2.7.1.164: O-phosphoseryl-tRNASec kinase
This is an abbreviated version!
For detailed information about O-phosphoseryl-tRNASec kinase, go to the full flat file.
Word Map on EC 2.7.1.164
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2.7.1.164
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selenocysteine
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selenoproteins
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sep-trna:sec-trna
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selenophosphate
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jannaschii
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sepsecs
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decoding
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serylates
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ser-trnasec
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methanocaldococcus
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methanococcus
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anticodon
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aminoacylated
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trna-dependent
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selenide
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selenocysteine-specific
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selenocysteinyl-trna
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eukarya
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trnasersec
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aminoacyl-trnas
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maripaludis
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d-stem
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aa-trnas
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amidotransferases
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amppnp
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trnaser
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misacylated
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serrs
- 2.7.1.164
- selenocysteine
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selenoproteins
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sep-trna:sec-trna
- selenophosphate
- jannaschii
- sepsecs
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decoding
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serylates
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ser-trnasec
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methanocaldococcus
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methanococcus
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anticodon
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aminoacylated
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trna-dependent
- selenide
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selenocysteine-specific
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selenocysteinyl-trna
- eukarya
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trnasersec
- aminoacyl-trnas
- maripaludis
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d-stem
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aa-trnas
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amidotransferases
- amppnp
- trnaser
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misacylated
- serrs
Reaction
Synonyms
O-phosphoseryl-tRNA kinase, O-phosphoseryl-tRNA(Sec) kinase, O-phosphoseryl-tRNASec kinase, phosphoseryl-tRNASec kinase, phosphoseryl-tRNA[Ser]Sec kinase, PSTK, Tb10.6k15.1110, TbPSTK
ECTree
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General Information
General Information on EC 2.7.1.164 - O-phosphoseryl-tRNASec kinase
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malfunction
metabolism
physiological function
knockdown of TbPSTK impairs selenoprotein synthesis in the parasite procyclic form (PCF). TbPSTK and TbSEPSECS double-knockout cell lines demonstrate that Trypanosoma brucei parasite procyclic form does not depend on selenoproteins
malfunction
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knockdown of TbPSTK impairs selenoprotein synthesis in the parasite procyclic form (PCF). TbPSTK and TbSEPSECS double-knockout cell lines demonstrate that Trypanosoma brucei parasite procyclic form does not depend on selenoproteins
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the enzyme is involved in the selenocysteine incorporation pathway in this primitive eukaryote
metabolism
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the synthesis of selenocysteine, the 21st amino acid, occurs on its transfer RNA, tRNASec. tRNASec is initially aminoacylated with serine by seryl-tRNA synthetase and the resulting seryl moiety is converted to phosphoserine by O-phosphoseryl-tRNA kinase (PSTK) in eukaryotes. The selenium donor, selenophosphate is synthesized from selenide and ATP by selenophosphate synthetase. Selenocysteinyl-tRNA synthase (Sep-SecS) then uses the O-phosphoseryl-tRNASec and selenophosphate to form Sec-tRNASec in eukaryotes. Leishmania SepSecS enzyme is active and able to complement the DELTAselA deletion in Escherichia coli JS1 strain only in the presence of archaeal PSTK, indicating the conserved nature of the PSTK-SepSecS pathway, selenocysteinyl-tRNA synthase is dependent on the action of PSTK enzyme in the Sec insertion pathway
metabolism
selenocysteine biosynthesis and incorporation into selenoproteins require an intricate molecular machinery that is present, but not ubiquitous, in all domains of life. In eukaryotes it begins with tRNA[Ser]Sec acylation with L-serine by the seryl-tRNA synthetase (SerRS) followed by its conversion to Sec-tRNA[Ser]Sec, sequentially catalyzed by phosphoseryl-tRNASec kinase (PSTK) and Sec-tRNA[Ser]Sec synthase (SEPSECS). Selenophosphate synthetase (SEPHS) is a key enzyme in the Sec pathway, being responsible for catalyzing the formation of the active selenium donor for this reaction, selenophosphate, from selenide and ATP. Enzyme phosphoseryl-tRNASec kinase (PSTK) forms a stable complex with the Sec-tRNASec synthase (SEPSECS)
metabolism
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the enzyme is involved in the selenocysteine incorporation pathway in this primitive eukaryote
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metabolism
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the synthesis of selenocysteine, the 21st amino acid, occurs on its transfer RNA, tRNASec. tRNASec is initially aminoacylated with serine by seryl-tRNA synthetase and the resulting seryl moiety is converted to phosphoserine by O-phosphoseryl-tRNA kinase (PSTK) in eukaryotes. The selenium donor, selenophosphate is synthesized from selenide and ATP by selenophosphate synthetase. Selenocysteinyl-tRNA synthase (Sep-SecS) then uses the O-phosphoseryl-tRNASec and selenophosphate to form Sec-tRNASec in eukaryotes. Leishmania SepSecS enzyme is active and able to complement the DELTAselA deletion in Escherichia coli JS1 strain only in the presence of archaeal PSTK, indicating the conserved nature of the PSTK-SepSecS pathway, selenocysteinyl-tRNA synthase is dependent on the action of PSTK enzyme in the Sec insertion pathway
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metabolism
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selenocysteine biosynthesis and incorporation into selenoproteins require an intricate molecular machinery that is present, but not ubiquitous, in all domains of life. In eukaryotes it begins with tRNA[Ser]Sec acylation with L-serine by the seryl-tRNA synthetase (SerRS) followed by its conversion to Sec-tRNA[Ser]Sec, sequentially catalyzed by phosphoseryl-tRNASec kinase (PSTK) and Sec-tRNA[Ser]Sec synthase (SEPSECS). Selenophosphate synthetase (SEPHS) is a key enzyme in the Sec pathway, being responsible for catalyzing the formation of the active selenium donor for this reaction, selenophosphate, from selenide and ATP. Enzyme phosphoseryl-tRNASec kinase (PSTK) forms a stable complex with the Sec-tRNASec synthase (SEPSECS)
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the enzyme is involved in the biosynthesis of selenocysteine
physiological function
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the enzyme is essential in the selenocysteine insertion
physiological function
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the enzyme is involved in the biosynthesis of selenocysteine
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physiological function
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the enzyme is essential in the selenocysteine insertion
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