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EC Tree
IUBMB Comments A pyridoxal-phosphate protein. Dithiothreitol or 2-sulfanylethan-1-ol (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) .
The taxonomic range for the selected organisms is: Mus musculus The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
scl, selenocysteine lyase, selenocysteine beta-lyase, sec lyase, aba3-nifs,
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selenocysteine beta-lyase
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selenocysteine reductase
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SCL
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alpha,beta-elimination
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elimination of H2Se
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cleavage of C-Se bond
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elimination of SO2
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oxidative elimination of NH3
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elimination of chloride
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L-selenocysteine selenide-lyase (L-alanine-forming)
A pyridoxal-phosphate protein. Dithiothreitol or 2-sulfanylethan-1-ol (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].
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L-cysteine sulfinic acid + reduced acceptor
SO2 + L-alanine + acceptor
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
additional information
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L-cysteine sulfinic acid + reduced acceptor
SO2 + L-alanine + acceptor
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L-cysteine sulfinic acid + reduced acceptor
SO2 + L-alanine + acceptor
less than 10% of activity
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L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
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L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
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L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
probably functions as selenide delivery system
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L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
most likely metabolizes small amounts of selenocysteine in tissue
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?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
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L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
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L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
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L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
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additional information
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traces of activity with L-cysteine
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additional information
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traces of activity with L-cysteine
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additional information
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traces of activity with L-cysteine
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additional information
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traces of activity with L-cysteine
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additional information
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the enzyme is specific for L-selenocysteine versus L-cysteine on a molecular level, no activity with L-cysteine
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L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
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?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
probably functions as selenide delivery system
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L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
most likely metabolizes small amounts of selenocysteine in tissue
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L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
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L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
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L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
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L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
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?
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pyridoxal 5'-phosphate
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required
pyridoxal 5'-phosphate
required
pyridoxal 5'-phosphate
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required
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hydroxylamine
almost completely reversible by dialysis against pyridoxal 5'-phosphate
major urinary protein 1
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about 60% remaining relative enzyme activity
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major urinary protein 2
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about 60% remaining relative enzyme activity
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8.6
L-cysteine sulfinate
pH 9.0, 37°C
8.6
L-cysteine sulfinate
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pH 9.0, 37°C
9.9
L-selenocysteine
pH 9.0, 37°C
9.9
L-selenocysteine
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pH 9.0, 37°C
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0.35
L-cysteine sulfinate
0.35
L-cysteine sulfinate
pH 9.0, 37°C
0.35
L-cysteine sulfinate
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pH 9.0, 37°C
46
L-selenocysteine
pH 9.0, 37°C
46
L-selenocysteine
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pH 9.0, 37°C
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29
purified enzyme, pH 7.4
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SwissProt
brenda
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low activity
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dominantly in Leydig cells and spermatids
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low enzyme level
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high enzyme content and activity
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the levels of selenocysteine lyase in the stomach of 7 out of 8 mice fed a Se-supplemented diet are markedly lower than those of mice fed a Se-deficient diet
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additional information
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tissue expression pattern, cell-specific expression in kidney and liver, overview
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highest activity
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high expression level in nuclei of renal proximal tubules, less in distal tubules, no expression in glomerulus cells
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highest activity
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malfunction
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disruption of the selenocysteine lyase-mediated selenium recycling pathway leads to metabolic syndrome in mice affecting hepatic glucose and lipid homeostasis. Mice lacking the enzyme and raised on an Se-adequate diet exhibit hyperinsulinemia, hyperleptinemia, glucose intolerance, and hepatic steatosis, with increased hepatic oxidative stress, but maintain selenoprotein levels and circulating Se status. Insulin challenge of enyme KO mice results in attenuated Akt phosphorylation but does not decrease phosphorylation levels of AMP kinase alpha. Upon dietary Se restriction, enzyme KO animals develop several characteristics of metabolic syndrome, such as obesity, fatty liver, and hypercholesterolemia, with aggravated hyperleptinemia, hyperinsulinemia, and glucose intolerance. Hepatic glutathione peroxidase 1 and selenoprotein S production and circulating selenoprotein P levels are significantly diminished. Enzyme disruption increases the levels of insulin-signaling inhibitor insulin signaling inhibitor protein phosphatase 1B
physiological function
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the enzyme is involved in Sec decomposition to salvage Se, e.g. from plasma glutathione peroxidase 3 and Sepp1 proteins, for selenoprotein production. Because insulin signaling inhibitor protein phosphatase 1B expression is regulated by Se levels, it is also possible that the hepatic Se decline in enzyme KO mice is driving the expression of insulin signaling inhibitor protein phosphatase 1B, suggesting that Se derived from Sec decomposition participates in insulin signaling inhibitor protein phosphatase 1B regulation
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SCLY_MOUSE
432
0
47174
Swiss-Prot
other Location (Reliability: 1 )
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105000
gel filtration
47000
SDS-PAGE
47200
calculated from amino acid sequence
47200
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calculated from amino acid sequence
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dimer
2 * 47000, SDS-PAGE
dimer
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2 * 47000, SDS-PAGE
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additional information
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construction of enzyme knockout mice, phenotype, overview
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-80°C, purified enzyme, stable for several weeks
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overexpressed protein
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expressed in Escherichia coli BL21(DE3)
transfection of HepG2, Hepa12-6, Ht22 cells
expressed in Brassica juncea using Agrobacterium tumefaciens to introduce genetic sequence, transformation results in enhanced enzyme activity but decreased Se tolerance
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expressed in chloroplasts and cytosol of Arabidopsis sp., enhanced Se tolerance when enzyme is expressed in cytosol, decreased Se tolerance when expressed in chloroplasts
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recombinant expression of GFP-tagged enzyme in spermatids of mature testes of transgenic mice
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expressed in Escherichia coli BL21(DE3)
expressed in Escherichia coli BL21(DE3)
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expression differs in response to Se levels in a cell type-specific manner. Expression and activity do not correlate with the presence of selenoprotein P
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degradation
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transgenic plants could be used for decontamination of high Se soil or water
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Esaki, N.; Nakamura, T.; Tanaka, H.; Soda, K.
Selenocysteine lyase, a novel enzyme that specifically acts on selenocysteine
J. Biol. Chem.
257
4386-4391
1982
Bos taurus, Canis lupus familiaris, Cavia porcellus, Oryctolagus cuniculus, Felis catus, Platyrrhini, Mus musculus, Rattus norvegicus, Sus scrofa
brenda
Mihara, H.; Kurihara, T.; Watanabe, T.; Yoshimura, T.; Esaki, N.
cDNA cloning, purification, and characterization of mouse liver selenocysteine lyase. Candidate for selenium delivery protein in selenoprotein synthesis
J. Biol. Chem.
275
6195-6200
2000
Sus scrofa, Mus musculus (Q9JLI6), Mus musculus
brenda
Mihara, H.; Esaki, N.
Selenocysteine lyase from mouse liver
Methods Enzymol.
347
198-203
2002
Mus musculus (Q9JLI6), Mus musculus
brenda
Garifullina, G.F.; Owen, J.D.; Lindblom, S.D.; Tufan, H.; Pilon, M.; Pilon-Smits, E.A.H.
Expression of a mouse selenocysteine lyase in Brassica juncea chloroplasts affects selenium tolerance and accumulation
Physiol. Plant.
118
538-544
2003
Mus musculus
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brenda
Pilon, M.; Owen, J.D.; Garifullina, G.F.; Kurihara, T.; Mihara, H.; Esaki, N.; Pilon-Smits, E.A.
Enhanced selenium tolerance and accumulation in transgenic Arabidopsis expressing a mouse selenocysteine lyase
Plant Physiol.
131
1250-1257
2003
Mus musculus
brenda
Kurokawa, S.; Mihara, H.; Kurihara, T.; Esaki, N.
Expression analysis of mammalian selenocysteine lyase
Biomed. Res. Trace Elements
15
278-280
2004
Mus musculus, Mus musculus C57BL/6
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brenda
Tobe, R.; Mihara, H.; Kurihara, T.; Esaki, N.
Identification of proteins interacting with selenocysteine lyase
Biosci. Biotechnol. Biochem.
73
1230-1232
2009
Mus musculus
brenda
Kurokawa, S.; Takehashi, M.; Tanaka, H.; Mihara, H.; Kurihara, T.; Tanaka, S.; Hill, K.; Burk, R.; Esaki, N.
Mammalian selenocysteine lyase is involved in selenoprotein biosynthesis
J. Nutr. Sci. Vitaminol.
57
298-305
2011
Homo sapiens, Mus musculus, Rattus norvegicus, Mus musculus C57/BL6
brenda
Seale, L.A.; Hashimoto, A.C.; Kurokawa, S.; Gilman, C.L.; Seyedali, A.; Bellinger, F.P.; Raman, A.V.; Berry, M.J.
Disruption of the selenocysteine lyase-mediated selenium recycling pathway leads to metabolic syndrome in mice
Mol. Cell. Biol.
32
4141-4154
2012
Mus musculus
brenda
Seale, L.A.; Ha, H.Y.; Hashimoto, A.C.; Berry, M.J.
Relationship between selenoprotein P and selenocysteine lyase Insights into selenium metabolism
Free Radic. Biol. Med.
127
182-189
2018
Mus musculus (Q9JLI6)
brenda