Synthesis of New N-Analogous Corollosporine Derivatives with Antibacterial Activity by Laccase-Catalyzed Amination

Mikolasch, Annett; Hessel, Susanne; Salazar, Manuela Gesell; Neumann, Helfried; Manda, Katrin; Gördes, Dirk; Schmidt, Enrico; Thurow, Kerstin; Hammer, Elke; Lindequist, Ulrike; Beller, Matthias; Schauer, Frieder

doi:10.1248/cpb.56.781

Cited by 51 publications

(38 citation statements)

References 28 publications

(34 reference statements)

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“…For instance, the ferulic acid was modified using laccase to produce two dimeric molecules with higher antioxidant capacity than the ferulic acid 16 . An additional example is the enzymatic modification of antibiotics using nitrogen compounds, the products showed higher antibiotic activity than the initial antibiotic 20,21 . Similarly, in this study, the enzymatic modification of syringic acid with aniline increased its antifungal activity.…”

Section: Amount Of Laccase (U)mentioning

confidence: 99%

“…Another example is the coupling between p-hydroquinones with p-aminobenzoic acid 18 . On the other hand, modification of antibiotics using laccase coupling reactions produced compounds with lower activities 19 , however, using nitrogen compounds to modify the antibiotics, the synthesized products showed higher antibacterial activities 20,21 . The anticancer activity of naphtohydroquinones has been improved by nuclear monoamination with anilines using laccase 22 .…”

Section: Introductionmentioning

confidence: 99%

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Improvement of the Antifungal Activity Against Botrytis Cinerea of Syringic Acid, a Phenolic Acid From Grape Pomace

Mendoza

Castro

Melo

et al. 2016

J. Chil. Chem. Soc.

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The aim of this study was to improve the antifungal activity against Botrytis cinerea of syringic acid by using the enzyme laccase to synthesize a heterodimeric compound by a coupling reaction with aniline. The synthesized heterodimer is a quinone-imine like compound (2,6-dimethoxy-4-(phenylimino)benzenone), which was characterized by using 1 H and 13 C NMR, IR, and mass spectrometry. The antifungal activity of the heterodimeric compound against B. cinerea was determined in vitro and showed a higher antifungal effect than the substrates (syringic acid and aniline), inhibiting the mycelial growth with an IC 50 value of 0.14mM and delayed 2 hours the conidial germination. Also, using the fluorochrome calcofluor white, cell wall damage was observed when B. cinerea was incubated with the compound. This is the first report on antifungal activity of this type of compound against B. cinerea.

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Section: Amount Of Laccase (U)mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Improvement of the Antifungal Activity Against Botrytis Cinerea of Syringic Acid, a Phenolic Acid From Grape Pomace

Mendoza

Castro

Melo

et al. 2016

J. Chil. Chem. Soc.

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“…Laccases can be used as biosensors of phenols in different samples, such as olive oil mill wastewater [80] and, in combination with a tyrosinase, in beer [81]. Another interesting application of laccases is their use as biocatalysts in the modification and generation of novel compounds with biological activities: for example, the modification of beta-lactamic antibiotics [82], of corollosporine, which is isolated from the marine fungus Corollospora maritima [83] and of curcuphenol, a metabolite derived from the sponge Didiscus aceratus [84]. …”

Section: Multicopper Oxidases (Mcos) and Laccasesmentioning

confidence: 99%

Finding New Enzymes from Bacterial Physiology: A Successful Approach Illustrated by the Detection of Novel Oxidases in Marinomonas mediterranea

2010

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The identification and study of marine microorganisms with unique physiological traits can be a very powerful tool discovering novel enzymes of possible biotechnological interest. This approach can complement the enormous amount of data concerning gene diversity in marine environments offered by metagenomic analysis, and can help to place the activities associated with those sequences in the context of microbial cellular metabolism and physiology. Accordingly, the detection and isolation of microorganisms that may be a good source of enzymes is of great importance. Marinomonas mediterranea, for example, has proven to be one such useful microorganism. This Gram-negative marine bacterium was first selected because of the unusually high amounts of melanins synthesized in media containing the amino acid l-tyrosine. The study of its molecular biology has allowed the cloning of several genes encoding oxidases of biotechnological interest, particularly in white and red biotechnology. Characterization of the operon encoding the tyrosinase responsible for melanin synthesis revealed that a second gene in that operon encodes a protein, PpoB2, which is involved in copper transfer to tyrosinase. This finding made PpoB2 the first protein in the COG5486 group to which a physiological role has been assigned. Another enzyme of interest described in M. mediterranea is a multicopper oxidase encoding a membrane-associated enzyme that shows oxidative activity on a wide range of substrates typical of both laccases and tyrosinases. Finally, an enzyme very specific for l-lysine, which oxidises this amino acid in epsilon position and that has received a new EC number (1.4.3.20), has also been described for M. mediterranea. Overall, the studies carried out on this bacterium illustrate the power of exploring the physiology of selected microorganisms to discover novel enzymes of biotechnological relevance.

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“…Another example is the coupling between p-hydroquinones with p-aminobenzoic acid 8 . Antibiotic modifications using laccase coupling reactions have shown products with lower activities 9 ; however, using nitrogen compounds to modify the antibiotics, the synthesized products showed higher antibacterial activities 10,11 . The anticancer activity of naphtohydroquinones has been improved by nuclear monoamination with anilines using laccase 12 .…”

Section: Introductionmentioning

confidence: 99%

Laçasse Catalyzed-Synthesis of 4,4'-Biphenyldiamine From P-Chloroaniline. Evaluation of Antifungal and Antioxidant Activities

Campos

Mendoza

Vásquez

et al. 2016

J. Chil. Chem. Soc.

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Laccase is a copper-containing oxidase that catalyzes reduction of molecular oxygen to water and the oxidation of a phenolic compound. In this paper, laccase was utilized to synthesize 4,4'-Biphenyldiamine using p-chloroaniline as substrate by means of a coupling reaction. The synthesized compound, 4,4'-Biphenyldiamine, presented low antifungal activity against the phytopathogenic fungus Botrytis cinerea, however the antioxidant ability, measurement by ORAC-PGR method, was higher than substrate.This work corresponds to the first report of synthesis 4,4'-Biphenyldiamine, from p-chloroaniline in a lacasse-catalyzed reaction.

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Synthesis of New N-Analogous Corollosporine Derivatives with Antibacterial Activity by Laccase-Catalyzed Amination

Cited by 51 publications

References 28 publications

Improvement of the Antifungal Activity Against Botrytis Cinerea of Syringic Acid, a Phenolic Acid From Grape Pomace

Improvement of the Antifungal Activity Against Botrytis Cinerea of Syringic Acid, a Phenolic Acid From Grape Pomace

Finding New Enzymes from Bacterial Physiology: A Successful Approach Illustrated by the Detection of Novel Oxidases in Marinomonas mediterranea

Laçasse Catalyzed-Synthesis of 4,4'-Biphenyldiamine From P-Chloroaniline. Evaluation of Antifungal and Antioxidant Activities

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