Information on EC 2.9.1.2 - O-phospho-L-seryl-tRNASec:L-selenocysteinyl-tRNA synthase

for references in articles please use BRENDA:EC2.9.1.2
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The expected taxonomic range for this enzyme is: Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
2.9.1.2
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RECOMMENDED NAME
GeneOntology No.
O-phospho-L-seryl-tRNASec:L-selenocysteinyl-tRNA synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
O-phospho-L-seryl-tRNASec + selenophosphate + H2O = L-selenocysteinyl-tRNASec + 2 phosphate
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-selenocysteine biosynthesis II (archaea and eukaryotes)
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selenocysteine biosynthesis
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Selenocompound metabolism
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Aminoacyl-tRNA biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
selenophosphate:O-phospho-L-seryl-tRNASec selenium transferase
A pyridoxal-phosphate protein [4]. In archaea and eukarya selenocysteine formation is achieved by a two-step process: EC 2.7.1.164 (O-phosphoseryl-tRNASec kinase) phosphorylates the endogenous L-seryl-tRNASec to O-phospho-L-seryl-tRNASec, and then this misacylated amino acid-tRNA species is converted to L-selenocysteinyl-tRNASec by Sep-tRNA:Sec-tRNA synthase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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enzyme silencing clearly inhibits proliferation of JEG-3 cells, significantly induces cell apoptosis and reduces the production of progesterone and human chorionic gonadotropin
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-phosphoseryl-tRNASec + selenophosphate
L-selenocysteinyl-tRNASec + phosphate
show the reaction diagram
O-phospho-L-seryl-tRNASec + selenophosphate
L-selenocysteinyl-tRNASec + phosphate
show the reaction diagram
O-phospho-L-seryl-tRNASec + selenophosphate + H2O
L-selenocysteinyl-tRNASec + phosphate
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-phosphoseryl-tRNASec + selenophosphate
L-selenocysteinyl-tRNASec + phosphate
show the reaction diagram
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selenocysteine is the only genetically encoded amino acid in humans whose biosynthesis occurs on its cognate transfer RNA (tRNA). O-Phosphoseryl-tRNA:selenocysteinyl-tRNA synthase catalyzes the final step of selenocysteine formation by a tRNA-dependent mechanism
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?
O-phospho-L-seryl-tRNASec + selenophosphate
L-selenocysteinyl-tRNASec + phosphate
show the reaction diagram
O-phospho-L-seryl-tRNASec + selenophosphate + H2O
L-selenocysteinyl-tRNASec + phosphate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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primary cultured chicken embryos neurons
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of the quaternary complex between human SepSecS, unacylated tRNASec, and a mixture of O-phosphoserine and thiophosphate to 2.8 A resolution
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sitting-drop vapor diffusion method at 20°C, crystal structure of the enzyme complexed with pyridoxal 5'-phosphate at 2.5 A resolution
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
recombinent enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli SelA-deficient strain JS1
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
significant increase in mRNA levels is observed in all of the brain tissues of chickens fed diets containing 1-5 mg/kg sodium selenite. Significant changes in SepSecS mRNA levels are not observed in neurons treated with Se. Presence of Se alters the SepSecS mRNA half-life in cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K173A
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in vivo activity of the mutant is indistinguishable from that of the wild-type enzyme
K173M
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in vivo activity of the mutant is indistinguishable from that of the wild-type enzyme
Q105A
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mutant is inactive in vivo
R313A
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mutant is inactive in vivo
R75A
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mutant is inactive in vivo
R97A
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in vivo activity of the mutant is indistinguishable from that of the wild-type enzyme
R97Q
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in vivo activity of the mutant is indistinguishable from that of the wild-type enzyme
H166A
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the mutant is partially active in forming Sec-tRNASec in vivo. In vitro, the mutant is partially active in forming Cys-tRNASec
H166F
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mutant is inactive in vivo
H166Q
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mutant is inactive in vivo
R307A
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the mutant is significantly less active in L-selenocysteinyl-tRNASec formation in vivo and Cys-tRNASec formation in vitro
R72A
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the mutant enzyme is significantly less active in L-selenocysteinyl-tRNASec formation in vivo and Cys-tRNASec formation in vitro. The mutant enzyme is unable to form L-selenocysteinyl-tRNASec in vitro
Show AA Sequence (482 entries)
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