scholarly journals Study of IspH, a Key Enzyme in the Methylerythritol Phosphate Pathway Using Fluoro-Substituted Substrate Analogues

2011 ◽  
Vol 13 (21) ◽  
pp. 5912-5915 ◽  
Author(s):  
Youli Xiao ◽  
Wei-chen Chang ◽  
Hung-wen Liu ◽  
Pinghua Liu
2019 ◽  
Vol 20 (7) ◽  
pp. 1669 ◽  
Author(s):  
Hui Wei ◽  
Ali Movahedi ◽  
Chen Xu ◽  
Weibo Sun ◽  
Amir Almasi Zadeh Yaghuti ◽  
...  

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.


2021 ◽  
Vol 16 (11) ◽  
pp. 1934578X2110564
Author(s):  
Xian Hui ◽  
Bo-Rong Zhu ◽  
Long-Long Wu ◽  
Wen-Yun Gao ◽  
Yi-Ming Li ◽  
...  

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.


2007 ◽  
Vol 65 (1-2) ◽  
pp. 177-187 ◽  
Author(s):  
Atsushi Okada ◽  
Takafumi Shimizu ◽  
Kazunori Okada ◽  
Tomohisa Kuzuyama ◽  
Jinichiro Koga ◽  
...  

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