Aufklärung der Struktur von Hormaomycin

Rössner, Ellen; Zeeck, Axel; König, Wilfried Α.

doi:10.1002/ange.19901020122

Cited by 40 publications

(17 citation statements)

References 12 publications

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“…[13] Hormaomycin is a depsipeptide antibiotic formed by Streptomyces griseoflavus W-384. [14][15][16] It also contains a pyrrole-2-carboxylic acid moiety, which is in this case attached by an amide bond to the peptide backbone of the molecule. However, in contrast to clorobiocin and coumermycin A 1 , the pyrrole The depsipeptide antibiotic hormaomycin, which is produced by Streptomyces griseoflavus W-384, contains a 5-chloropyrrole moiety.…”

Section: Introductionmentioning

confidence: 99%

Use of a Halogenase of Hormaomycin Biosynthesis for Formation of New Clorobiocin Analogues with 5‐Chloropyrrole Moieties

et al. 2008

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The depsipeptide antibiotic hormaomycin, which is produced by Streptomyces griseoflavus W-384, contains a 5-chloropyrrole moiety. In the producer strain we identified the gene hrmQ that shows sequence similarity to FADH(2)-dependent halogenases. This gene was cloned and heterologously expressed in Streptomyces roseochromogenes var. oscitans DS12.976, which is the producer of the aminocoumarin antibiotic clorobiocin, which contains a 5-methylpyrrole moiety. For the present experiment, we used a mutant of this strain in which the respective pyrrole-5-methyltransferase had been inactivated. Expression of the halogenase hrmQ in this mutant strain led to the formation of two new clorobiocin derivatives that carried a 5-chloropyrrole moiety. These compounds were isolated on a preparative scale, their structures were elucidated by (1)H NMR spectroscopy and mass spectrometry, and their antibacterial activity was determined. The substrate of HrmQ is likely to be a pyrrole-2-carboxyl-S-[acyl carrier protein] thioester. If this assumption is true, this study presents the first experiment in combinatorial biosynthesis that uses a halogenase that acts on an acyl carrier protein-bound substrate.

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Section: Introductionmentioning

confidence: 99%

Use of a Halogenase of Hormaomycin Biosynthesis for Formation of New Clorobiocin Analogues with 5‐Chloropyrrole Moieties

et al. 2008

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“…[6] Important examples of natural nonaromatic nitro compounds are nitropropionic acid [7] and the bacterial signal metabolite hormaomycin. [8,9] Surprisingly, the biosynthesis of aromatic nitro groups is understood only to a small extent. One possible pathway involves aromatic substitution of nitro groups, as is the case for the unusual nitro alkaloid 1-nitroaknadinine (7) from Stephania sutchuenensis, which occurs simultaneously with the non-nitrated alkaloid.…”

mentioning

confidence: 99%

“…The proposed biosynthetic nitration step was mimicked in vitro with HNO 3 . [10] More recently, it was reported that a NO synthase (NOS) takes part in the nitration of the diketopiperazine thaxtomin (8), a phytotoxin produced by the plant pathogen Streptomyces turgidiscabies. [11] Additional studies revealed that tryptophan is regioselectively nitrated by a complex of Deinococcus radiodurans NOS and Trp-tRNA synthetase.…”

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confidence: 99%

Sequential Enzymatic Oxidation of Aminoarenes to Nitroarenes via Hydroxylamines

Winkler

Hertweck

2005

Angew Chem Int Ed

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“…Hormaomycin (28, Abbildung 13) ist ein anderes Hexapeptidolacton, das auch zahlreiche nichtkanonische Aminosäureeinheiten enthält, darunter zwei b-Methyl-Phe, ein Propenylprolin und ein auffälliges Nitrocyclopropylalanin. [85] Die OH-Gruppe eines Thr ist an der Bildung des Hexapeptidolacton-Makrocyclus beteiligt. Dessen Aminogruppe ist mit einem Dipeptid acyliert, der ein weiteres Nitrocyclopropyl-Ala und einen von Prolin abstammenden N-OH-2-Chlorpyrrolcarboxylrest trägt.…”

Section: Nichtproteinogene Aminosäurenunclassified

Nichtproteinogene Aminosäurebausteine für Peptidgerüste aus nichtribosomalen Peptiden und hybriden Polyketiden

2013

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Frei vorkommende nichtproteinogene Aminosäuren sind schon lange wegen ihrer antimetabolen Eigenschaften bekannt. Entdeckt werden sie meist aufgrund der Reaktivität gegenüber der katalytischen Wirkung der Zielenzyme. Führt man sie regiospezifisch in biogene Peptide und Proteine ein, kann es möglich werden, eine neue Ära der Medizinalchemie an der Grenze zwischen kleinen und großen Wirkstoffen einzuleiten. Außerdem eröffnet die ortsspezifische Funktionalisierung von Proteinen besonders attraktive Strategien für die posttranslationale Proteinmodifizierung. Auch bieten viele der Aminosäuren, die von der Natur nicht für den Einbau in Proteine ausgewählt wurden, reiche architektonische Möglichkeiten bei Einführung in ribosomal hergestellte Polypeptide. Dieser Aufsatz fasst die Biosynthesewege zu den wichtigsten Klassen nichtkanonischer Bausteine und deren Stoffwechsellogik zusammen, die in nichtribosomalen Peptidgerüsten und nichtribosomalen Peptid‐Polyketid‐Hybriden resultieren.

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Aufklärung der Struktur von Hormaomycin

Cited by 40 publications

References 12 publications

Use of a Halogenase of Hormaomycin Biosynthesis for Formation of New Clorobiocin Analogues with 5‐Chloropyrrole Moieties

Use of a Halogenase of Hormaomycin Biosynthesis for Formation of New Clorobiocin Analogues with 5‐Chloropyrrole Moieties

Sequential Enzymatic Oxidation of Aminoarenes to Nitroarenes via Hydroxylamines

Nichtproteinogene Aminosäurebausteine für Peptidgerüste aus nichtribosomalen Peptiden und hybriden Polyketiden

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