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Structure and Biosynthesis of Lignin
Published in Jean-Luc Wertz, Magali Deleu, Séverine Coppée, Aurore Richel, Hemicelluloses and Lignin in Biorefineries, 2017
Jean-Luc Wertz, Magali Deleu, Séverine Coppée, Aurore Richel
In plants, chorismate is a common precursor of at least four branches of metabolic pathways leading to the formation of Trp, Phe/Tyr, salicylate/phylloquinone, and folate.10 Four enzymes catalyze the committed step of the respective pathways and compete for chorismate. The Trp pathway converts chorismate to Trp via six enzymatic reactions. In contrast to the Trp pathway, the knowledge of the plant Phe and Tyr pathways is still in its infancy. In the first step of the pathways, chorismate is converted by chorismate mutase (CM) to prephenate, of which subsequent conversion to Phe and Tyr may occur via two alternative pathways. In one route (the arogenate pathway), prephenate is first transaminated to L-arogenate followed by dehydration/decarboxylation to Phe or dehydrogenation/decarboxylation to Tyr. In the other route (the phenylpyruvate or 4-hydroxyphenylpyruvate pathway), these reactions occur in reverse order. Recent genetic evidence indicates that the arogenate pathway is the predominant route for Phe biosynthesis in plants.
Synthesis and evaluation of antimicrobial, antitubercular and anticancer activities of benzimidazole derivatives
Published in Egyptian Journal of Basic and Applied Sciences, 2018
Snehlata Yadav, Balasubramanian Narasimhan, Siong Meng Lim, Kalavathy Ramasamy, Mani Vasudevan, Syed Adnan Ali Shah, Abhishek Mathur
The results of mycobacterial enzyme assays were expressed in terms of percent inhibition of mycobacterial enzymes i.e., isocitrate lyase, chorismate mutase and pantothenate synthetase, by the mycobacterium. The inhibition of the enzyme activity by the tested compounds was less than that of streptomycin sulphate used as positive control (Table 5). Compound 19 emerged as the best compound that inhibited the mycobacterial isocitrate lyase, pantothenate synthetase and chorismate mutase to 67.56%, 53.45% and 47.56% respectively which was comparable to inhibition of 75.12%, 77.06%, and 79.56%, respectively by streptomycin sulphate.