leads and improve their bioactivity. Here, we investigated four putative DMATS-type prenyltransferases from lichen-forming fungi, an underexplored group of organisms that produce more than 1,000 unique metabolites. We were able to successfully express two functional lichen prenyltransferases in the heterologous hostA. oryzae, which allowed us to identify them as 4-O-dimethylallyltyrosine synthases. Our extensive bioinformatic analysis shows that related lichen prenyltransferases are likely not active on indoles but rather on aromatic polyketides and phenylpropanoids, common metabolites in these organisms. Overall, our work not only provides new insights into fungal DMATS-type prenyltransferases at the family level, but it also enables future efforts aimed at identifying new candidates for biocatalytic transformations of aromatic compounds.

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Section: Resultsmentioning

confidence: 98%

“…DMATSs are known to be involved in the biosynthesis of indole alkaloids—compounds with potent biological activities in animals, most notably on the nervous and circulatory systems [18]. However, to the best of our knowledge, no indole alkaloids have ever been reported in extracts of lichens [19].…”

Section: Introductionmentioning

confidence: 99%

Discovery and heterologous expression of functional 4-O-dimethylallyl-L-tyrosine synthases from lichen-forming fungi

Iacovelli,

He,

Sokolova

et al. 2024

Preprint

View full text Add to dashboard Cite

show abstract

Discovery and Heterologous Expression of Functional 4-O-Dimethylallyl-l-tyrosine Synthases from Lichen-Forming Fungi

Iacovelli,

He,

Sokolova

et al. 2024

J. Nat. Prod.

View full text Add to dashboard Cite

Fungal aromatic prenyltransferases are a family of biosynthetic enzymes that catalyze the prenylation of a range of aromatic substrates during the biosynthesis of bioactive indole alkaloids, diketopiperazines, and meroterpenoids. Their broad substrate scope and soluble nature make these enzymes particularly adept for applications in biocatalysis; for example, the enzymatic derivatization of aromatic drugs improves their bioactivity. Here, we investigated four putative aromatic prenyltransferases from lichen-forming fungi, an underexplored group of organisms that produce more than 1,000 unique metabolites. We successfully expressed two enzymes, annotated as dimethylallyltryptophan synthases, from two lichen species in the heterologous host A. oryzae. Based on their in vivo activity, we hypothesize that these enzymes are in fact 4-O-dimethylallyl-L-tyrosine synthases. Our extensive bioinformatic analysis further confirmed that these and related lichen aromatic prenyltransferases are likely not active on indoles but rather on aromatic polyketides and phenylpropanoids, major metabolites in lichens. Overall, our work provides new insights into fungal aromatic prenyltransferases at the family level and enables future efforts aimed at identifying new candidates for biocatalytic transformations of aromatic compounds.

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Lichens

Cited by 2 publications

References 154 publications

Discovery and heterologous expression of functional 4-O-dimethylallyl-L-tyrosine synthases from lichen-forming fungi

Discovery and heterologous expression of functional 4-O-dimethylallyl-L-tyrosine synthases from lichen-forming fungi

Discovery and Heterologous Expression of Functional 4-O-Dimethylallyl-l-tyrosine Synthases from Lichen-Forming Fungi

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