Homologous Modeling of Transketolase AtTKL1 and Its Combination with α-Terthienyl in Arabidopsis Thaliana†

doi:10.7503/cjcu20140934

Abstract

Abstract:

Transketolase is the key enzyme of photosynthesis pathways. It is of great importance for herbicide seeking through new herbicidal substance targeting transketolase. In this study, homologous protein of transketolase was obtained through Modeler and optimized using Amber12, its binding sites of pivotal amino acids were identified with bioinformatics tools. Interaction between AtTKL1 and α-terthienyl finally got verified by spectroscopy and enzyme activity analysis. The three dimensional frame model of transketolase protein AtTKL1 in Arabidopsis thaliana was homologically modeled according to Maize transketolase protein 1ITZ, revised by dynamic molecular methods. With bioinformatics tools, the sites in AtTKL1 were determined, His143, Gly234, Asn263, Arg434, Ser461, Gln488, Phe515, His539, Asp547and Arg598 for binding, His103 and His340 for catalysis. The molecular docking of AtTKL1 and α-terthienyl was performed by computer simulation, and the results confirmed the perfect match of α-terthienyl with active cleavage of AtTKL1. The binding sites His143 and Gly234, and the catalytic sites His103 and His340 were the responsible binding sites of α-terthienyl. Prokaryotic expression of the protein and fluorescence quenching spectroscopy have verified the combination of α-terthienyl and AtTKL1. The reduction on the activity of transketolase treatmented with α-terthienyl gave a further confirmation about the interaction between AtTKL1 and α-terthienyl. The results will contribute to exploiting new efficient and low toxic herbicides.

Key words: Transketolase, α-Terthienyl, Homologous modeling, Molecular docking

CLC Number:

O629.7

TrendMD:

ZHAO Bin, HUO Jingqian, XING Jihong, QI Meng, ZHANG Jinlin, DONG Jingao. Homologous Modeling of Transketolase AtTKL1 and Its Combination with α-Terthienyl in Arabidopsis Thaliana^†[J]. Chem. J. Chinese Universities, 2015, 36(4): 682.

Figures/Tables 2

References 23

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Final concentration/(mg·L^-1)	Max value of fluorescence/a.u.	Enzyme activity/U
20	31.43±0.31	26.07±2.14
40	29.44±0.27	22.50±2.21
60	26.97±0.14	18.31±2.00
80	24.35±0.17	13.93±1.21
100	21.61±0.28	9.16±0.77
120	19.46±0.24	6.43±1.03

Final concentration/(mg·L^-1)	Max value of fluorescence/a.u.	Enzyme activity/U
20	31.43±0.31	26.07±2.14
40	29.44±0.27	22.50±2.21
60	26.97±0.14	18.31±2.00
80	24.35±0.17	13.93±1.21
100	21.61±0.28	9.16±0.77
120	19.46±0.24	6.43±1.03