Methionine gamma-lyase

From Wikipedia, the free encyclopedia

In enzymology, a methionine gamma-lyase (EC 4.4.1.11) is an enzyme that catalyzes the chemical reaction

L-methionine + H₂O $\rightleftharpoons$ methanethiol + NH₃ + 2-oxobutanoate

Thus, the two substrates of this enzyme are L-methionine and H₂O, whereas its 3 products are methanethiol, NH₃, and 2-oxobutanoate.

This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is L-methionine methanethiol-lyase (deaminating 2-oxobutanoate-forming). Other names in common use include L-methioninase, methionine lyase, methioninase, methionine dethiomethylase, L-methionine gamma-lyase, and L-methionine methanethiol-lyase (deaminating). This enzyme participates in selenoamino acid metabolism. It employs one cofactor, pyridoxal phosphate.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1E5E, 1E5F, 1GC0, 1GC2, 1PFF, 1PG8, 1UKJ, and 1Y4I.