scholarly journals Inhibitory Activity of Proanthocyanidins Against Escherichia coli 1-Deoxy-D-Xylulose-5-Phosphate Reductoisomerase

2021 ◽  
Vol 16 (11) ◽  
pp. 1934578X2110564
Author(s):  
Xian Hui ◽  
Bo-Rong Zhu ◽  
Long-Long Wu ◽  
Wen-Yun Gao ◽  
Yi-Ming Li ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Moderate Activity ◽  
Terpenoid Biosynthesis ◽  
Inhibitory Effects ◽  
Methylerythritol Phosphate Pathway ◽  
Methylerythritol Phosphate ◽  
Structure Activity ◽  
Initial Characterization ◽  
Key Enzyme ◽  
Relationship Of

1-Deoxy-D-xylulose 5-phosphate reductoisomerase (DXR) is a key enzyme in the methylerythritol phosphate pathway for terpenoid biosynthesis. Furthermore, it is an ideal target for the screening of novel antibiotics because it is present in causative organisms, but absent from humans. To identify more lipophilic DXR inhibitors from natural resources, we tested the DXR inhibitory activity of five proanthocyanidins in this study. The results indicated that all these compounds specifically restrained the activity of DXR, with procyanid B2 exhibiting a relatively low effect against DXR (IC50 ∼ 305 μM) and procyanid C1 displaying moderate activity (IC50 75.1 μM). The other three compounds cinnamtannin A2, cinnamtannin B1, and cinnamtannin D1 (IC50 ∼ 89.3, 105.0, and 97.8 μM, respectively) showed DXR inhibitory effects that were slightly weaker than that of procyanid C1. In addition, based on the initial characterization, the structure–activity relationship of this series of compounds against DXR is discussed.

scholarly journals Overexpression of PtDXS Enhances Stress Resistance in Poplars

2019 ◽  
Vol 20 (7) ◽  
pp. 1669 ◽  
Author(s):  
Hui Wei ◽  
Ali Movahedi ◽  
Chen Xu ◽  
Weibo Sun ◽  
Amir Almasi Zadeh Yaghuti ◽  
...  
Keyword(s):  
Populus Trichocarpa ◽  
Terpenoid Biosynthesis ◽  
Functional Protein ◽  
Methylerythritol Phosphate Pathway ◽  
E Coli ◽  
Methylerythritol Phosphate ◽  
Transgenic Lines ◽  
Key Enzyme ◽  
Young Leaves ◽  
Rate Limiting

1-Deoxy-d-xylulose-5-phosphate synthase (DXS) is the rate-limiting enzyme in the plastidial methylerythritol phosphate pathway (MEP). In this study, PtDXS (XM_024607716.1) was isolated from Populus trichocarpa. A bioinformatics analysis revealed that PtDXS had high homology with the DXSs of other plant species. PtDXS expression differed among plant tissues and was highest in young leaves and lowest in roots. The recombinant protein was produced in Escherichia coli BL21 (DE3), purified, and its activity evaluated. The purified protein was capable of catalyzing the formation of 1-deoxy-d-xylulose-5-phosphate (DXP) from glyceraldehyde-3-phosphate and pyruvate. A functional color assay in E. coli harboring pAC-BETA indicated that PtDXS encodes a functional protein involved in the biosynthesis of isoprenoid precursors. The treatment of P. trichocarpa seedlings with 200 μM abscisic acid (ABA), 200 mM NaCl, 10% polyethylene glycol6000, and 2 mM H2O2 resulted in increased expression of PtDXS. The ABA and gibberellic acid contents of the transgenic lines (Poplar Nanlin 895) were higher than wild types, suggesting that DXS is important in terpenoid biosynthesis. Overexpression of PtDXS enhanced resistance to S. populiperda infection. Furthermore, the transgenic lines showed decreased feeding by Micromelalopha troglodyta, supporting the notion that PtDXS is a key enzyme in terpenoid biosynthesis.

Structure-activity relationship of the inhibitory effects of flavonoids on nitric oxide production in RAW264.7 cells

2017 ◽  
Vol 25 (2) ◽  
pp. 779-788 ◽  
Author(s):  
Wen-Jun Jiang ◽  
Akihiro Daikonya ◽  
Mitsuyoshi Ohkawara ◽  
Takashi Nemoto ◽  
Ryusuke Noritake ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
Raw264.7 Cells ◽  
Nitric Oxide Production ◽  
Inhibitory Effects ◽  
Oxide Production ◽  
Structure Activity ◽  
Relationship Of

Combined 3D-quantitative structure–activity relationships and topomer technology-based molecular design of human 4-hydroxyphenylpyruvate dioxygenase inhibitors

2020 ◽  
Vol 12 (9) ◽  
pp. 795-811 ◽  
Author(s):  
Yong-Xuan Liu ◽  
Shuang Gao ◽  
Tong Ye ◽  
Jia-Zhong Li ◽  
Fei Ye ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Binding Free Energy ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
Type I ◽  
Quantitative Structure ◽  
Structure Activity Relationships ◽  
Structure Activity ◽  
Quantitative Structure Activity Relationships ◽  
Relationship Of

Aim: 4-Hydroxyphenylpyruvate dioxygenase (HPPD) has attracted increasing attention as an important target against tyrosinemia type I. This paper aimed to explore the structure–activity relationship of HPPD inhibitors with pyrazole scaffolds and to design novel HPPD inhibitors. Methodology & results: The best 3D-quantitative structure–activity relationships model was established by two different strategies based on 40 pyrazole scaffold-based analogs. Screening of molecular fragments by topomer technology, combined with molecular docking, 14 structures were identified for potential human HPPD inhibitory activity. Molecular dynamics results demonstrated that all the compounds obtained bound to the enzyme and possessed a satisfactory binding free energy. Conclusion: The quantitative structure–activity relationship of HPPD inhibitors of pyrazole scaffolds was clarified and 14 original structures with potential human HPPD inhibitory activity were obtained.

Quantitative Structure-Activity Relationship of Substituted Benzoquinones as Inhibitors of Photosynthetic Electron Transport

1978 ◽  
Vol 33 (9-10) ◽  
pp. 695-703 ◽  
Author(s):  
Walter Oettmeier ◽  
Susanne Reimer ◽  
Klaus Link
Keyword(s):  
Inhibitory Activity ◽  
Electron Flow ◽  
Photosynthetic Electron Transport ◽  
Quantitative Structure Activity Relationship ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
Quantitative Structure ◽  
Structure Activity ◽  
Alkyl Side Chains ◽  
Relationship Of

Abstract 1.4-benzoquinones have been tested for their inhibitory activity on photosynthetic NADP+ reduction by chloroplasts. Benzoquinones with one or two branched alkyl side chains are inhibitors of electron flow. Inhibitory activity can be highly increased if one - and even more if two - halogen substitutents are introduced into the quinone moiety. Iodine substitution yields a better inhibitor than bromine than chlorine. A quantitative structure activity relationship according to a bilinear model, as developed by Kubinyi, with the lipophilicity as the only parameter could be established.

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