<i>N</i>-Acyl Dehydrotyrosines, Tyrosinase Inhibitors from the Marine Bacterium <i>Thalassotalea</i> sp. PP2-459

Deering, Robert W.; Chen, Jianwei; Sun, Jiadong; Ma, Hang; Dubert, Javier; Barja, Juan L.; Seeram, Navindra P.; Wang, Hong; Rowley, David C.

doi:10.1021/acs.jnatprod.5b00972

Cited by 31 publications

(48 citation statements)

References 28 publications

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“…Analysis of in vitro and in vivo effects of stieleriacine A 1 . In previous studies, it has been shown that N-acyl amino acids can display antimicrobial activities against various bacteria [12][13][14][15][16][17] , while N-acylated tyrosine derivatives were shown to inhibit the enzyme tyrosinase 18 . Employing in vivo and in vitro assays with purified stieleriacine A 1 , the major stieleriacine produced by strain Mal15 T , we could show that these compounds exhibit only moderate antimicrobial activity against Gram-positive bacteria (Supplementary Table 1) and negligible inhibition of tyrosinase, indicating that neither of the two effects reflects the major function of stieleriacines.…”

Section: Resultsmentioning

confidence: 99%

“…However, it should not be excluded that the strain is capable of producing other N-acyl amino acids. The C-methylation in metaposition of the aromatic ring and an uncommon double bond in the α,β-position of the tyrosine moiety were identified as characteristic molecular features separating stieleriacines from other N-acyl tyrosines identified so far 18,26 . In the biosynthetic cluster, Mal15_37250 encodes a putative methyltransferase similar to the L-tyrosine C3-methyltransferase SfmM2 of Streptomyces lavendulae.…”

Section: Supplementary Table 2 Supplementary Movie 1 and 2)mentioning

confidence: 96%

“…Genome analysis identifies a putative stieleriacine biosynthesis pathway. Although microbial synthesis of N-acyl tyrosine molecules has been reported in several recent studies 18,26,27 , the genetic basis for biosynthesis has not been elucidated in greater detail. The key enzyme for stieleriacine biosynthesis in strain Mal15 T is likely an N-acyl amino acid synthase (NAS) (Fig.…”

Section: Supplementary Table 2 Supplementary Movie 1 and 2)mentioning

confidence: 99%

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The planctomycete Stieleria maiorica Mal15T employs stieleriacines to alter the species composition in marine biofilms

et al. 2020

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Bacterial strains of the phylum Planctomycetes occur ubiquitously, but are often found on surfaces of aquatic phototrophs, e.g. alga. Despite slower growth, planctomycetes are not outcompeted by faster-growing bacteria in biofilms on such surfaces; however, strategies allowing them to compensate for slower growth have not yet been investigated. Here, we identified stieleriacines, a class of N-acylated tyrosines produced by the novel planctomycete Stieleria maiorica Mal15T, and analysed their effects on growth of the producing strain and bacterial species likely co-occurring with strain Mal15T. Stieleriacines reduced the lag phase of Mal15T and either stimulated or inhibited biofilm formation of two bacterial competitors, indicating that Mal15T employs stieleriacines to specifically alter microbial biofilm composition. The genetic organisation of the putative stieleriacine biosynthetic cluster in strain Mal15T points towards a functional link of stieleriacine biosynthesis to exopolysaccharide-associated protein sorting and biofilm formation.

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Section: Resultsmentioning

confidence: 99%

Section: Supplementary Table 2 Supplementary Movie 1 and 2)mentioning

confidence: 96%

Section: Supplementary Table 2 Supplementary Movie 1 and 2)mentioning

confidence: 99%

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The planctomycete Stieleria maiorica Mal15T employs stieleriacines to alter the species composition in marine biofilms

et al. 2020

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“…Through a combination of mass spectrometry and spectroscopic techniques, with notable insight provided by 1,1-ADEQUATE NMR, 1 H-15 N HMBC NMR, and the identity of degradation products formed in basic methanol 51,52 , we were able to assign the products of oxzAB as a series of oxazolones (Figs. 4b, S9, S10).…”

Section: Heterologous Expression Of Oxzab Leads To Production Of Novementioning

confidence: 99%

Co-Occurrence of Enzyme Domains Guides the Discovery of an Oxazolone Synthetase

Rond

Asay

Moore

2020

Preprint

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Multi-domain enzymes are cellular machines that orchestrate two or more catalytic activities to carry out metabolic transformations with increased control and speed. Here, we report the development of a new genome mining approach for the targeted discovery of new metabolic pathways based on the cooccurrence of enzyme domains (CO-ED) in a single protein. CO-ED was designed to identify unannotated multifunction proteins for accelerated functional characterization and discovery based on the premise that linked enzyme domains have evolved to function collaboratively. Guided by CO-ED, we targeted an unannotated predicted ThiF-nitroreductase di-domain enzyme found in more than 50 proteobacteria. Through heterologous expression and biochemical reconstitution of this enzyme, we discovered a series of new natural products containing the rare oxazolone heterocycle, and identified the first reported oxazolone synthetase in biology. This proof-of-principle experiment validates CO-ED-guided genome mining as a new method with potential broad utility for both the discovery of novel enzymatic transformations and the functional gene annotation of multi-domain enzymes. SignificanceBillions of years of evolution has provided immense genetic -and hence, biochemical -diversity, much of which is still un-annotated. Genome mining seeks to explore this "metabolic dark matter" for new pharmaceuticals, biocatalysts and biochemical insight. Historically, these efforts have been guided by sequence homology to known biosynthetic genes, which often leads to re-discovery of known enzymatic transformations. Here, in contrast, we prioritize enzymes harboring multiple catalytic domains in combinations that have not been investigated before. Our approach, "CO-ED", led to the discovery of new natural products and the identification of an enzyme capable of catalyzing the formation of an oxazolone heterocycle, a versatile chemical feedstock. CO-ED has the potential to guide the functional characterization of thousands of unannotated multi-domain enzymes.

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“…The marine bacterium Thalassotalea sp. PP2-459, isolated from a bivalve, is also described to produce a N-acyl dehydrotyrosine derivatives tyrosinase inhibitor the thalassotalic acids [88]. Astaxanthin, which belongs to the carotenoids family, also presents interesting depigmentation properties.…”

Section: Active Ingredients With Skin Whitening Propertiesmentioning

confidence: 99%

Applications for Marine Resources in Cosmetics

2017

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Abstract:Marine resources represent an interesting source of active ingredients for the cosmetics industry. Algae (macro and micro) are rich in proteins, amino acids, carbohydrates, vitamins (A, B, and C) and oligo-elements such as copper, iron and zinc. All those active principles play roles in hydration, firming, slimming, shine and protection. Marine organisms inhabit a wide spectrum of habitats. Photo-protective compounds can be obtained from organisms subjected to strong light radiation, such as in tropical systems or in shallow water. In the same way, molecules with antioxidant potential can be obtained from microorganisms inhabiting extreme systems such as hydrothermal vents. For example, marine bacteria collected around deep-sea hydrothermal vents produce complex and innovative polysaccharides in the laboratory which are useful in cosmetics. There are many properties that will be put forward by the cosmetic industries.

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N-Acyl Dehydrotyrosines, Tyrosinase Inhibitors from the Marine Bacterium Thalassotalea sp. PP2-459

Cited by 31 publications

References 28 publications

The planctomycete Stieleria maiorica Mal15T employs stieleriacines to alter the species composition in marine biofilms

The planctomycete Stieleria maiorica Mal15T employs stieleriacines to alter the species composition in marine biofilms

Co-Occurrence of Enzyme Domains Guides the Discovery of an Oxazolone Synthetase

Applications for Marine Resources in Cosmetics

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