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Structural Profiling of Bioactive Compounds with Medicinal Potential from Traditional Indian Medicinal Plants
Published in Jayanta Kumar Patra, Gitishree Das, Sanjeet Kumar, Hrudayanath Thatoi, Ethnopharmacology and Biodiversity of Medicinal Plants, 2019
C. Sareena, A. Anju Suresh, Swetha Sunil, T. V. Suchithra
The mode of action of 2-hydroxyl 5-bezylisouvarinol, berberine, curcumin, dichamanetin, kaempferol, p-coumaric acid, quercitrin and sanguinarine were reported against Bacillus subtilis. The most common target reported in B. subtilis is FtZ. Berberine, 2-hydroxy 5-benzyl isouvarinol, curcumin, dichamanetin and sanguinarine can block bacterial division by binding on the FtZ protein. In addition to FtZ, berberine has two more target namely, Bmr multidrug efflux transporter and BmrR, transcriptional regulator. In the case of kaempferol, targets are ImrA (a transcriptional repressor of lmrAB and yxaGH operons), ImrB Efflux pump protein, Quercetin dioxygenase, YxaF (a transcriptional regulator) and YxaH (a putative integral inner membrane protein). The p-coumaric acid targets histidine ammonia-lyase, phenolic acid decarboxylase, succinyl CoA-3-oxoacid CoA-transferase, and urease γ subunit. While the targets of action of quercitrin are DesR-DesK two-component response regulator, phosphotransferase system (PTS) lichenan-specific enzyme IIA component, polar chromosome segregation protein, and quercetin dioxygenase. They can interfere with membrane lipid fluidity regulation, uptake, and metabolism of lichenan, axial filament formation, and resistance mechanism respectively.
Handbook of Phytochemical Constituents of GRAS Herbs and Other Economic Plants
Published in James A. Duke, Handbook of Phytochemical Constituents of GRAS Herbs and Other Economic Plants, 2017
“Thai Chaulmoogra”ARACHNIC-ACID SD 411/CHAULMOOGRIC-ACID SD CCODIHYDROCHAULMOOGRIC-ACID SD 411/DIHYDROHYDNOCARPIC-ACID SD 411/GORLIC-ACID SD CCOHYDNOCARPIC-ACID (51 %OEL) FR HHBISOGALEIC-ACID SD 411/LICHENIN FR HHBTARAKTOGENIC-ACID SD 411/
Linear and branched β-Glucans degrading enzymes from versatile Bacteroides uniformis JCM 13288T and their roles in cooperation with gut bacteria
Published in Gut Microbes, 2020
Ravindra Pal Singh, Sivasubramanian Rajarammohan, Raksha Thakur, Mohsin Hassan
The BuGH158 was predicted to cleave 1–3 linkage of curdlan. It showed very weak activity against native curdlan; therefore, it was pretreated with two different methods. With the pre-treatment, Km of curdlan-B was slightly reduced, while Km of curdlan-A was dropped to approximately threefold (Figure 4(a)). As a result of pre-treatment, Kcat of curdlan-A and curdlan-B increased around 2.5 to 1.7-fold, respectively. Since curdlan is less soluble in water and in order to rationally check impact of the solubility problem, the BuGH158 was tested with laminarin and it showed same magnitude of Km, but Kcat was increased by twofold. These patterns highlight that enzyme could not properly access the binding site on the substrate when curdlan is present in triple helix conformation (Figure 4). During the digestion of laminarin, it can generate DP-1 to DP-3 oligosaccharides from laminarin as final product, whereas it generated a variety of oligosaccharides from curdlan-A (Figure 4(b and c)). Successively, Michaelis-Menten kinetics of BuGH158 with yeast β- glucan and lichenin at the optimum pH and temperature (Supplementary Fig. S6) revealed that Kcat/Km is about 6-fold magnitude higher for lichenin than yeast β- glucan. Three different major oligosaccharides were detected from lichenin, i.e. DP-2 to DP-4 (Figure 4(b and d)). These assays confirmed that GH158 is an endolytic enzyme with broad spectrum hydrolytic potential.