Recombinant L-methionine gamma-lyase Active protein (mutated F47L + D172E + S308Y)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

L-methionine gamma-lyase also known as methionine gamma-lyase is an enzyme primarily involved in the deamination of L-methionine to produce α-ketobutyrate ammonia and thiol. This enzyme is particularly notable in that it can also degrade S-methyl-L-cysteine and homocysteine therefore playing a role in sulfur amino acid metabolism. L-methionine gamma-lyase has an approximate molecular weight of 172 kDa depending on the organism and is expressed mostly in bacteria such as Pseudomonas putida but not in humans.

Biological function summary

L-methionine gamma-lyase contributes to the metabolism of sulfur-containing amino acids. It is not typically part of a complex but operates independently to catalyze reactions involving L-methionine transforming it into useful metabolites that organisms like bacteria can utilize effectively. Its activity influences intracellular levels of methionine and sulfur compounds which can affect various biochemical processes including oxidative stress responses and regulation of cellular homeostasis.

Pathways

Sulfur amino acid metabolism relies significantly on L-methionine gamma-lyase. This enzyme influences the transsulfuration pathway through which methionine is ultimately converted into cysteine. It interplays with enzymes such as cystathionine gamma-lyase within this pathway. Furthermore its action links methionine metabolism to the broader context of the one-carbon metabolism pathway important for the synthesis of nucleotides and methylation reactions necessary for cell proliferation and gene expression.

Researchers have explored L-methionine gamma-lyase as a potential target in cancer therapy due to its ability to affect methionine metabolism important for some tumor growths reliant on high methionine levels. Its activity may also be relevant in bacterial infections where this enzyme's presence in pathogenic bacteria highlights a potential target for antibiotic development. L-methionine gamma-lyase's interaction with human methionine metabolism-related proteins while indirect can significantly impact cellular pathways altered in disease contexts.