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Information on EC 4.4.1.16 - selenocysteine lyase and Organism(s) Mus musculus and UniProt Accession Q9JLI6

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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) .
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This record set is specific for:
Mus musculus
UNIPROT: Q9JLI6
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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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Scly
-
-
selenocysteine beta-lyase
-
-
-
-
selenocysteine lyase
-
-
selenocysteine reductase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha,beta-elimination
-
-
-
-
elimination of H2Se
-
-
-
-
cleavage of C-Se bond
-
-
-
-
elimination of SO2
-
-
-
-
oxidative elimination of NH3
-
-
-
-
elimination of chloride
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
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].
CAS REGISTRY NUMBER
COMMENTARY hide
82047-76-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-cysteine sulfinic acid + reduced acceptor
SO2 + L-alanine + acceptor
show the reaction diagram
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
show the reaction diagram
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
show the reaction diagram
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
hydroxylamine
almost completely reversible by dialysis against pyridoxal 5'-phosphate
NaBH4
irreversible
major urinary protein 1
-
about 60% remaining relative enzyme activity
-
major urinary protein 2
-
about 60% remaining relative enzyme activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.6
L-cysteine sulfinate
9.9
L-selenocysteine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.35
L-cysteine sulfinate
46
L-selenocysteine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29
purified enzyme, pH 7.4
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
low activity
Manually annotated by BRENDA team
-
dominantly in Leydig cells and spermatids
Manually annotated by BRENDA team
-
low enzyme level
Manually annotated by BRENDA team
-
high enzyme content and activity
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
additional information
-
tissue expression pattern, cell-specific expression in kidney and liver, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
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
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SCLY_MOUSE
432
0
47174
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
105000
47000
47200
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
construction of enzyme knockout mice, phenotype, overview
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, purified enzyme, stable for several weeks
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpressed protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
expressed in chloroplasts and cytosol of Arabidopsis sp., enhanced Se tolerance when enzyme is expressed in cytosol, decreased Se tolerance when expressed in chloroplasts
-
recombinant expression of GFP-tagged enzyme in spermatids of mature testes of transgenic mice
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation
-
transgenic plants could be used for decontamination of high Se soil or water
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Mihara, H.; Esaki, N.
Selenocysteine lyase from mouse liver
Methods Enzymol.
347
198-203
2002
Mus musculus (Q9JLI6), Mus musculus
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
Tobe, R.; Mihara, H.; Kurihara, T.; Esaki, N.
Identification of proteins interacting with selenocysteine lyase
Biosci. Biotechnol. Biochem.
73
1230-1232
2009
Mus musculus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team