Chemo-enzymatic synthesis of optically pure l-leucovorin, an augmentor of 5-fluorouracil cytotoxicity against cancer

Biochem Biophys Res Commun. 1990 Sep 14;171(2):684-9. doi: 10.1016/0006-291x(90)91200-c.

Abstract

Optically pure l-leucovorin was synthesized on a large scale by the combination of chemical and enzymatic processes. After reduction of folate with zinc, dihydrofolate was reduced asymmetrically to (6)-tetra-hydrofolate by use of dihydrofolate reductase from E. coli C600/pTP600, with simultaneous NADPH cofactor recycling using glucose dehydrogenase from Gluconobacter scleroideus KY3613. Calcium l-leucovorin.4H2O (113 g) was obtained from (6S)-tetrahydrofolate via 5,10-methyenyltetrahydrofolate by formylation, reflux, addition of calcium ions and floricil column chromatography, with an overall yield of 50% based on folate. The l-leucovorin showed optical purity of 99.9% de as (6S)-form.

MeSH terms

  • Escherichia coli / enzymology
  • Escherichia coli / genetics
  • Fluorouracil / therapeutic use
  • Fluorouracil / toxicity*
  • Isomerism
  • Leucovorin / chemical synthesis*
  • Leucovorin / therapeutic use
  • NAD / metabolism
  • Neoplasms / drug therapy
  • Oxidation-Reduction
  • Plasmids
  • Promoter Regions, Genetic
  • Tetrahydrofolate Dehydrogenase / genetics
  • Tetrahydrofolate Dehydrogenase / isolation & purification
  • Tetrahydrofolate Dehydrogenase / metabolism

Substances

  • NAD
  • Tetrahydrofolate Dehydrogenase
  • Leucovorin
  • Fluorouracil