Selenocysteine lyase

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In enzymology, a selenocysteine lyase (EC 4.4.1.16) is an enzyme that catalyzes the chemical reaction

L-selenocysteine + reduced acceptor $\rightleftharpoons$ selenide + L-alanine + acceptor

Thus, the two substrates of this enzyme are L-selenocysteine and reduced acceptor, whereas its 3 products are selenide, L-alanine, and acceptor.

This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is L-selenocysteine selenide-lyase (L-alanine-forming). Other names in common use include selenocysteine reductase, and selenocysteine beta-lyase. 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, 4 structures have been solved for this class of enzymes, with PDB accession codes 1I29, 1JF9, 1KMJ, and 1KMK.

[edit] References

IUBMB entry for 4.4.1.16
BRENDA references for 4.4.1.16 (Recommended.)
PubMed references for 4.4.1.16
PubMed Central references for 4.4.1.16
Google Scholar references for 4.4.1.16
Esaki N, Nakamura T, Tanaka H, Soda K (1982). "Selenocysteine lyase, a novel enzyme that specifically acts on selenocysteine. Mammalian distribution and purification and properties of pig liver enzyme". J. Biol. Chem. 257: 4386–91. PMID 6461656.