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2'(3')-O-(2,4,6-trinitrophenyl)adenosine-5'-triphosphate + selenide + H2O
2'(3')-O-(2,4,6-trinitrophenyl)adenosine-5'-monophosphate + selenophosphate + phosphate
ATP + dithiothreitol + H2O
?
-
as effective as selenide
-
-
?
ATP + selenide
AMP + selenophosphate + phosphate
ATP + selenide + H2O
AMP + selenophosphate + phosphate
additional information
?
-
2'(3')-O-(2,4,6-trinitrophenyl)adenosine-5'-triphosphate + selenide + H2O
2'(3')-O-(2,4,6-trinitrophenyl)adenosine-5'-monophosphate + selenophosphate + phosphate
-
the compound is used as a synthetic analogue of the substrate ATP for the monitoring and quantitative analysis of the functional activity of SPS
-
-
?
2'(3')-O-(2,4,6-trinitrophenyl)adenosine-5'-triphosphate + selenide + H2O
2'(3')-O-(2,4,6-trinitrophenyl)adenosine-5'-monophosphate + selenophosphate + phosphate
-
the compound is used as a synthetic analogue of the substrate ATP for the monitoring and quantitative analysis of the functional activity of SPS
-
-
?
ATP + selenide
AMP + selenophosphate + phosphate
selenophosphate synthetase catalyzes the activation of selenide with ATP to synthesize selenophosphate, the reactive selenium donor for biosyntheses of both the 21st amino acid selenocysteine and 2-selenouridine nucleotides in tRNA anticodons
-
-
?
ATP + selenide
AMP + selenophosphate + phosphate
the phosphate moiety of selenophosphate is derived from the ATP gamma-phosphate, while the orthophosphate is from the beta-phosphate
-
-
?
ATP + selenide
AMP + selenophosphate + phosphate
-
-
-
-
?
ATP + selenide
AMP + selenophosphate + phosphate
-
-
-
-
?
ATP + selenide
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide
AMP + selenophosphate + phosphate
SelD is a key factor for Se utilization by generating a Se donor compound and therefore discriminating Se from sulfur for further use
-
-
?
ATP + selenide
AMP + selenophosphate + phosphate
-
-
-
-
?
ATP + selenide
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide
AMP + selenophosphate + phosphate
selenophosphate synthetase produces the biologically active selenium donor compound, monoselenophosphate, from ATP and selenide, for the synthesis of selenocysteine
-
-
?
ATP + selenide
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide
AMP + selenophosphate + phosphate
SPS2
-
-
?
ATP + selenide
AMP + selenophosphate + phosphate
SPS2 acts as an autoregulator of selenoprotein synthesis, selenocysteine biosynthesis, overview
-
-
?
ATP + selenide
AMP + selenophosphate + phosphate
SPS2, the catalytically important selenocysteine residue is located at position 63
-
-
?
ATP + selenide
AMP + selenophosphate + phosphate
-
-
-
-
?
ATP + selenide
AMP + selenophosphate + phosphate
-
selenophosphate synthetase produces the biologically active selenium donor compound, monoselenophosphate, from ATP and selenide, for the synthesis of selenocysteine
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
Sec replaces the catalytically essential Cys residue, SPS is strictly conserved in the organisms that utilize Sec and/or selenouridine
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
the phosphate moiety of selenophosphate is derived from the ATP gamma-phosphate group, while the orthophosphate is from the beta-phosphate group. Although Thr221 is not essential for the reaction, it contributes to the enzyme activity, probably by interacting with the ATP gamma-phosphate group and a water molecule. Sec/Cys13 and Lys16 are essential for the SPS catalysis. Thr221 and Gly222 interact with the gamma-phosphate group of ATP
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
involved in synthesis of selenoproteins, that provide protection against oxidative stress by acting as cellular antioxidants
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
required for synthesis of selenoproteins and therefore involved in cell differentiation and development
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
r
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
specific for ATP
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
in the absence of selenide, ATP is converted completely to AMP and phosphate
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
in the absence of selenide, ATP is converted completely to AMP and phosphate
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
in the absence of selenide, ATP is converted completely to AMP and phosphate
selenophosphate is derived from the gamma phosphoryl group and phosphate from the beta phosphoryl group of ATP
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
the gamma-phosphoryl group of the substrate ATP is cleaved in a kinetically competent reaction to form a phosphoryl-enzyme intermediate in the absence of the second substrate, selenide
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
the enzyme provides the biologically active selenium donor compound monoseleniumphosphate
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
required for synthesis of selenocysteine and seleno-tRNAs
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
the Sps1-encoded enzyme depends on a selenium salvage system that recycles L-selenocysteine
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
the Sps2-encoded can function with a selenite assimilation system
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
the enzyme is involved in biosynthesis of selenophosphate, that is the in vivo selenium donor for selenoprotein synthesis of Methanococcus maripaludis S2
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
specific for ATP
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
required for synthesis of selenocysteine and seleno-tRNAs
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
selenide can be substituted by dithiothreitol, but only very poorly by L-selenocysteine and NaSH
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
provides the selenium donor substrate for the rRNA 2-selenouridine synthase reaction
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
provides selenophosphate, that can serve as selenium donor for the reaction in which 5-methylaminomethyl-2-thiouridine is converted to 5-methylaminomethyl-2-selenouridine
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
-
-
?
additional information
?
-
SPS orthologs, SPS1 and SPS2, exist, and SPS2 is the one that synthesizes selenophosphate, while SPS1 does not
-
-
?
additional information
?
-
-
SPS orthologs, SPS1 and SPS2, exist, and SPS2 is the one that synthesizes selenophosphate, while SPS1 does not
-
-
?
additional information
?
-
-
a DNA replication-related element downstream from the initiation site of selenophosphate synthetase 2 gene is essential for its transcription
-
-
?
additional information
?
-
no activity by selenophosphate synthetase 1
-
-
?
additional information
?
-
-
Enterococcus faecalis lacks both the selenocysteine and selenouridine systems, but possesses orphan selenophosphate synthetase SelD
-
-
?
additional information
?
-
enzymes involved in selenium utilization, i.e. SelA/SelB and YbbB that define Sec and SeU pathways, respectively, and NADH oxidoreductase generating a SelD substrate, overview. Non-Sec utilization of selenium occurs in Enterococcus faecalis, metabolic labeling, overview
-
-
?
additional information
?
-
-
enzymes involved in selenium utilization, i.e. SelA/SelB and YbbB that define Sec and SeU pathways, respectively, and NADH oxidoreductase generating a SelD substrate, overview. Non-Sec utilization of selenium occurs in Enterococcus faecalis, metabolic labeling, overview
-
-
?
additional information
?
-
-
no activity by selenophosphate synthetase 1
-
-
?
additional information
?
-
Haloarcula marismortui lacks both the selenocysteine and selenouridine systems, but possesses orphan selenophosphate synthetase SelD
-
-
?
additional information
?
-
-
Haloarcula marismortui lacks both the selenocysteine and selenouridine systems, but possesses orphan selenophosphate synthetase SelD
-
-
?
additional information
?
-
SPS2 is involved in the synthesis of selenophosphate for Sel synthesis, selen and selenoprotien metabolism, physiological functions, detailed overview
-
-
?
additional information
?
-
development of a non-radioactive assay for detection of selenophosphate synthetase activity using recombinant pyruvate diphosphate dikinase, PPDK, from Thermus thermophilus strain HB8 in an enzyme-coupled reaction system, overview
-
-
?
additional information
?
-
-
SPS1 probably has a specialized, non-essential role in selenoprotein metabolism
-
-
?
additional information
?
-
SPS1 probably has a specialized, non-essential role in selenoprotein metabolism
-
-
?
additional information
?
-
SPS1 probably has a specialized, non-essential role in selenoprotein metabolism
-
-
?
additional information
?
-
Sps2 is both a selenoprotein and a factor involved in synthesis of other selenoproteins
-
-
?
additional information
?
-
-
Sps2 is both a selenoprotein and a factor involved in synthesis of other selenoproteins
-
-
?
additional information
?
-
-
SPS2 is essential for generating the selenium donor for selenocysteine biosynthesis in mammals
-
-
?
additional information
?
-
SPS2 is essential for generating the selenium donor for selenocysteine biosynthesis in mammals
-
-
?
additional information
?
-
SPS2 is essential for generating the selenium donor for selenocysteine biosynthesis in mammals
-
-
?
additional information
?
-
no activity by selenophosphate synthetase 1
-
-
?
additional information
?
-
Se in the form of the amino acid, selenocysteine, is incorporated into selenoproteins at UGA codons
-
-
?
additional information
?
-
-
Se in the form of the amino acid, selenocysteine, is incorporated into selenoproteins at UGA codons
-
-
?
additional information
?
-
SPS1 shows no activity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + selenide
AMP + selenophosphate + phosphate
ATP + selenide + H2O
AMP + selenophosphate + phosphate
additional information
?
-
ATP + selenide
AMP + selenophosphate + phosphate
selenophosphate synthetase catalyzes the activation of selenide with ATP to synthesize selenophosphate, the reactive selenium donor for biosyntheses of both the 21st amino acid selenocysteine and 2-selenouridine nucleotides in tRNA anticodons
-
-
?
ATP + selenide
AMP + selenophosphate + phosphate
-
-
-
-
?
ATP + selenide
AMP + selenophosphate + phosphate
SelD is a key factor for Se utilization by generating a Se donor compound and therefore discriminating Se from sulfur for further use
-
-
?
ATP + selenide
AMP + selenophosphate + phosphate
selenophosphate synthetase produces the biologically active selenium donor compound, monoselenophosphate, from ATP and selenide, for the synthesis of selenocysteine
-
-
?
ATP + selenide
AMP + selenophosphate + phosphate
SPS2
-
-
?
ATP + selenide
AMP + selenophosphate + phosphate
SPS2 acts as an autoregulator of selenoprotein synthesis, selenocysteine biosynthesis, overview
-
-
?
ATP + selenide
AMP + selenophosphate + phosphate
-
selenophosphate synthetase produces the biologically active selenium donor compound, monoselenophosphate, from ATP and selenide, for the synthesis of selenocysteine
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
Sec replaces the catalytically essential Cys residue, SPS is strictly conserved in the organisms that utilize Sec and/or selenouridine
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
involved in synthesis of selenoproteins, that provide protection against oxidative stress by acting as cellular antioxidants
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
required for synthesis of selenoproteins and therefore involved in cell differentiation and development
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
the enzyme provides the biologically active selenium donor compound monoseleniumphosphate
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
required for synthesis of selenocysteine and seleno-tRNAs
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
the Sps1-encoded enzyme depends on a selenium salvage system that recycles L-selenocysteine
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
the Sps2-encoded can function with a selenite assimilation system
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
the enzyme is involved in biosynthesis of selenophosphate, that is the in vivo selenium donor for selenoprotein synthesis of Methanococcus maripaludis S2
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
required for synthesis of selenocysteine and seleno-tRNAs
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
provides the selenium donor substrate for the rRNA 2-selenouridine synthase reaction
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
provides selenophosphate, that can serve as selenium donor for the reaction in which 5-methylaminomethyl-2-thiouridine is converted to 5-methylaminomethyl-2-selenouridine
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
-
-
-
?
ATP + selenide + H2O
AMP + selenophosphate + phosphate
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
-
-
?
additional information
?
-
SPS orthologs, SPS1 and SPS2, exist, and SPS2 is the one that synthesizes selenophosphate, while SPS1 does not
-
-
?
additional information
?
-
-
SPS orthologs, SPS1 and SPS2, exist, and SPS2 is the one that synthesizes selenophosphate, while SPS1 does not
-
-
?
additional information
?
-
-
a DNA replication-related element downstream from the initiation site of selenophosphate synthetase 2 gene is essential for its transcription
-
-
?
additional information
?
-
-
Enterococcus faecalis lacks both the selenocysteine and selenouridine systems, but possesses orphan selenophosphate synthetase SelD
-
-
?
additional information
?
-
enzymes involved in selenium utilization, i.e. SelA/SelB and YbbB that define Sec and SeU pathways, respectively, and NADH oxidoreductase generating a SelD substrate, overview. Non-Sec utilization of selenium occurs in Enterococcus faecalis, metabolic labeling, overview
-
-
?
additional information
?
-
-
enzymes involved in selenium utilization, i.e. SelA/SelB and YbbB that define Sec and SeU pathways, respectively, and NADH oxidoreductase generating a SelD substrate, overview. Non-Sec utilization of selenium occurs in Enterococcus faecalis, metabolic labeling, overview
-
-
?
additional information
?
-
Haloarcula marismortui lacks both the selenocysteine and selenouridine systems, but possesses orphan selenophosphate synthetase SelD
-
-
?
additional information
?
-
-
Haloarcula marismortui lacks both the selenocysteine and selenouridine systems, but possesses orphan selenophosphate synthetase SelD
-
-
?
additional information
?
-
SPS2 is involved in the synthesis of selenophosphate for Sel synthesis, selen and selenoprotien metabolism, physiological functions, detailed overview
-
-
?
additional information
?
-
-
SPS1 probably has a specialized, non-essential role in selenoprotein metabolism
-
-
?
additional information
?
-
SPS1 probably has a specialized, non-essential role in selenoprotein metabolism
-
-
?
additional information
?
-
SPS1 probably has a specialized, non-essential role in selenoprotein metabolism
-
-
?
additional information
?
-
Sps2 is both a selenoprotein and a factor involved in synthesis of other selenoproteins
-
-
?
additional information
?
-
-
Sps2 is both a selenoprotein and a factor involved in synthesis of other selenoproteins
-
-
?
additional information
?
-
-
SPS2 is essential for generating the selenium donor for selenocysteine biosynthesis in mammals
-
-
?
additional information
?
-
SPS2 is essential for generating the selenium donor for selenocysteine biosynthesis in mammals
-
-
?
additional information
?
-
SPS2 is essential for generating the selenium donor for selenocysteine biosynthesis in mammals
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
-
selenoproteins (containing the 21st proteinogenic amino acid selenocysteine) play important roles throughout all domains of life. A number of taxa have small selenoproteomes, and Hymenopteran insects appear to have fully lost selenoproteins. Nevertheless, their genomes contain genes for several proteins of the selenocysteine insertion machinery, including selenophosphate synthetase 1 (SELD/SPS1)
evolution
selenoproteins are proteins that incorporate selenocysteine (Sec), a nonstandard amino acid encoded by UGA, normally a stop codon. Sec synthesis requires the enzyme selenophosphate synthetase, conserved in all prokaryotic and eukaryotic genomes encoding selenoproteins. SPS1 genes originated through a number of independent gene duplications from an ancestral metazoan selenoprotein SPS2 gene that most likely already carried the SPS1 function. In SPS genes, parallel duplications and subsequent convergent subfunctionalization have resulted in the segregation to different loci of functions initially carried by a single gene. Evolutionary history of SPS genes, mapping of selenoprotein function spanning the whole tree of life. SPS is itself a selenoprotein in many species, although functionally equivalent homologues that replace the Sec site with cysteine (Cys) are common, e.g. Drosophila melanogaster possesses three selenoprotein genes, while Drosophila willistoni has replaced Sec with Cys in them and lost the capacity to synthesize Sec. Unequal selective pressure on SPS1 and SPS2 genes after duplication, overview
evolution
-
selenoproteins are proteins that incorporate selenocysteine (Sec), a nonstandard amino acid encoded by UGA, normally a stop codon. Sec synthesis requires the enzyme selenophosphate synthetase, conserved in all prokaryotic and eukaryotic genomes encoding selenoproteins. SPS1 genes originated through a number of independent gene duplications from an ancestral metazoan selenoprotein SPS2 gene that most likely already carried the SPS1 function. In SPS genes, parallel duplications and subsequent convergent subfunctionalization have resulted in the segregation to different loci of functions initially carried by a single gene. Evolutionary history of SPS genes, mapping of selenoprotein function spanning the whole tree of life. SPS is itself a selenoprotein in many species, although functionally equivalent homologues that replace the Sec site with cysteine (Cys) are common. At the root of ascidians, the ancestral SPS2-Sec gene acquired a novel SPS-Gly transcript isoform through alternative exon usage at the 5'-end. Then, at the root of the ascidian lineage, Styelidae and Pyuridae, the SPS-Sec transcript of this dual SPS1/SPS2 gene (SPS-ae) retrotransposed to the genome creating a novel SPS2-Sec gene (GDR). This presumably triggered the loss of Sec from the parental gene, which, because both the SECIS and the UGA containing exon degenerated (SL), specialized only in the production of SPS1-Gly. Parallel gene duplications of SPS proteins in metazoa, phylogenetic analysis, overview
evolution
-
selenoproteins are proteins that incorporate selenocysteine (Sec), a nonstandard amino acid encoded by UGA, normally a stop codon. Sec synthesis requires the enzyme selenophosphate synthetase, conserved in all prokaryotic and eukaryotic genomes encoding selenoproteins. SPS1 genes originated through a number of independent gene duplications from an ancestral metazoan selenoprotein SPS2 gene that most likely already carried the SPS1 function. In SPS genes, parallel duplications and subsequent convergent subfunctionalization have resulted in the segregation to different loci of functions initially carried by a single gene. Evolutionary history of SPS genes, mapping of selenoprotein function spanning the whole tree of life. SPS is itself a selenoprotein in many species, although functionally equivalent homologues that replace the Sec site with cysteine (Cys) are common. At the root of ascidians, the ancestral SPS2-Sec gene acquired a novel SPS-Gly transcript isoform through alternative exon usage at the 5'-end. Then, at the root of the ascidian lineage, Styelidae and Pyuridae, the SPS-Sec transcript of this dual SPS1/SPS2 gene (SPS-ae) retrotransposed to the genome creating a novel SPS2-Sec gene (GDR). This presumably triggered the loss of Sec from the parental gene, which, because both the SECIS and the UGA containing exon degenerated (SL), specialized only in the production of SPS1-Gly. Parallel gene duplications of SPS proteins in metazoa, phylogenetic analysis, overview
evolution
-
selenoproteins are proteins that incorporate selenocysteine (Sec), a nonstandard amino acid encoded by UGA, normally a stop codon. Sec synthesis requires the enzyme selenophosphate synthetase, conserved in all prokaryotic and eukaryotic genomes encoding selenoproteins. SPS1 genes originated through a number of independent gene duplications from an ancestral metazoan selenoprotein SPS2 gene that most likely already carried the SPS1 function. In SPS genes, parallel duplications and subsequent convergent subfunctionalization have resulted in the segregation to different loci of functions initially carried by a single gene. Evolutionary history of SPS genes, mapping of selenoprotein function spanning the whole tree of life. SPS is itself a selenoprotein in many species, although functionally equivalent homologues that replace the Sec site with cysteine (Cys) are common. At the root of ascidians, the ancestral SPS2-Sec gene acquired a novel SPS-Gly transcript isoform through alternative exon usage at the 5'-end. Then, at the root of the ascidian lineage, Styelidae and Pyuridae, the SPS-Sec transcript of this dual SPS1/SPS2 gene (SPS-ae) retrotransposed to the genome creating a novel SPS2-Sec gene (GDR). This presumably triggered the loss of Sec from the parental gene, which, because both the SECIS and the UGA containing exon degenerated (SL), specialized only in the production of SPS1-Gly. Parallel gene duplications of SPS proteins in metazoa, phylogenetic analysis, overview
evolution
-
selenoproteins are proteins that incorporate selenocysteine (Sec), a nonstandard amino acid encoded by UGA, normally a stop codon. Sec synthesis requires the enzyme selenophosphate synthetase, conserved in all prokaryotic and eukaryotic genomes encoding selenoproteins. SPS1 genes originated through a number of independent gene duplications from an ancestral metazoan selenoprotein SPS2 gene that most likely already carried the SPS1 function. In SPS genes, parallel duplications and subsequent convergent subfunctionalization have resulted in the segregation to different loci of functions initially carried by a single gene. Evolutionary history of SPS genes, mapping of selenoprotein function spanning the whole tree of life. SPS is itself a selenoprotein in many species, although functionally equivalent homologues that replace the Sec site with cysteine (Cys) are common. At the root of ascidians, the ancestral SPS2-Sec gene acquired a novel SPS-Gly transcript isoform through alternative exon usage at the 5'-end. Then, at the root of the ascidian lineage, Styelidae and Pyuridae, the SPS-Sec transcript of this dual SPS1/SPS2 gene (SPS-ae) retrotransposed to the genome creating a novel SPS2-Sec gene (GDR). This presumably triggered the loss of Sec from the parental gene, which, because both the SECIS and the UGA containing exon degenerated (SL), specialized only in the production of SPS1-Gly. Parallel gene duplications of SPS proteins in metazoa, phylogenetic analysis, overview
evolution
selenoproteins are proteins that incorporate selenocysteine (Sec), a nonstandard amino acid encoded by UGA, normally a stop codon. Sec synthesis requires the enzyme selenophosphate synthetase, conserved in all prokaryotic and eukaryotic genomes encoding selenoproteins. SPS1 genes originated through a number of independent gene duplications from an ancestral metazoan selenoprotein SPS2 gene that most likely already carried the SPS1 function. In SPS genes, parallel duplications and subsequent convergent subfunctionalization have resulted in the segregation to different loci of functions initially carried by a single gene. Evolutionary history of SPS genes, mapping of selenoprotein function spanning the whole tree of life. SPS is itself a selenoprotein in many species, although functionally equivalent homologues that replace the Sec site with cysteine (Cys) are common. In Caenorhabditis elegans, the entire pathway is maintained only to synthesize a single selenoprotein. Unequal selective pressure on SPS1 and SPS2 genes after duplication, overview
evolution
-
selenoproteins are proteins that incorporate selenocysteine (Sec), a nonstandard amino acid encoded by UGA, normally a stop codon. Sec synthesis requires the enzyme selenophosphate synthetase, conserved in all prokaryotic and eukaryotic genomes encoding selenoproteins. SPS1 genes originated through a number of independent gene duplications from an ancestral metazoan selenoprotein SPS2 gene that most likely already carried the SPS1 function. In SPS genes, parallel duplications and subsequent convergent subfunctionalization have resulted in the segregation to different loci of functions initially carried by a single gene. Evolutionary history of SPS genes, mapping of selenoprotein function spanning the whole tree of life. SPS is itself a selenoprotein in many species, although functionally equivalent homologues that replace the Sec site with cysteine (Cys) are common. Phylogenetic profile of SPS and selenium utilization traits in prokaryotes, overview
evolution
selenoproteins are proteins that incorporate selenocysteine (Sec), a nonstandard amino acid encoded by UGA, normally a stop codon. Sec synthesis requires the enzyme selenophosphate synthetase, conserved in all prokaryotic and eukaryotic genomes encoding selenoproteins. SPS1 genes originated through a number of independent gene duplications from an ancestral metazoan selenoprotein SPS2 gene that most likely already carried the SPS1 function. In SPS genes, parallel duplications and subsequent convergent subfunctionalization have resulted in the segregation to different loci of functions initially carried by a single gene. Evolutionary history of SPS genes, mapping of selenoprotein function spanning the whole tree of life. SPS is itself a selenoprotein in many species, although functionally equivalent homologues that replace the Sec site with cysteine (Cys) are common. Unequal selective pressure on SPS1 and SPS2 genes after duplication, overview
evolution
-
SEPHS1 and SEPHS2 most likely segregate from their common ancestor prior to speciation
evolution
SEPHS1 and SEPHS2 most likely segregate from their common ancestor prior to speciation
evolution
-
the dimeric organization is functionally important throughout the domains of life
evolution
the dimeric organization is functionally important throughout the domains of life
evolution
the dimeric organization is functionally important throughout the domains of life
evolution
-
the dimeric organization is functionally important throughout the domains of life
-
malfunction
isoform SPS2 absence severely hampers the parasite survival in the presence of an oxidizing environment that results in an apoptotic-like phenotype and cell death
malfunction
-
vitamin B6 biosynthesis is significantly affected at the early stage at which megamitochondria are not formed (day 3) after isoform SPS1 knockdown. Genes related to defense and amino acid metabolism are affected at a later stage (day 5) following enzyme knockdown. Levels of pyridoxal phosphate, an active form of vitamin B6, are decreased by isoform SPS1 knockdown
malfunction
-
in the enzyme knockout mutant, the function of SPS2 proteins is significantly inhibited, it is possible that the expression levels of selenoproteins in fruit flies might be reduced
malfunction
systemic SPS1 deficiency in Sps1 knockout mice leads to embryos are clearly underdeveloped by E8.5 and virtually resorbed by E14.5. The knockout of Sps1 in the liver preserves viability, but significantly affects the expression of a large number of mRNAs involved in cancer, embryonic development, and the glutathione system, especially extreme deficiency of glutaredoxin 1 (GLRX1) and glutathione-S-transferase omega 1. Targeted removal of SPS1 in F9 cells, a mouse embryonal carcinoma cell line, affects the glutathione system proteins and accordingly leads to the accumulation of hydrogen peroxide in the cell. Hydrogen peroxide accumulates due to the downregulation of GLRX1 in SPS1-deficient F9 cells. Overexpression of mouse or human GLRX1 leads to a reversal of observed increases in reactive oxygen species in the F9 SPS1/GLRX1-deficient cells and result in levels that are similar to those in F9 SPS1-sufficient cells. Loss of Sps1 in the liver affects iron and manganese levels. The expression of genes encoding proteins responsible for the de novo synthesis of glutathione, such as glutamate cysteine ligase catalytic subunit (GCLC), glutamate-cysteine modifier subunit (GCLM), and glutathione synthetase (GSS), is not affected by a deficiency in SPS1
malfunction
-
the selD CRISPR deletion mutant has a growth defect in protein-rich medium and mimicks the phenotype of a generated TargeTron selD mutation
malfunction
-
systemic SPS1 deficiency in Sps1 knockout mice leads to embryos are clearly underdeveloped by E8.5 and virtually resorbed by E14.5. The knockout of Sps1 in the liver preserves viability, but significantly affects the expression of a large number of mRNAs involved in cancer, embryonic development, and the glutathione system, especially extreme deficiency of glutaredoxin 1 (GLRX1) and glutathione-S-transferase omega 1. Targeted removal of SPS1 in F9 cells, a mouse embryonal carcinoma cell line, affects the glutathione system proteins and accordingly leads to the accumulation of hydrogen peroxide in the cell. Hydrogen peroxide accumulates due to the downregulation of GLRX1 in SPS1-deficient F9 cells. Overexpression of mouse or human GLRX1 leads to a reversal of observed increases in reactive oxygen species in the F9 SPS1/GLRX1-deficient cells and result in levels that are similar to those in F9 SPS1-sufficient cells. Loss of Sps1 in the liver affects iron and manganese levels. The expression of genes encoding proteins responsible for the de novo synthesis of glutathione, such as glutamate cysteine ligase catalytic subunit (GCLC), glutamate-cysteine modifier subunit (GCLM), and glutathione synthetase (GSS), is not affected by a deficiency in SPS1
-
malfunction
-
the selD CRISPR deletion mutant has a growth defect in protein-rich medium and mimicks the phenotype of a generated TargeTron selD mutation
-
metabolism
-
isoform selenophosphate synthetase 1 regulates vitamin B6 metabolism
metabolism
-
isoform SPS-1 plays a potential role in selenoprotein W biosynthesis
metabolism
-
considering that Se utilization and homeostasis may play a role in diabetogenesis and some other metabolic disorder, regucalcin can become a potential link between the Se metabolism and those metabolic disorders/diseases
metabolism
-
selenophosphate synthetase (SEPHS/SPS) plays an indispensable role in selenium metabolism, being responsible for catalyzing the formation of selenophosphate, the biological selenium donor for selenocysteine synthesis
metabolism
selenophosphate synthetase (SEPHS/SPS) plays an indispensable role in selenium metabolism, being responsible for catalyzing the formation of selenophosphate, the biological selenium donor for selenocysteine synthesis
metabolism
selenophosphate synthetase (SEPHS/SPS) plays an indispensable role in selenium metabolism, being responsible for catalyzing the formation of selenophosphate, the biological selenium donor for selenocysteine synthesis
metabolism
the enzyme is essential for selenoprotein biosynthesis. It is required for the development and selenium homeostasis of central nervous system
metabolism
-
the enzyme is involved in selenocysteine biosynthesis. The interaction between selenocysteine lyase and selenophosphate synthetase occurs with a stoichiometry of 1:1
metabolism
-
selenophosphate synthetase (SEPHS/SPS) plays an indispensable role in selenium metabolism, being responsible for catalyzing the formation of selenophosphate, the biological selenium donor for selenocysteine synthesis
-
physiological function
-
selenophosphate synthetase is a key enzyme of the selenium pathway in the cell
physiological function
-
SPS1/SelD regulates the intracellular glutamine level by regulating genes involved in glutamine biosynthesis
physiological function
isoform SPS2 is involved in oxidative stress protection of the parasite
physiological function
the cloned enzyme in hemocytes plays a role in viability by renewing hemocytes and antioxidative stress response for new exoskeleton synthesis during the molt cycle of shrimp
physiological function
the enzyme is involved in biosynthesis of selenophosphate, that is the in vivo selenium donor for selenoprotein synthesis of Methanococcus maripaludis S2
physiological function
Drosophila SPS1 (i.e., ptuf/SelD) lacks the ability to catalyze selenide-dependent ATP hydrolysis or to complement SelD deficiency in Escherichia coli. Drosophila SPS1 has been proposed to be involved in vitamin B6 metabolism and in redox homeostasis since it protects from damage induced by reactive oxygen species
physiological function
-
enzyme SPS2 may play an important role in regulating basic metabolic pathways as well as redox homeostasis, probably via some of the key regulators. The product of SPS2, selenophosphate, activity is required during the translation of selenoprotein genes
physiological function
isozyme SPS1 is an essential mammalian enzyme with roles in regulating redox homeostasis and controlling cell growth. Isozyme SPS1 plays a role in supporting and/or sustaining cancer
physiological function
-
SELD/SPS 1 might play an important role in oxidative stress defense, and might therefore be involved in the life-prolonging effect of mating, and in the stronger life-prolonging effect of winged males
physiological function
the enzyme plays an indispensable role in selenium metabolism, being responsible for catalyzing the activation of selenide with adenosine 5'-triphosphate (ATP) to generate selenophosphate, the essential selenium donor for selenocysteine synthesis
physiological function
SEPHS2 is responsible for de novo synthesis of monoselenophosphate. SEPHS2 interacts with SEPSECS and SEPHS1
physiological function
-
the enzyme is essential for the specific incorporation of selenium into selenoproteins
physiological function
-
the enzyme plays a role for the Trypanosoma brucei selenophosphate synthetase in the regulation of the ER stress response of the parasite
physiological function
the enzyme plays a role for the Trypanosoma brucei selenophosphate synthetase in the regulation of the parasite's ER stress response
physiological function
the enzyme plays a role for the Trypanosoma brucei selenophosphate synthetase in the regulation of the parasite's ER stress response
physiological function
-
isozyme SPS1 is an essential mammalian enzyme with roles in regulating redox homeostasis and controlling cell growth. Isozyme SPS1 plays a role in supporting and/or sustaining cancer
-
physiological function
-
the enzyme is essential for the specific incorporation of selenium into selenoproteins
-
physiological function
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
the enzyme plays an indispensable role in selenium metabolism, being responsible for catalyzing the activation of selenide with adenosine 5'-triphosphate (ATP) to generate selenophosphate, the essential selenium donor for selenocysteine synthesis
-
physiological function
-
the enzyme plays a role for the Trypanosoma brucei selenophosphate synthetase in the regulation of the parasite's ER stress response
-
additional information
SPS2, i.e. Sephs2, invertebrates is a selenoprotein
additional information
-
the non-linear regression analysis of the saturation curve of TNP-ATP binding to D197 SPS fits to a model with 2 distinct binding sites with KDs different in order. Enzyme SPS exists in a form of tetramer in given reaction conditions, in accordance with the concentration stoichiometry of 4 mol of 2'(3')-O-(2,4,6-trinitrophenyl)adenosine-5'-triphosphate to 1 mole of recombinant protein
additional information
-
the non-linear regression analysis of the saturation curve of TNP-ATP binding to D197 SPS fits to a model with 2 distinct binding sites with KDs different in order. Enzyme SPS exists in a form of tetramer in given reaction conditions, in accordance with the concentration stoichiometry of 4 mol of 2'(3')-O-(2,4,6-trinitrophenyl)adenosine-5'-triphosphate to 1 mole of recombinant protein
-
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a single SPS gene, phylogenetic analysis
-
DNA and amino acid sequence determination and analysis of SPS1
DNA and amino acid sequence determination and analysis of SPS2, complementation of SPS2 knockout NIH3T3 cells by expression of SPS2
DNA sequence determination and analysis
DNA sequence determination and analysis, chromosomal mapping, expression in COS-7 cells as FLAG tagged enzyme
expressed in CHO-K1 cells
-
expressed in Escherichia coli BL21(DE3) cells
expression analysis for SPS2 and selenoproteins, overview
expression in Escherichia coli
expression in Eschetrichia coli
expression in Spodoptera frugiperda Sf9 insect cells via baculovirus infection, expression as N-FLAG tagged protein
-
expression in strain BL21(DE3)
-
expression of His-tagged SPS1 and of His-tagged SPS2 mutant Sec69Cys in Escherichia coli strain Rosetta (DE3)
expression of trigger factor-fused SPS2 in Escherichia coli
expression of truncated mutant enzyme SPS-DELTAN in Escherichia coli
gene ptuf/SelD or SPS1, genetic structure analysis, SPS1-UGA might perhaps be translated by a readthrough mechanism not involving Sec insertion. In this respect, there is growing evidence for abundant stop codon readthrough in insects, with UGA being the most frequently observed readthrough codon in Drosophila
gene selD, DNA and amino acid sequence determination and analysis of enzymes from Escherichia coli strains DH5alpha-T1 AND BL21-Gold (DE3), that differ in position 14 and 197, and compared to the DNA sequence from Escherichia coli strain K-12, recombinant overexpression of wild-type and mutant enzymes in Escherichia coli strain BL21-Gold (DE3)
-
gene selD, DNA and amino acid sequence determination and analysis, genomic location, phylogenetic analysis and multiple sequence alignment, genes involved in selenium utilization, overview
gene selD, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain BL21(DE3), and functional complementation of Escherichia coli SelD deletion strain WL400
gene selD, DNA and amino acid sequence determination and analysis, phylogenetic profiling
gene selD, DNA sequence determination and analysis, subcloning and transient expression in enzyme deficient Escherichia coli resulting in poor complemetation of the bacteria by the human gene, and expression in mammalian HtTA cells together with human type I iodothyronine 5'-deiodinase and Xenopus tRNASeC
gene selD, expression of SelD1 alone in Escherichia coli results in low selenophosphate synthetase activity in the wild-type strain XL1-Blue, an Escherichia coli SelB mutant strain WL81300 does not show any selenophosphate synthetase activity. Co-expression of SelB, SelC, and SelD from Eubacterium acidaminophilum leads to production of selenocystein containing proteins, selenoprotein synthesis in Escherichia coli requires the products of the genes selA, selB, selC, and selD
-
gene seld-1, genetic structure analysis
gene selD/sps1, DNA and amino acid sequence determination and analysis, the gene is actually translated in male accessory glands of the selenoprotein-less ant Cardiocondyla obscurior
-
gene Sephs2, recombinant expression of C-terminally His6-tagged enzyme mutant Sephs2U60C in Escherichia coli Rosetta (DE3) pLysS
gene SPS, phylogenetic analysis
gene Sps1, located on chromosome 2, expression anaysis
gene sps2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, sequence comparison, expression in Escherichia coli strain BL21(DE3)
gene SPS2, gene expression profiles of the knockdown of SPS2 in larval and adult stages, quantitative real-time PCR enzyme exxpression analysis in wild-type and mutant strains, detailed overview
-
gene SPS2, phylogenetic analysis
-
into the vector pCR2.1 and subsequently into pKK233.2 for expression in Escherichia coli MB08 cells
-
into the vector pET28a for expression in Escherichia coli Rosetta DE3 cells
NIH3T3 cells are stably transfected with the Tet-on U6 control construct or the Tet-siSPS2 construct and grown in the presence or absence of doxycycline for 3 d to induce SPS2 knockdown, then transiently transfected with pTriEX expression vector or the expression vector encoding SPS2 wild-type gene or SPS2 knock-in gene, SPS2 overexpression and functional restoration
-
overexpression in Escherichia coli strain BL21
-
overexpression of the wild-type enzyme in motoneurons does not extend longevity
-
recombinant expression of His6-tagged enzyme with a thrombin-cleavage site in Escherichia coli strain BL21(DE3)
the mutated sps2 gene, which contains cysteine in the place of the TGA encoded selenocysteine in the wild-type, is expressed in Escherichia coli selD deficient mutant, MB08. Like the Escherichia coli wild-type selD gene, the mutant spos2 gene complements the selD mutation. Replacement of Cys with either Ala, Ser, or Thr results in a loss of ability to complement the selD mutation
-
the open reading frame of Dsps2 mRNA is interrupted by a UGA stop codon. The 3'-UTR contains a mammalian-like Sec insertion sequence which causes translation readthrough in both transfected Drosophila cells and transgenic embryos
-
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
-
expression in Escherichia coli
gene selD, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain BL21(DE3), and functional complementation of Escherichia coli SelD deletion strain WL400
-
gene selD, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain BL21(DE3), and functional complementation of Escherichia coli SelD deletion strain WL400
gene selD, DNA and amino acid sequence determination and analysis, phylogenetic profiling
-
gene selD, DNA and amino acid sequence determination and analysis, phylogenetic profiling
-
gene selD, DNA and amino acid sequence determination and analysis, phylogenetic profiling
gene selD, DNA and amino acid sequence determination and analysis, phylogenetic profiling
gene SPS, phylogenetic analysis
-
gene SPS, phylogenetic analysis
-
gene sps2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, sequence comparison, expression in Escherichia coli strain BL21(DE3)
-
gene sps2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, sequence comparison, expression in Escherichia coli strain BL21(DE3)
-
gene sps2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, sequence comparison, expression in Escherichia coli strain BL21(DE3)
gene sps2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, sequence comparison, expression in Escherichia coli strain BL21(DE3)
recombinant expression of His6-tagged enzyme with a thrombin-cleavage site in Escherichia coli strain BL21(DE3)
recombinant expression of His6-tagged enzyme with a thrombin-cleavage site in Escherichia coli strain BL21(DE3)
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Veres, Z.; Kim, I.Y.; Scholz, T.D.; Stadtman, T.C.
Selenophosphate synthetase. Enzyme properties and catalytic reaction
J. Biol. Chem.
269
10597-10603
1994
Escherichia coli
brenda
Veres, Z.; Stadtman, T.C.
A purified selenophosphate-dependent enzyme from Salmonella typhimurium catalyzes the replacement of sulfur in 2-thiouridine residues in tRNAs with selenium
Proc. Natl. Acad. Sci. USA
91
8092-8096
1994
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Walker, H.; Ferretti, J.A.; Stadtman, T.C.
Isotope exchange studies on the Escherichia coli selenophosphate synthetase mechanism
Proc. Natl. Acad. Sci. USA
95
2180-2185
1998
Escherichia coli
brenda
Veres, Z.; Tsai, L.; Scholz, T.D.; Politino, M.; Balaban, R.S.; Stadtman, T.C
Synthesis of 5-methylaminomethyl-2-selenouridine in tRNAs: 31P NMR studies show the labile selenium donor synthesized by the selD gene product contains selenium bonded to phosphorus
Proc. Natl. Acad. Sci. USA
89
2975-2979
1992
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Kim, I.Y.; Stadtman, T.C.
Effects of monovalent cations and divalent metal ions on Escherichia coli selenophosphate synthetase
Proc. Natl. Acad. Sci. USA
91:
7326-7329
1994
Escherichia coli
brenda
Kim, I.Y.; Stadtman, T.C.
Selenophosphate synthetase: detection in extracts of rat tissues by immunoblot assay and partial purification of the enzyme from the archaeon Methanococcus vannielii
Proc. Natl. Acad. Sci. USA
92
7710-7713
1995
Escherichia coli, Methanococcus vannielii, Rattus norvegicus
brenda
Kim, I.Y.; Veres, Z.; Stadtman, T.C.
Biochemical analysis of Escherichia coli selenophosphate synthetase mutants
J. Biol. Chem.
268
27020-27025
1993
Escherichia coli
brenda
Low, S.C.; Harney, J.W.; Berry, M.J.
Cloning and functional characterization of human selenophosphate synthetase, an essential component of selenoprotein synthesis
J. Biol. Chem.
270
21659-21664
1995
Homo sapiens (P49903), Homo sapiens
brenda
Kim, I.Y.; Guimaraes, M.J.; Zlotnik, A.; Bazan, J.F.; Stadtman, T.C.
Fetal mouse selenophosphate synthetase 2 (SPS2): Characterization of the cysteine mutant form overproduced in a baculovirus-insect cell system
Proc. Natl. Acad. Sci. USA
94
418-421
1997
Mus musculus
brenda
Liu, S.Y.; Stadtman, T.C.
Selenophosphate synthetase: enzyme labeling studies with [gamma-32P]ATP, [beta-32P]ATP, [8-14C]ATP, and [75Se]selenide
Arch. Biochem. Biophys.
341
353-359
1997
Escherichia coli
brenda
Liu, S.Y.; Stadtman, T.C.
A non-r4adioactive and two radioactive assays for selenophosphate synthetase activity
BioFactors
6
305-309
1997
Escherichia coli
brenda
Lacourciere, G.M.; Stadtman, T.C.
Catalytic properties of selenophosphate synthetases: comparison of the selenocysteine-containing enzyme from Haemophilus influenzae with the corresponding cysteine-containing enzyme from Escherichia coli
Proc. Natl. Acad. Sci. USA
96
44-48
1999
Escherichia coli, Haemophilus influenzae
brenda
Mullins, L.S.; Hong, S.B.; Gibson, G.E.; Walker, H.; Stadtman, T.C.; Raushel, F.M.
Identification of a phosphorylated enzyme intermediate in the catalytic mechanism for selenophosphate synthetase
J. Am. Chem. Soc.
119
6684-6685
1997
Escherichia coli
-
brenda
Guimaraes, M.J.; Peterson, D.; Vicari, A.; Cocks, B.G.; Copeland, N.G.; Gilbert, D.J.; Jenkins, N.A.; Ferrick, D.A.; Kastelein, R.A.; Bazan, J.F.; Zlotnik, A.
Identification of a novel selD homolog from eukaryotes, bacteria, and archaea: Is there an autoregulatory mechanism in selenocysteine metabolism?
Proc. Natl. Acad. Sci. USA
93
15086-15091
1996
Haemophilus influenzae, Methanocaldococcus jannaschii, Mus musculus (P97364), Mus musculus, Homo sapiens (Q99611), Homo sapiens
brenda
Serras, F.; Morey, M.; Alsina, B.; Baguna, J.; Corominas, M.
The Drosophila selenophosphate synthetase (selD) gene is required for development and cell proliferation
Biofactors
14
143-149
2001
Drosophila melanogaster
brenda
Morey, M.; Serras, F.; Corominas, M.
Halving the selenophosphate synthetase gene dose confers hypersensitivity to oxidative stress in Drosophila melanogaster
FEBS Lett.
534
111-114
2003
Drosophila melanogaster
brenda
Jayakumar, P.C.; Musande, V.V.; Shouche, Y.S.; Patole, M.S.
The Selenophosphate synthetase gene from Leishmania major
DNA Seq.
15
66-70
2004
Leishmania major
brenda
Hirosawa-Takamori, M.; Jackle, H.; Vorbruggen, G.
The class 2 selenophosphate synthetase gene of Drosophila contains a functional mammalian-type SECIS
EMBO Rep.
1
441-446
2000
Drosophila melanogaster (Q9VKY8)
brenda
Wolfe, M.D.
Mechanistic insights revealed through characterization of a novel chromophore in selenophosphate synthetase from Escherichia coli
IUBMB Life
55
689-693
2003
Escherichia coli
brenda
Kim, T.S.; Yu, M.H.; Chung, Y.W.; Kim, J.; Choi, E.J.; Ahn, K.; Kim, I.Y.
Fetal mouse selenophosphate synthetase 2 (SPS2): biological activities of mutant forms in Escherichia coli
Mol. Cells
9
422-428
1999
Mus musculus
brenda
Jin, J.S.; Baek, S.; Lee, H.; Oh, M.Y.; Koo, Y.E.; Shim, M.S.; Kwon, S.Y.; Jeon, I.; Park, S.Y.; Baek, K.; Yoo, M.A.; Hatfield, D.L.; Lee, B.J.
A DNA replication-related element downstream from the initiation site of Drosophila selenophosphate synthetase 2 gene is essential for its transcription
Nucleic Acids Res.
32
2482-2493
2004
Drosophila melanogaster
brenda
Tamura, T.; Yamamoto, S.; Takahata, M.; Sakaguchi, H.; Tanaka, H.; Stadtman, T.C.; Inagaki, K.
Selenophosphate synthetase genes from lung adenocarcinoma cells: Sps1 for recycling L-selenocysteine and Sps2 for selenite assimilation
Proc. Natl. Acad. Sci. USA
101
16162-16167
2004
Homo sapiens
brenda
Ogasawara, Y.; Lacourciere, G.M.; Ishii, K.; Stadtman, T.C.
Characterization of potential selenium-binding proteins in the selenophosphate synthetase system
Proc. Natl. Acad. Sci. USA
102
1012-1016
2005
Haemophilus influenzae
brenda
Xu, X.M.; Carlson, B.A.; Irons, R.; Mix, H.; Zhong, N.; Gladyshev, V.N.; Hatfield, D.L.
Selenophosphate synthetase 2 is essential for selenoprotein biosynthesis
Biochem. J.
404
115-120
2007
Mus musculus, Mus musculus (P97364), Mus musculus (Q8BH69)
brenda
Chung, H.J.; Yoon, S.I.; Shin, S.H.; Koh, Y.A.; Lee, S.J.; Lee, Y.S.; Bae, S.
p53-mediated enhancement of radiosensitivity by selenophosphate synthetase 1 overexpression
J. Cell. Physiol.
209
131-141
2006
Homo sapiens
brenda
Zhang, C.; Meng, Q.; Gai, J.; Yu, D.
Cloning and functional characterization of an O-acetylserine(thiol)lyase-encoding gene in wild soybean (Glycine soja)
Mol. Biol. Rep.
35
527-534
2008
Bos taurus
brenda
Matsumoto, E.; Sekine, S.; Akasaka, R.; Otta, Y.; Katsura, K.; Inoue, M.; Kaminishi, T.; Terada, T.; Shirouzu, M.; Yokoyama, S.
Structure of an N-terminally truncated selenophosphate synthetase from Aquifex aeolicus
Acta Crystallogr. Sect. F
F64
453-458
2008
Aquifex aeolicus (O67139), Aquifex aeolicus
brenda
Gursinsky, T.; Groebe, D.; Schierhorn, A.; Jaeger, J.; Andreesen, J.R.; Soehling, B.
Factors and selenocysteine insertion sequence requirements for the synthesis of selenoproteins from a gram-positive anaerobe in Escherichia coli
Appl. Environ. Microbiol.
74
1385-1393
2008
Peptoclostridium acidaminophilum
brenda
Haft, D.H.; Self, W.T.
Orphan SelD proteins and selenium-dependent molybdenum hydroxylases
Biol. Direct
3
4
2008
Clostridioides difficile (Q182I1), Enterococcus faecalis, Escherichia coli, Haloarcula marismortui (Q5V6B2), Haloarcula marismortui
brenda
Xu, X.M.; Carlson, B.A.; Zhang, Y.; Mix, H.; Kryukov, G.V.; Glass, R.S.; Berry, M.J.; Gladyshev, V.N.; Hatfield, D.L.
New developments in selenium biochemistry: selenocysteine biosynthesis in eukaryotes and archaea
Biol. Trace Elem. Res.
119
234-241
2007
Mus musculus (P97364)
brenda
Abe, K.; Mihara, H.; Nishijima, Y.; Kurokawa, S.; Esaki, N.
Functional analysis of two homologous mouse selenophosphate synthetases
Biomed. Res. Trace Elem.
19
76-79
2008
Mus musculus (P97364)
-
brenda
Zhang, Y.; Turanov, A.A.; Hatfield, D.L.; Gladyshev, V.N.
In silico identification of genes involved in selenium metabolism: evidence for a third selenium utilization trait
BMC Genomics
9
251
2008
Enterococcus faecalis (Q831E4), Enterococcus faecalis, no activity in Methanosarcina acetivorans, no activity in Methanosarcina mazei, no activity in Pyrobaculum aerophilum, no activity in Pyrobaculum calidifontis, no activity in Thermotoga maritima
brenda
Pappas, A.C.; Zoidis, E.; Surai, P.F.; Zervas, G.
Selenoproteins and maternal nutrition
Comp. Biochem. Physiol. B
151
361-372
2008
Homo sapiens (Q99611)
brenda
Itoh, Y.; Sekine, S.I.; Matsumoto, E.; Akasaka, R.; Takemoto, C.; Shirouzu, M.; Yokoyama, S.
Structure of selenophosphate synthetase essential for selenium incorporation into proteins and RNAs
J. Mol. Biol.
385
1456-1469
2008
Aquifex aeolicus (O67139), Aquifex aeolicus
brenda
Sculaccio, S.A.; Rodrigues, E.M.; Cordeiro, A.T.; Magalhaes, A.; Braga, A.L.; Alberto, E.E.; Thiemann, O.H.
Selenocysteine incorporation in kinetoplastid: selenophosphate synthetase (SELD) from Leishmania major and Trypanosoma brucei
Mol. Biochem. Parasitol.
162
165-171
2008
Leishmania major (Q4Q0M0), Leishmania major, Trypanosoma brucei
brenda
Furumiya, K.; Kanaya, K.; Tanabe, K.; Tanaka, Y.; Mizutani, T.
Active bovine selenophosphate synthetase 2, not having selenocysteine
Mol. Biol. Rep.
35
541-549
2007
Bos taurus
brenda
Hoffmann, P.R.; Hoege, S.C.; Li, P.A.; Hoffmann, F.W.; Hashimoto, A.C.; Berry, M.J.
The selenoproteome exhibits widely varying, tissue-specific dependence on selenoprotein P for selenium supply
Nucleic Acids Res.
35
3963-3973
2007
Mus musculus (P97364), Mus musculus
brenda
Xu, X.; Carlson, B.A.; Mix, H.; Zhang, Y.; Saira, K.; Glass, R.S.; Berry, M.J.; Gladyshev, V.N.; Hatfield, D.L.
Biosynthesis of selenocysteine on its tRNA in eukaryotes
PLoS Biol.
5
96-105
2007
Caenorhabditis elegans, Escherichia coli, Mus musculus (P97364), Drosophila melanogaster (Q9VKY8)
-
brenda
Lobanov, A.V.; Hatfield, D.L.; Gladyshev, V.N.
Selenoproteinless animals: selenophosphate synthetase SPS1 functions in a pathway unrelated to selenocysteine biosynthesis
Protein Sci.
17
176-182
2008
no activity in Tribolium castaneum, no activity in Bombyx mori
brenda
Yoo, M.H.; Xu, X.M.; Turanov, A.A.; Carlson, B.A.; Gladyshev, V.N.; Hatfield, D.L.
A new strategy for assessing selenoprotein function: siRNA knockdown/knock-in targeting the 3'-UTR
RNA
13
921-929
2007
Mus musculus
brenda
Preabrazhenskaya, Y.V.; Kim, I.Y.; Stadtman, T.C.
Binding of ATP and its derivatives to selenophosphate synthetase from Escherichia coli
Biochemistry (Moscow)
74
910-916
2009
Escherichia coli
brenda
Shim, M.S.; Kim, J.Y.; Jung, H.K.; Lee, K.H.; Xu, X.M.; Carlson, B.A.; Kim, K.W.; Kim, I.Y.; Hatfield, D.L.; Lee, B.J.
Elevation of glutamine level by selenophosphate synthetase 1 knockdown induces megamitochondrial formation in Drosophila cells
J. Biol. Chem.
284
32881-32894
2009
Drosophila melanogaster
brenda
Wang, K.T.; Wang, J.; Li, L.F.; Su, X.D.
Crystal structures of catalytic intermediates of human selenophosphate synthetase 1
J. Mol. Biol.
390
747-759
2009
Homo sapiens (P49903), Homo sapiens
brenda
Kim, J.Y.; Lee, K.H.; Shim, M.S.; Shin, H.; Xu, X.M.; Carlson, B.A.; Hatfield, D.L.; Lee, B.J.
Human selenophosphate synthetase 1 has five splice variants with unique interactions, subcellular localizations and expression patterns
Biochem. Biophys. Res. Commun.
397
53-58
2010
Homo sapiens
brenda
Han, Y.H.; Zhang, Z.W.; Shao, C.; Li, S.; Xu, S.W.; Wang, X.L.
The expression of chicken selenoprotein W, selenocysteine-synthase (SecS), and selenophosphate synthetase-1 (SPS-1) in CHO-K1 cells
Biol. Trace Elem. Res.
148
61-68
2012
Gallus gallus
brenda
Lee, K.H.; Shim, M.S.; Kim, J.Y.; Jung, H.K.; Lee, E.; Carlson, B.A.; Xu, X.M.; Park, J.M.; Hatfield, D.L.; Park, T.; Lee, B.J.
Drosophila selenophosphate synthetase 1 regulates vitamin B6 metabolism: prediction and confirmation
BMC Genomics
12
426
2011
Drosophila melanogaster
brenda
Yeh, M.S.; Huang, C.J.; Guo, C.H.; Liu, K.F.; Tsai, I.H.; Cheng, W.
Identification and cloning of a selenophosphate synthetase (SPS) from tiger shrimp, Penaeus monodon, and its transcription in relation to molt stages and following pathogen infection
Dev. Comp. Immunol.
36
21-30
2012
Penaeus monodon (F5CBP8), Penaeus monodon
brenda
Noinaj, N.; Wattanasak, R.; Lee, D.Y.; Wally, J.L.; Piszczek, G.; Chock, P.B.; Stadtman, T.C.; Buchanan, S.K.
Structural insights into the catalytic mechanism of Escherichia coli selenophosphate synthetase
J. Bacteriol.
194
499-508
2012
Escherichia coli (P16456), Escherichia coli
brenda
Costa, F.C.; Oliva, M.A.; de Jesus, T.C.; Schenkman, S.; Thiemann, O.H.
Oxidative stress protection of Trypanosomes requires selenophosphate synthase
Mol. Biochem. Parasitol.
180
47-50
2011
Trypanosoma brucei (Q38A34), Trypanosoma brucei
brenda
Stock, T.; Selzer, M.; Rother, M.
In vivo requirement of selenophosphate for selenoprotein synthesis in archaea
Mol. Microbiol.
75
149-160
2010
Methanococcus maripaludis (P60820), Methanococcus maripaludis
brenda
Faim, L.M.; Rosa e Silva, I.; Bertacine Dias, M.V.; DMuniz Pereira, H.; Brandao-Neto, J.; Alves da Silva, M.T.; Thiemann, O.H.
Crystallization and preliminary X-ray diffraction analysis of selenophosphate synthetases from Trypanosoma brucei and Leishmania major
Acta Crystallogr. Sect. F
69
864-867
2013
Trypanosoma brucei brucei (Q38A34), Leishmania major (Q4Q0M0), Leishmania major, Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927 (Q38A34)
brenda
Tobe, R.; Carlson, B.A.; Huh, J.H.; Castro, N.P.; Xu, X.M.; Tsuji, P.A.; Lee, S.G.; Bang, J.; Na, J.W.; Kong, Y.Y.; Beaglehole, D.; Southon, E.; Seifried, H.; Tessarollo, L.; Salomon, D.S.; Schweizer, U.; Gladyshev, V.N.; Hatfield, D.L.; Lee, B.J.
Selenophosphate synthetase 1 is an essential protein with roles in regulation of redox homoeostasis in mammals
Biochem. J.
473
2141-2154
2016
Mus musculus (Q8BH69), Mus musculus, Mus musculus C57BL/6 (Q8BH69)
brenda
Kamada, S.; Okugochi, T.; Asano, K.; Tobe, R.; Mihara, H.; Nemoto, M.; Inagaki, K.; Tamura, T.
A non-radioactive assay for selenophosphate synthetase activity using recombinant pyruvate pyrophosphate dikinase from Thermus thermophilus HB8
Biosci. Biotechnol. Biochem.
80
1970-1972
2016
Homo sapiens (Q99611)
brenda
Mariotti, M.; Santesmasses, D.; Capella-Gutierrez, S.; Mateo, A.; Arnan, C.; Johnson, R.; D'Aniello, S.; Yim, S.H.; Gladyshev, V.N.; Serras, F.; Corominas, M.; Gabaldon, T.; Guigo, R.
Evolution of selenophosphate synthetases: emergence and relocation of function through independent duplications and recurrent subfunctionalization
Genome Res.
25
1256-1267
2015
Botryllus schlosseri, Caenorhabditis elegans (O62461), Ciona intestinalis, Drosophila melanogaster (O18373), Escherichia coli, Homo sapiens (Q99611), Molgula tectiformis, no activity in Acyrthosiphon pisum, no activity in Coleoptera, no activity in Drosophila willistoni, no activity in Endopterygota, no activity in Hymenoptera, no activity in Lepidoptera, Oikopleura dioica
brenda
Preobrazhenskaya, Y.V.; Stenko, A.I.; Shvarts, M.V.; Lugovtsev, V.Y.
Binding stoichiometry of a recombinant selenophosphate synthetase with one synonymic substitution E197D to a fluorescent nucleotide analog of ATP, TNP-ATP
J. Amino Acids
2013
983565
2013
Escherichia coli, Escherichia coli DH5alpha-T1 and BL21-Gold(DE3)
brenda
Fuessl, M.; Reinders, J.; Oefner, P.J.; Heinze, J.; Schrempf, A.
Selenophosphate synthetase in the male accessory glands of an insect without selenoproteins
J. Insect Physiol.
71
46-51
2014
Cardiocondyla obscurior
brenda
Li, G.; Liu, L.; Li, P.; Chen, L.; Song, H.; Zhang, Y.
Gene expression profiling of selenophosphate synthetase 2 knockdown in Drosophila melanogaster
Metallomics
8
354-365
2016
Drosophila melanogaster
brenda
Oudouhou, F.; Casu, B.; Dopgwa Puemi, A.S.; Sygusch, J.; Baron, C.
Analysis of Novel interactions between components of the selenocysteine biosynthesis pathway, SEPHS1, SEPHS2, SEPSECS, and SECp43
Biochemistry
56
2261-2270
2017
Homo sapiens (Q99611)
brenda
Na, J.; Jung, J.; Bang, J.; Lu, Q.; Carlson, B.A.; Guo, X.; Gladyshev, V.N.; Kim, J.; Hatfield, D.L.; Lee, B.J.
Selenophosphate synthetase 1 and its role in redox homeostasis, defense and proliferation
Free Radic. Biol. Med.
127
190-197
2018
Escherichia coli, Homo sapiens (Q99611), Homo sapiens
brenda
Scortecci, J.F.; Serrao, V.H.B.; Fernandes, A.F.; Basso, L.G.M.; Gutierrez, R.F.; Araujo, A.P.U.; Neto, M.O.; Thiemann, O.H.
Initial steps in selenocysteine biosynthesis The interaction between selenocysteine lyase and selenophosphate synthetase
Int. J. Biol. Macromol.
156
18-26
2020
Escherichia coli
brenda
Li, J.L.; Li, W.; Sun, X.T.; Xia, J.; Li, X.N.; Lin, J.; Zhang, C.; Sun, X.C.; Xu, S.W.
Selenophosphate synthetase 1 (SPS1) is required for the development and selenium homeostasis of central nervous system in chicken (Gallus gallus)
Oncotarget
8
35919-35932
2017
Gallus gallus (F1N876), Gallus gallus
brenda
da Silva, M.T.A.; Silva, I.R.E.; Faim, L.M.; Bellini, N.K.; Pereira, M.L.; Lima, A.L.; de Jesus, T.C.L.; Costa, F.C.; Watanabe, T.F.; Pereira, H.D.; Valentini, S.R.; Zanelli, C.F.; Borges, J.C.; Dias, M.V.B.; da Cunha, J.P.C.; Mittra, B.; Andrews, N.W.; Thiemann, O.H.
Trypanosomatid selenophosphate synthetase structure, function and interaction with selenocysteine lyase
PLoS Negl. Trop. Dis.
14
e0008091
2020
Trypanosoma cruzi, Trypanosoma brucei brucei (Q38A34), Leishmania major (Q4Q0M0), Leishmania major, Trypanosoma brucei brucei 927/4 GUTat10.1 (Q38A34)
brenda
McAllister, K.N.; Bouillaut, L.; Kahn, J.N.; Self, W.T.; Sorg, J.A.
Using CRISPR-Cas9-mediated genome editing to generate C. difficile mutants defective in selenoproteins synthesis
Sci. Rep.
7
14672
2017
Clostridioides difficile, Clostridioides difficile R20291
brenda