L-Methionine γ-Lyase, Pseudomonas putida recombinant

Methionine gamma-lyase (EC 4.4.1.11) from Pseudomonas putida is a PLP-dependent enzyme which plays a central role in sulfur amino acid metabolism. METase catalyzes the α, γ-elimination of methionine to α-ketobutyrate, methanethiol, and ammonia. METase also catalyzes the α, γ-elimination of other sulfur containing amino acids, such as homocysteine, cysteine. Because of its ability to deplete methionine, METase has been considered as a viable component of cancer therapeutics against methionine-dependent tumor cells. METase has also been utilized to design drug targets for the infectious diseases caused by parasitic protozoa and anaerobic periodontal bacteria.