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Engineering methionine γ-lyase from Citrobacter freundii for anticancer activity.

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Methionine deprivation therapy for cancer shows promise. Researchers engineered methionine gamma-lyase (MGL) variants, with V358Y demonstrating enhanced cytotoxic activity against cancer cells, offering a potential new therapeutic strategy.

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Cancer therapyCytotoxicity activityMethionine depletionProtein engineeringPyridoxal 5′-phosphate dependent enzymeSite-saturation mutagenesis

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Area of Science:

  • Biochemistry
  • Enzymology
  • Cancer Therapeutics

Background:

  • Cancer cells often lack methionine biosynthesis, making them vulnerable to methionine deprivation.
  • Methionine gamma-lyase (MGL) degrades methionine, offering a strategy to reduce its availability to cancer cells.

Purpose of the Study:

  • To enhance the catalytic activity of MGL for improved cancer therapy.
  • To investigate the role of the C-terminal flexible loop in MGL activity and allosteric regulation.

Main Methods:

  • Sequence and structure conservation analysis of MGLs.
  • Site-saturation mutagenesis of the C-terminal flexible loop (P357, V358, P360, A366) in Citrobacter freundii MGL.
  • Screening of mutant libraries for enzyme activity and cytotoxic effects.
  • 3D-structure comparison of wild-type and mutant MGLs.

Main Results:

  • Mutagenesis identified active variants, including V358Y MGL with a 1.9-fold increased catalytic rate.
  • V358Y MGL exhibited lower IC50 values against cancer cell lines compared to wild-type MGL.
  • Structural analysis revealed C-terminal loop flexibility but indicated mutations allosterically affect catalysis.

Conclusions:

  • Engineering MGL, particularly at the V358 position, can enhance its cytotoxic potential against cancer cells.
  • The C-terminal flexible loop plays a crucial role in MGL's allosteric regulation and catalytic efficiency.
  • Modified MGL holds promise as a targeted cancer therapeutic strategy by exploiting methionine dependency.