An insilico approach to structural elucidation of 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase from Arabidopsis thaliana: Hints for herbicide design

2012 ◽  
Vol 73 ◽  
pp. 7-14 ◽  
Author(s):  
Sushmita Bhattacharya ◽  
Pravindra Kumar
Keyword(s):  
Arabidopsis Thaliana ◽  
Structural Elucidation ◽  
Phosphate Synthase

The trehalose-6-phosphate synthase TPS5 negatively regulates ABA signaling in Arabidopsis thaliana

2019 ◽  
Vol 38 (8) ◽  
pp. 869-882 ◽  
Author(s):  
Lianfu Tian ◽  
Zijing Xie ◽  
Changqing Lu ◽  
Xiaohua Hao ◽  
Sha Wu ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Aba Signaling ◽  
Phosphate Synthase

Electroporation of maize embryogenic calli with the trehalose-6-phosphate synthase gene from Arabidopsis thaliana

2007 ◽  
Vol 29 (3) ◽  
pp. 273-281 ◽  
Author(s):  
André M. Almeida ◽  
Enrique Villalobos ◽  
Susana S. Araújo ◽  
Luis A. Cardoso ◽  
Dulce M. Santos ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Embryogenic Calli ◽  
Phosphate Synthase

scholarly journals Functional and biochemical characterization of a recombinant Arabidopsis thaliana 3-deoxy-D-manno-octulosonate 8-phosphate synthase

2004 ◽  
Vol 381 (1) ◽  
pp. 185-193 ◽  
Author(s):  
Jing WU ◽  
Mayur A. PATEL ◽  
Appavu K. SUNDARAM ◽  
Ronald W. WOODARD
Keyword(s):  
Arabidopsis Thaliana ◽  
Molecular Mass ◽  
Biochemical Characterization ◽  
Dipicolinic Acid ◽  
Kinetic Studies ◽  
Maximum Activity ◽  
Reading Frame ◽  
Sequential Mechanism ◽  
Phosphate Synthase

An open reading frame, encoding for KDOPS (3-deoxy-D-manno-octulosonate 8-phosphate synthase), from Arabidopsis thaliana was cloned into a T7-driven expression vector. The protein was overexpressed in Escherichia coli and purified to homogeneity. Recombinant A. thaliana KDOPS, in solution, displays an apparent molecular mass of 76 kDa and a subunit molecular mass of 31.519 kDa. Unlike previously studied bacterial KDOPSs, which are tetrameric, A. thaliana KDOPS appears to be a dimer in solution. The optimum temperature of the enzyme is 65 °C and the optimum pH is 7.5, with a broad peak between pH 6.5 and 9.5 showing 90% of maximum activity. The enzyme cannot be inactivated by EDTA or dipicolinic acid treatment, nor it can be activated by a series of bivalent metal ions, suggesting that it is a non-metallo-enzyme, as opposed to the initial prediction that it would be a metallo-enzyme. Kinetic studies showed that the enzyme follows a sequential mechanism with Km=3.6 μM for phosphoenolpyruvate and 3.8 μM for D-arabinose 5-phosphate and kcat=5.9 s−1 at 37 °C. On the basis of the characterization of A. thaliana KDOPS and phylogenetic analysis, plant KDOPSs may represent a new, distinct class of KDOPSs.

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