Regulation of Glycine Decarboxylase and l-Serine Hydroxymethyltransferase Activities by Glyoxylate in Tobacco Leaf Mitochondrial Preparations.

@article{Peterson1982RegulationOG,
  title={Regulation of Glycine Decarboxylase and l-Serine Hydroxymethyltransferase Activities by Glyoxylate in Tobacco Leaf Mitochondrial Preparations.},
  author={Richard B Peterson},
  journal={Plant physiology},
  year={1982},
  volume={70 1},
  pages={61-6}
}
Glyoxylate at a concentration of 10 millimolar caused 50% inhibition of decarboxylation of 20 millimolar [1-(14)C]glycine and accompanying synthesis of serine in a mitochondria-enriched preparation from tobacco (Nicotiana tabacum var. John Williams Broadleaf) leaves. None of the other compounds tested including formate, acetate, oxalate, aspartate, and glutamate appreciably affected activity. Occasional inhibition produced by glycolate may have resulted from residual glycolate oxidase in these… CONTINUE READING

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