Stoffwechselprodukte von Mikroorganismen 6‐Chlorgenistein und 6,3′‐Dichlorgenistein. 164. Mitteilung

König, Wilfried Α.; Krauss, C.; Zähner, Hans

doi:10.1002/hlca.19770600627

Cited by 20 publications

(5 citation statements)

References 5 publications

(4 reference statements)

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“…This process dramatically reduced the dataset complexity, leaving <200 unique ions from an original set of ∼3000. Manual curation showed that most of the remaining ions corresponded to halogenated molecules (based on isotope patterns), leaving twelve previously identified fasamycin and formicamycin congeners, two additional fasamycin/formicamycin congeners that remain uncharacterized due to trace levels, and the known isoflavone 6-chlorogenistein 11 (Supplementary Note 1 and Supplementary Figs. 11–14) along with a regioisomer.…”

Section: Resultsmentioning

confidence: 99%

A role for antibiotic biosynthesis monooxygenase domain proteins in fidelity control during aromatic polyketide biosynthesis

et al. 2019

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The formicamycin biosynthetic gene cluster encodes two groups of type 2 polyketide antibiotics: the formicamycins and their biosynthetic precursors the fasamycins, both of which have activity against methicillin-resistant Staphylococcus aureus . Here, we report the formicapyridines which are encoded by the same gene cluster and are structurally and biosynthetically related to the fasamycins and formicamycins but comprise a rare pyridine moiety. These compounds are trace-level metabolites formed by derailment of the major biosynthetic pathway. Inspired by evolutionary logic we show that rational mutation of a single gene in the biosynthetic gene cluster encoding an antibiotic biosynthesis monooxygenase (ABM) superfamily protein leads to a significant increase both in total formicapyridine production and their enrichment relative to the fasamycins/formicamycins. Our observations broaden the polyketide biosynthetic landscape and identify a non-catalytic role for ABM superfamily proteins in type II polyketide synthase assemblages for maintaining biosynthetic pathway fidelity.

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Section: Resultsmentioning

confidence: 99%

A role for antibiotic biosynthesis monooxygenase domain proteins in fidelity control during aromatic polyketide biosynthesis

et al. 2019

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“…Funayama et al (21) used long-range selective proton decoupling (LSPD) experiments to make a similar assignment for 8-chloro-3',4',5',7-tetrahydroxyisoflavone, which was isolated from a streptomycete grown on soybean-containing medium. Kónig et al (22) claimed to isolate 6-chlorogenistein from fermentations of S. griseus grown in a soybean-meal containing medium. However, structural assignments were based largely on the proximity of the single A ring proton signal at 6.50 ppm to the H-8 proton of 1 which resonates at 6.42 ppm, and were not confirmed by necessary proton-carbon correlation techniques such as HMBC or LSPD.…”

Section: Resultsmentioning

confidence: 99%

“…Although 2 and 3 are new compounds, there have been two other reports (21,22) of chlorinated isoflavonoids being isolated from streptomycetes grown on soybean-meal containing media. These compounds were 6-chlorogenistein, 6,3-dichlorogenistein, and 8-chloro-3' ,4', 5,7-tetrahydroxyisoflavone.…”

Section: Resultsmentioning

confidence: 99%

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Isoflavonoids from Streptomycetes: Origins of Genistein, 8-Chlorogenistein, and 6,8-Dichlorogenistein

Anyanwutaku¹,

Zirbes²,

Rosazza³

1992

J. Nat. Prod.

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Fermentations conducted with aureolic-acid producing and non-producing Streptomyces griseus strains in soybean-meal-containing medium yielded phenolic metabolites which were chomatographically and spectrally unrelated to either aureolic acid or its aglycone, chomomycinone. The yellow, phenolic compounds were isolated and characterized by *H nmr, 13C nmr, and ms as the isoflavonoidsgenistein(5,7,4'trihydroxyisoflavone) [1], 8-chlorogenistein [2], and 6,8-dichlorogenistein [3]. The presence of 1 in the soybean meal used in these fermentations was confirmed by extraction, isolation, and spectral identification. S. griseus grown in medium without soybean meal produced no isoflavonoids. Biotransformation of 1 yielded both chlorinated metabolites 2 and 3, demonstrating that these isoflavonoids are products of microbial halogenation. Labelled isoflavonoids were not obtained when S. griseus was incubated with radiolabelled acetate or phenylalanine. These results demonstrate that isoflavonoids isolated from streptomycetes cultivated in media containing plant-derived nutrients such as soybean meal or cotton seed meal likely originate from the medium components and are not of microbial biosynthetic origin.Isoflavonoids exhibit antimicrobial, insecticidal, estrogenic, and anticancer properties (1-6). The isoflavonoids are well known in members of the Leguminosae family (1), and numerous reports (7-13) claim the isolation of isoflavonoids from bacterial sources.

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“…Bacterial strains, culture conditions, and vectors Streptomyces albogriseolus MJ286-76F7 was cultured in soybean flour Ámannitol medium (Kö nig et al 1977) at 278C for 3 days with shaking at 160 rpm. Overnight cultures of Escherichia coli TG1 (Gibson 1984), E. coli BL21(DE3)pLysS (Invitrogen), and E. coli S17-1 (Simon et al 1983) were grown in HNB medium (Wynands & van Pée 2004) at 378C.…”

Section: Methodsmentioning

confidence: 99%

A flavin-dependent tryptophan 6-halogenase and its use in modification of pyrrolnitrin biosynthesis

Seibold

Schnerr

Rumpf

et al. 2006

Biocatalysis and Biotransformation

122

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Regioselective halogenation of electron rich substrates is catalysed by flavin-dependent halogenases. Thienodolin produced by Streptomyces albogriseolus contains a chlorine atom in the 6-position of the indole ring system and is believed to be derived from tryptophan. Using the gene of the tryptophan 7-halogenase (PrnA) from the pyrrolnitrin biosynthetic gene cluster the gene for a tryptophan 6-halogenase was cloned, sequenced and heterologously overexpressed in Pseudomonas strains. In vitro activity of the purified enzyme could only be shown in a two-component enzyme system consisting of the halogenase, a flavin reductase, NADH, FAD and halide ions. The enzyme catalyses the regioselective chlorination and bromination of Land D-tryptophan. In its native form the enzyme is probably a homodimer with a relative molecular mass of the subunits of 63 600 (including the His-tag). Transformation of the pyrrolnitrin producer Pseudomonas chlororaphis ACN with a plasmid containing the tryptophan 6-halogenase gene lead to the formation of the new aminopyrrolnitrin derivative 3-(2?-amino-4?-chlorophenyl)pyrrole.

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Stoffwechselprodukte von Mikroorganismen 6‐Chlorgenistein und 6,3′‐Dichlorgenistein. 164. Mitteilung

Cited by 20 publications

References 5 publications

A role for antibiotic biosynthesis monooxygenase domain proteins in fidelity control during aromatic polyketide biosynthesis

A role for antibiotic biosynthesis monooxygenase domain proteins in fidelity control during aromatic polyketide biosynthesis

Isoflavonoids from Streptomycetes: Origins of Genistein, 8-Chlorogenistein, and 6,8-Dichlorogenistein

A flavin-dependent tryptophan 6-halogenase and its use in modification of pyrrolnitrin biosynthesis

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