A review on L-methioninase in cancer therapy: Precision targeting, advancements and diverse applications for a promising future

Int J Biol Macromol. 2024 Apr;265(Pt 2):130997. doi: 10.1016/j.ijbiomac.2024.130997. Epub 2024 Mar 19.

Abstract

Cancer remains a global health challenge, demanding novel therapeutic options due to the debilitating side effects of conventional treatments on healthy tissues. The review highlights the potential of L-methioninase, a pyridoxal-5-phosphate (PLP)-dependent enzyme, as a promising avenue in alternative cancer therapy. L-methioninase offers a unique advantage, its ability to selectively target and inhibit the growth of cancer cells without harming healthy cells. This selectivity arises because tumor cells lack an essential enzyme called methionine synthase, which healthy cells use to make the vital amino acid L-methionine. Several sources harbor L-methioninase, including bacteria, fungi, plants, and protozoa. Future research efforts can explore and exploit this diverse range of sources to improve the therapeutic potential of L-methioninase in the fight against cancer. Despite challenges, research actively explores microbial L-methioninase for its anticancer potential. This review examines the enzyme's side effects, advancements in combination therapies, recombinant technologies, polymer conjugation and novel delivery methods like nanoparticles, while highlighting the success of oral administration in preclinical trials. Beyond its promising role in cancer therapy, L-methioninase holds potential applications in food science, antioxidants, and various health concerns like diabetes, cardiovascular issues, and neurodegenerative diseases. This review provides a piece of current knowledge and future prospects of L-methioninase, exploring its diverse therapeutic potential.

Keywords: L-methioninase; Methionine synthase; Preclinical trials; Therapeutic.

Publication types

  • Review

MeSH terms

  • Carbon-Sulfur Lyases* / metabolism
  • Combined Modality Therapy
  • Fungi / metabolism
  • Humans
  • Methionine / metabolism
  • Neoplasms* / drug therapy
  • Recombinant Proteins / therapeutic use

Substances

  • L-methionine gamma-lyase
  • Carbon-Sulfur Lyases
  • Methionine
  • Recombinant Proteins