Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 4.4.1.16 - selenocysteine lyase and Organism(s) Homo sapiens

for references in articles please use BRENDA:EC4.4.1.16
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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) .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
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
Sec lyase
-
selenocysteine beta-lyase
-
-
-
-
selenocysteine reductase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor
show the reaction diagram
reaction mechanism and mechanism of substrate recognition, model, overview. A pyridoxal 5'-phosphate-substrate intermediate is attacked by a deprotonated active site Cys, producing the protein-bound persulfide or sulfoselenide, formation of the external Cys-aldimine intermediate.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha,beta-elimination
-
-
-
-
cleavage of C-Se bond
-
-
-
-
elimination of chloride
-
-
-
-
elimination of H2Se
-
-
-
-
elimination of SO2
-
-
-
-
oxidative elimination of NH3
-
-
-
-
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-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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-cysteine
-
noncompetitive
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
L-selenocysteine
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.85
L-cysteine
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
dominantly in Leydig cells and spermatids
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SCLY_HUMAN
445
0
48149
Swiss-Prot
other Location (Reliability: 2)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme in dimeric and tetrameric forms, sitting drop vapour diffusion method, 100 nl of 17 mg/ml protein solution with 100 nl of well solution 1 containing 100 mM HEPES, pH 6.7, and 10% PEG 6000, or well solution 2 containing 50 mM HEPES, pH 8.1, 200 mM ammonium nitrate and 25% PEG 3350, 20°C, 3 days or 7 days, respectively, X-ray diffraction structure determination and analysis of the two crystals forms at 2.1 A and 1.8 A resolution, respectively, modeling of dimeric enzyme complexed with pyridoxal 5'-phosphate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D146K
D146K/H389T
H389T
site-directed mutagenesis, the mutant variant shows loss of selenocysteine specificity and appearance of cysteine desulfurase activity
V256S
site-directed mutagenesis, the mutant variant shows loss of selenocysteine specificity and appearance of cysteine desulfurase activity
additional information
-
HeLa cells transfected with enzyme-specific siRNA show decreased seleno-labeling efficiency of selenoproteins with selenoprotein P compared to the wild-type
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
purified enzyme, pH 8.5, 2 min, inactivation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration, followed by tag cleavage through TEV protease, another step of nickel affinity chromatography, and dialysis
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
sequence comparisons, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
presence or absence of selenoproteins does not affect enzyme expression in HeLa cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Daher, R.; Van Lente, F.
Characterization of selenocysteine lyase in human tissues and its relationship to tissue selenium concentrations
J. Trace Elem. Electrolytes Health Dis.
6
189-194
1992
Homo sapiens, Sus scrofa
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
Johansson, A.L.; Collins, R.; Arner, E.S.; Brzezinski, P.; Hoegbom, M.
Biochemical discrimination between selenium and sulfur 2: mechanistic investigation of the selenium specificity of human selenocysteine lyase
PLoS ONE
7
e30528
2012
Homo sapiens (Q96I15), Homo sapiens
Manually annotated by BRENDA team
Collins, R.; Johansson, A.L.; Karlberg, T.; Markova, N.; van den Berg, S.; Olesen, K.; Hammarstroem, M.; Flores, A.; Schueler, H.; Schiavone, L.H.; Brzezinski, P.; Arner, E.S.; Hoegbom, M.
Biochemical discrimination between selenium and sulfur 1: a single residue provides selenium specificity to human selenocysteine lyase
PLoS ONE
7
e30581
2012
Homo sapiens (Q96I15), Homo sapiens
Manually annotated by BRENDA team