scholarly journals Characterization of glucosyltransferase and glucuronosyltransferase family members reveals how major flavone glycoside accumulate in the root of Scutellaria baicalensis

2021 ◽  
Author(s):  
Tianlin Pei ◽  
Tian Li ◽  
Xiaoqiang Li ◽  
Yijia Yin ◽  
Mengying Cui ◽  
...  

Flavonoid glycosides extracted from roots of Scutellaria baicalensis exhibit strong pharmaceutical effect in antitumor, antioxidative, anti-inflammatory, and antiviral activity. UDP glycosyltransferase family members are responsible for the transfer of a glycosyl moiety from UDP sugars to a wide range of acceptor flavonoids. Here, we report the phylogenetic analysis, tissue-specific expression and biochemical characterization of 10 glucosyltrasferases (SbUGTs) and 6 glucuronosyltransferases (SbUGATs) based on the recently released genome of S. baicalensis. These results reveal that the high expression level and affinity to substrate of SbUGAT4 make baicalin become the richest flavonoid glycoside in the root of S. baicalensis.

2019 ◽  
Vol 6 (6) ◽  
pp. 190150 ◽  
Author(s):  
Yuan Li ◽  
Xin-Lin Li ◽  
Chang-Jiang-Sheng Lai ◽  
Rui-Shan Wang ◽  
Li-Ping Kang ◽  
...  

Andrographis paniculata is an important traditional medicinal herb in South and Southeast Asian countries with diverse pharmacological activities that contains various flavonoids and flavonoid glycosides. Glycosylation can transform aglycones into more stable, biologically active and structurally diverse glycosides. Here, we report three glycosyltransferases from the leaves of A. paniculata (ApUFGTs) that presented wide substrate spectra for flavonoid glycosylation and exhibited multi-site glycosylation on the substrate molecules. They acted on the 7-OH position of the A ring and were able to glycosylate several other different types of compounds. The biochemical properties and phylogenetic analysis of these glycosyltransferases were also investigated. This study provides a basis for further research on the cloning of genes involved in glycosylation from A. paniculata and offers opportunities for enhancing flavonoid glycoside production in heterologous hosts. These enzymes are expected to become effective tools for drug discovery and for the biosynthesis of derivatives via flavonoid glycosylation.


2008 ◽  
Vol 78 (Suppl_1) ◽  
pp. 297-297
Author(s):  
Keiichiro Yogo ◽  
Grisnarong Wongbandue ◽  
Akihito Ishigami ◽  
Hidenari Takahara ◽  
Tetsuya Kohsaka

2002 ◽  
Vol 249 (2) ◽  
pp. 204-218 ◽  
Author(s):  
Cornelia Leimeister ◽  
Christian Steidl ◽  
Nina Schumacher ◽  
Sabine Erhard ◽  
Manfred Gessler

2011 ◽  
Vol 49 (4) ◽  
pp. 635-640 ◽  
Author(s):  
Maria Dimou ◽  
Chrysoula Zografou ◽  
Anastasia Venieraki ◽  
Panagiotis Katinakis

Biologia ◽  
2011 ◽  
Vol 66 (1) ◽  
Author(s):  
Anjuli Sood ◽  
Pawan Singh ◽  
Arun Kumar ◽  
Rajendra Singh ◽  
Radha Prasanna

AbstractN2-fixing cyanobacteria are unique in their capacity to form symbiotic associations with a wide range of eukaryotic hosts belonging to different plant groups. The present study was undertaken to analyze the interactions of the cyanobiont PI 01 (from Azolla pinnata) and Nostoc PCC 9229 (from Gunnera monoika) with wheat seedlings, in co-culturing experiments. Each of the cyanobionts enhanced significantly the volume of root and shoot biomass in the experimental cultures. The transverse sections of roots in the co-cultured seedlings revealed the presence of aseriate packets of cyanobionts below the root epidermis. The investigated cyanobionts excreted amino acids (His, Met, Val) and sugars into the medium, while indoleacetic acid was detected when the cyanobionts were grown in a tryptophan containing medium. During the co-culturing, sugars and proline were detected in the extracellular filtrates. It can be hypothesized that these sugars and amino acids may serve as signal substances in the development of functional associations between the relevant cyanobionts and the wheat seedlings.


2015 ◽  
Vol 43 (5) ◽  
pp. 931-936 ◽  
Author(s):  
François Lefèvre ◽  
Amandine Baijot ◽  
Marc Boutry

ATP-binding cassette (ABC) proteins form a large and ubiquitous family, most members of which are membrane-associated primary transporters. Plant genomes code for a particularly large number of these ABC proteins, with more than 120 genes present in both Arabidopsis thaliana and Oryza sativa (rice). Although plant ABC transporters were initially identified as detoxifiers, sequestering xenobitotics into the vacuole, they were later found to be involved in a wide range of essential physiological processes. Currently, the exact substrates transported by most of these transporters are still unknown and we therefore cannot exclude that a single substrate (e.g. a hormone) is responsible for the diversity of physiological roles. This gap in our knowledge is mainly due to the fact that only a few studies have used direct methods to identify the substrates of these membrane transporters. To address this issue, transport assays involving isolated cells, vesicular membranes or reconstituted liposomes are essential. In this review, we will highlight the importance of the direct biochemical characterization of plant ABC transporters and give some insights into the current status of the homologous and heterologous expression of such proteins.


2016 ◽  
Author(s):  
Jessica M Morrison ◽  
Mostafa S Elshahed ◽  
Noha Youssef

Background. The anaerobic gut fungi (phylum Neocallimastigomycota) represent a promising source of novel lignocellulolytic enzymes. Here, we report on the cloning, expression, and characterization of a glycoside hydrolase family 39 (GH39) enzyme (Bgxg1) that is highly transcribed by the anaerobic fungus Orpinomyces sp. strain C1A under different growth conditions. This represents the first study of a GH39-family enzyme from the anaerobic fungi. Methods. Using enzyme activity assays, we performed a biochemical characterization of Bgxg1 on a variety of substrates over a wide range of pH and temperature values to identify the optimal enzyme conditions and the specificity of the enzyme. In addition, substrate competition studies and comparative modeling efforts were completed. Results. Contrary to the narrow range of activities (β-xylosidase or α-L-iduronidase) observed in previously characterized GH39 enzymes, Bgxg1 is unique in that it is multifunctional, exhibiting strong β-xylosidase, β-glucosidase, β-galactosidase activities (11.5 ± 1.2, 73.4 ± 7.15, and 54.6 ± 2.26 U/mg, respectively) and a weak xylanase activity (10.8 ± 1.25 U/mg), strength determined as compared to previously characterized enzymes. Physiological characterization revealed that Bgxg1 is active over a wide range of pH (3-8, optimum 6) and temperatures (25-60°C, optimum 39°C), and possesses excellent temperature and thermal stability. Substrate competition assays suggest that all observed activities occur at a single active site. Using comparative modeling and bioinformatics approaches, we putatively identified ten amino acid differences between Bgxg1 and previously biochemically characterized GH39 β-xylosidases that we speculate could impact active site architecture, size, charge, and/or polarity. The putative contributions of these changes to the observed relaxed specificities in Bgxg1 are discussed. Discussion. Collectively, the unique capabilities and multi-functionality of Bgxg1 render it an excellent candidate for inclusion in enzyme cocktails mediating cellulose and hemicellulose saccharification from lignocellulosic biomass.


2020 ◽  
Vol 17 (36) ◽  
pp. 831-844
Author(s):  
Kutayba Farhan DAWOOD ◽  
Ayoob Obaid ALFALAHI ◽  
Shamil Ismail NEAMAH ◽  
Omar Mahmood DHANNOON

Plants used in folk medicine not only represent rich sources for therapeutic materials, but it also plays a crucial role in developing completely or partially novel synthesized drugs. Mharut plant (Ferula rutbaensis) is an integral part of Bedouin therapeutic practices in the western desert of Anbar province-Iraq. Still, to date, this is the first study describing its phytochemical constituents. The plant was growing near the Iraq-Saudi Arabia borders and adapted to a wide range of soils. Traditionally, F. rutbaensis has been widely used to treat acne, stomach and bowel disorders, food poisoning and respiratory problems. Fresh plant samples were collected and morphologically characterized. Likewise, the ITS-based DNA barcoding technique was efficiently used to approve the morphological identification of F. rutbaensis. The GC-MS spectrum was adopted in the phytochemical characterization of aqueous and methanol extracts of fresh and dry plant parts. The aqueous extract of dry roots was the richest source for bioactive compounds than fresh or methanolic extracts of either fresh or dry plant parts. In general, the detected phytochemicals falling into fatty acids, terpenes, hydrocarbon alkanes, and esters. Notably, fatty acids in Oleic and Palmitic acids were the two most abundant bioactive compounds in both aqueous and methanolic extracts of plant fresh and dry roots. The detected unsaturated fatty acids and/or other bioactive components are laying behind the therapeutic properties of F. rutbaensis that can be useful ingredients to prepare Mharut-based cosmetics such as medical soaps, body lotions, skin conditioners and sunscreens. Additionally, some other components were found to have anti-inflammatory, antioxidants, and antimicrobial properties. Further investigations will be necessary to confirm the antimicrobial activity of F. rutbaensis extracts.


1993 ◽  
Vol 240 (2) ◽  
pp. 290-295 ◽  
Author(s):  
Madan Thangavelu ◽  
Dmitry Belostotsky ◽  
Michael W. Bevan ◽  
Richard B. Flavell ◽  
Hilary J. Rogers ◽  
...  

2019 ◽  
Author(s):  
Maria Marta Caffaro ◽  
Karina Beatriz Balestrasse ◽  
Gerardo Rubio

Abstract. Four purified phytases isolated from Aspergillus niger and Escherichia coli were characterized biochemically and in terms of their adsorption to soils belonging to the Mollisol order. Three different organic P substrates were used to measure enzyme activity in a wide range of pH (2.3 to 9) and temperatures (−10° to 70 °C): p-nitrophenyl-phosphate, glyceraldehyde-3-phosphate and phytic acid. Phytases from A. niger showed a higher capacity to release P (36 to 50 % of P contained in the substrates, 44 to 62 μg P), than phytases from E. coli (24 to 36 %, 20 to 44 μg P). The amount of P released from organic P substrates by A. niger phytases followed the following range: p-nitrophenyl-phosphate > glyceraldehyde-3-phosphate > phytic acid whereas in E. coli phytases the order was p-nitrophenyl-phosphate/glyceraldehyde-3-phosphate > phytic acid. All phytases were active throughout the pH and temperature ranges for optimum crop production. The proportion of phytases found in the solid phase of the soil 60 minutes after addition was lower than that found in the liquid phase (23–34 % vs. 66–77 %). Obtained results are promising in terms of the use of phytases as a complement to P fertilization in agricultural settings and encourages further studies under field conditions.


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