Biochemical properties and applications of L-Methionine γ-Lyase

Elsayed, Ashraf; Shindia, Ahmed; Emam, Esraa

doi:10.21608/bfszu.2024.334906.1443

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	Biochemical properties and applications of L-Methionine γ-Lyase
Article 20, Volume 2025, Issue 2, June 2025, Page 242-252 PDF (672.66 K)
Document Type: Original Article
DOI: 10.21608/bfszu.2024.334906.1443
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Authors
Ashraf Elsayed ; Ahmed Shindia¹; Esraa Emam²
¹Botany and Microbiology Department, Faculty of Science, Zagazig University, Egypt
²Botany and Microbiology Department, Faculty of Science, Zagazig University
Abstract
Methionine γ-lyase (MGL) is a pyridoxal-5-phosphate (PLP)-dependent enzyme with the ability to selectively target and inhibit the growth of cancer cells than the normal ones. Tumor cells often exhibit altered metabolic pathways compared to normal cells, due to the down-regulation or loss of methionine synthase that is crucial for converting homocysteine to methionine. Methionine serves as a building block for proteins, plays a role in various metabolic processes, including protein synthesis, cell growth, and DNA methylation. Normal cells primarily rely on methionine synthesized within the cell for their needs. Unlike normal cells, the tumor cells lack methionine synthase and depend on external L-methionine from the diet. While the exact mechanisms are still being investigated, tumor cells often exhibit altered metabolic pathways. They might have reduced methionine synthase activity or rely more heavily on external methionine sources for survival and proliferation. Thus, the objective of this review was to shed-light about biochemical features, molecular properties of this enzyme from different microbial sources.
Keywords
Methionine γ-lyase; Sources; Biochemical properties
Main Subjects
Basic and applied research of Microbiology


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