Selenocysteine lyase
| selenocysteine lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.4.1.16 | ||||||||
| CAS no. | 82047-76-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a selenocysteine lyase (EC 4.4.1.16) is an enzyme that catalyzes the chemical reaction
- L-selenocysteine + reduced acceptor 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.
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.
References
- 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 (8): 4386–91. PMID 6461656.
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