EC 4.4.1.16 - Selenocysteine lyase

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IntEnz Enzyme Nomenclature
EC 4.4.1.16

Names

Accepted name:
selenocysteine lyase
Other names:
selenocysteine β-lyase
selenocysteine reductase
Systematic name:
L-selenocysteine selenide-lyase (L-alanine-forming)

Reaction

Cofactor

Comments:

A pyridoxal-phosphate protein. Dithiothreitol or 2-mercaptoethanol can act as the reducing agent in the reaction. The enzyme from animals does not act on cysteine, serine or chloroalanine [1,3], while the enzyme from bacteria shows activity with cysteine (cf. EC 2.8.1.7, cysteine desulfurase) [2].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0009000
UniProtKB/Swiss-Prot: (67) [show] [UniProt]

References

  1. Esaki, N., Nakamura, T., Tanaka, H. and Soda, K.
    Selenocysteine lyase, a novel enzyme that specifically acts on selenocysteine. Mammalian distribution and purification and properties of pig liver enzyme.
    J. Biol. Chem. 257: 4386-4391 (1982). [PMID: 6461656]
  2. Mihara, H., Kurihara, T., Yoshimura, T., Soda, K., Esaki, N.
    Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. Gene cloning, purification, and characterization of a novel pyridoxal enzyme.
    J. Biol. Chem. 272: 22417-22424 (1997). [PMID: 9278392]
  3. Omi, R., Kurokawa, S., Mihara, H., Hayashi, H., Goto, M., Miyahara, I., Kurihara, T., Hirotsu, K., Esaki, N.
    Reaction mechanism and molecular basis for selenium/sulfur discrimination of selenocysteine lyase.
    J. Biol. Chem. 285: 12133-12139 (2010). [PMID: 20164179]

[EC 4.4.1.16 created 1986]