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Information on EC 4.4.1.16 - selenocysteine lyase and Organism(s) Rattus norvegicus and UniProt Accession Q68FT9

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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:
Rattus norvegicus
UNIPROT: Q68FT9
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
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
selenocysteine lyase
-
L-selenocysteine selenide-lyase
-
-
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
D-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
L-selenocysteine + reduced acceptor
selenide + L-alanine + acceptor
show the reaction diagram
selenomethionine reduced acceptor
methylselenole + selenide
show the reaction diagram
-
only the 76Se selenomethionine and not 77Se selenomethionine is used as substrate in liver homogenates
-
-
?
additional information
?
-
-
the enzyme is specific for L-selenocysteine versus L-cysteine on a molecular level, no activity with L-cysteine. Residue Cys375 sorts selenium from cysteine and directs it to the active site
-
-
?
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-cysteine
competitive inhibitor
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.6
L-cysteine
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
low activity
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
high activity
Manually annotated by BRENDA team
-
dominantly in Leydig cells and spermatids
Manually annotated by BRENDA team
additional information
-
no activity in fat and blood
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the enzyme is involved in selenocysteine recovering from selenoproteins to be used for synthesis of new selenoproteins
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SCLY_RAT
432
0
47256
Swiss-Prot
other Location (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C375A
mutation on the catalytically essential Cys-375 residue
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli rosetta
expression in Escherichia coli into the pGEM-T Easy vector for sequencing, 5’ constructs with deletions in the promoter region are subcloned into the promoterless luciferase expression vector
-
recombinant expression in Escherichia coli strain BL21(DE3)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
expression of selenocysteine lyase is higher in acute and lower in chronic glomerulonephritis, selenocysteine lyase is upregulated by IL1b in acute nephritis leading to the synthesis of selenoproteins, which act as oxygen radical scavengers and lead to the limitation and resolution of acute glomerular inflammation
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
Suzuki, K.T.; Kurasaki, K.; Suzuki, N.
Selenocysteine beta-lyase and methylselenol demethylase in the metabolism of Se-methylated selenocompounds into selenide
Biochim. Biophys. Acta
1770
1053-1061
2007
Rattus norvegicus, Rattus norvegicus Wistar
Manually annotated by BRENDA team
Jafari, C.; Panzer, U.; Steinmetz, O.M.; Zahner, G.; Stahl, R.A.; Harendza, S.
Enhanced expression of selenocysteine lyase in acute glomerulonephritis and its regulation by AP-1
Cell. Mol. Biol. Lett.
11
424-437
2006
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
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
Rattus norvegicus (Q68FT9)
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