Enzymes For Synthesis of 10-Formyltetrahydrofolate in Plants: Characterization of a Monofunctional 10-Formyltetrahydrofolate Synthetase and Copurification of 5,10-Methylenetetrahydrofolate Dehydrogenase and 5,10-Methenyltetrahydrofolate Cyclohydrolase Activities

  • Edwin A. Cossins
  • Carole D. Kirk
  • Helena C. Imeson
  • Li-li Zheng
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 338)


Plants require folates for the biosynthesis of purines, serine, methionine, formylmethionyl-tRNA and thymidylate (1). In leaves, mitochondrial folates mediate glycine cleavage and serine formation during photorespiration (2). Plants also have enzymes (1,3) that interconvert methylene-and formyltetrahydrofolates. Alternatively, these species generate 10-HCO-H4PteGlu from formate (1). Recent work from Rabinowitz’s laboratory (4,5) on the latter reaction in spinach leaves, identified a monofunctional 10-HCO-H4PteGlu synthetase protein whose primary structure is like the synthetase domain of the mammalian and yeast trifunctional Cl-THF synthase. Partial purification of the related dehydrogenase and cyclohydrolase activities suggested they may occur as a bifunctional complex in spinach leaves (4). However, it is not clear whether this structural organization is typical of higher plants in general or may reflect a possible chloroplastic origin.


Spinach Leave Streptomycin Sulphate Synthetase Protein High Plant Tissue Trifunctional Enzyme 
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Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • Edwin A. Cossins
    • 1
  • Carole D. Kirk
    • 1
  • Helena C. Imeson
    • 2
  • Li-li Zheng
    • 3
  1. 1.Department of BotanyUniversity of AlbertaEdmontonCanada
  2. 2.Department of BiologyUniversity of LethbridgeLethbridgeCanada
  3. 3.Department of HorticultureXiongyue Agricultural CollegeXiongyueThe People’s Republic of China

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