Activities | Families | Sequences | Fold types | References | Help
B6db activities:
Description Selenocysteine lyase
Alternative names Selenocysteine reductase;
Selenocysteine beta-lyase.
Catalyzed reaction L-selenocysteine + reduced acceptor = hydrogen selenide + L-alanine + acceptor.
Cofactor Pyridoxal-phosphate.
Comments -!- Dithiothreitol or 2-mercaptoethanol can act as reducing agent in the reaction.
-!- Does not act on cysteine, serine or chloroalanine.
Selenocysteine lyase enzymes have been considered as candidates for the control of free selenium levels in vivo.
These enzymes are phylogenetically related to cysteine desulfurases (EC, and often show some cysteine desulfurase activity.
In addition to the eubacterial/plant enzyme lineage (here included in family and to the distinct metazoan lineage (family a third, a very peculiar subgroup of selenocysteine lyases might occur in archaea.
Organisms -Eubacteria -Plants -Metazoa -Human

Family (28) (12)
Links Enzyme (activities)
BRENDA (activities)
KEGG (pathways)
PLPMDB (PLP mutants)
 Seale LA (2019) Selenocysteine β-Lyase: Biochemistry, Regulation and Physiological Role of the Selenocysteine Decomposition Enzyme Antioxidants (Basel) 8 pii: E357.

 Zafrilla B, Martínez-Espinosa RM, Esclapez J, Pérez-Pomares F, Bonete MJ. (2010) SufS protein from Haloferax volcanii involved in Fe-S cluster assembly in haloarchaea Biochim Biophys Acta 1804 1476-82 .

 Stadtman T. (2004) Methanococcus vannielii selenium metabolism: purification and N-terminal amino acid sequences of a novel selenium-binding protein and selenocysteine lyase IUBMB Life 56 427-31.

 Pilon-Smits EA, Garifullina GF, Abdel-Ghany S, Kato S, Mihara, H., Hale, K.L., Burkhead, J.L., Esaki, N., Kurihara, T., Pilon, M. (2002) Characterization of a NifS-like chloroplast protein from Arabidopsis. Implications for its role in sulfur and selenium metabolism Plant Physiol 130 1309-18.

 Fujii, T.; Maeda, M.; Mihara, H.; Kurihara, T.; Esaki, N.; Hata, Y. (2000) Structure of a NifS homologue: X-ray structure analysis of CsdB, an Escherichia coli counterpart of mammalian selenocysteine lyase Biochemistry 39 1263-73.

 Mihara, H.; Kurihara, T.; Watanabe, T.; Yoshimura, T.; Esaki, N. (2000) cDNA cloning, purification, and characterization of mouse liver selenocysteine lyase. Candidate for selenium delivery protein in selenoprotein synthesis J Biol Chem 275 6195-200.

 Mihara, H.; Maeda, M.; Fujii, T.; Kurihara, T.; Hata, Y.; Esaki, N. (1999) A nifS-like gene, csdB, encodes an Escherichia coli counterpart of mammalian selenocysteine lyase. Gene cloning, purification, characterization and preliminary x-ray crystallographic studies J Biol Chem 274 14768-72.

 Mihara, H.; Kurihara, T.; Yoshimura, T.; Soda, K.; Esaki, N. (1997) 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 22417-24.

Articles on
last changed 2019/06/20 13:35

B6db activities