Cystathionine gamma-synthase from Arabidopsis thaliana: purification and biochemical characterization of the recombinant enzyme overexpressed in Escherichia coli.

@article{Ravanel1998CystathionineGF,
  title={Cystathionine gamma-synthase from Arabidopsis thaliana: purification and biochemical characterization of the recombinant enzyme overexpressed in Escherichia coli.},
  author={St{\'e}phane Ravanel and Bertrand Gaki{\`e}re and D Job and Roland Douce},
  journal={The Biochemical journal},
  year={1998},
  volume={331 ( Pt 2)},
  pages={639-48}
}
Cystathionine gamma-synthase catalyses the first reaction specific for methionine biosynthesis in plants, the gamma-replacement of the phosphoryl substituent of O-phosphohomoserine by cysteine. A cDNA encoding cystathionine gamma-synthase from Arabidopsis thaliana has been cloned and used to overexpress the enzyme in Escherichia coli. The native recombinant enzyme is a homotetramer composed of 53 kDa subunits, each being tightly associated with one molecule of pyridoxal 5'-phosphate that binds… CONTINUE READING
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Methods Enzymol

  • A. H. Datko, S. H. Mudd
  • Plant Physiol
  • 1984

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