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Literature summary extracted from

  • da Silva, M.; E. Silva, I.; Faim, L.; Bellini, N.; Pereira, M.; Lima, A.; de Jesus, T.; Costa, F.; Watanabe, T.; Pereira, H.; Valentini, S.; Zanelli, C.; Borges, J.; Dias, M.; da Cunha, J.; Mittra, B.; Andrews, N.; Thiemann, O.
    Trypanosomatid selenophosphate synthetase structure, function and interaction with selenocysteine lyase (2020), PLoS Negl. Trop. Dis., 14, 1-31 .
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.1.164 cytoplasm
-
 Trypanosoma brucei brucei 5737
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2.7.1.164 additional information subcellular localization and complex formation analysis of enzyme PSTK, overview Trypanosoma brucei brucei
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2.7.1.164 nucleus
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 Trypanosoma brucei brucei 5634
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Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.164 Mg2+ required Trypanosoma brucei brucei

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.164 ATP + L-seryl-tRNASec Trypanosoma brucei brucei
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 ADP + O-phospho-L-seryl-tRNASec
-
 ?
2.7.1.164 ATP + L-seryl-tRNASec Trypanosoma brucei brucei 927/4 GUTat10.1
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 ADP + O-phospho-L-seryl-tRNASec
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.164 Trypanosoma brucei brucei Q38A45
-
-
2.7.1.164 Trypanosoma brucei brucei 927/4 GUTat10.1 Q38A45
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-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.164 ATP + L-seryl-tRNASec
-
 Trypanosoma brucei brucei ADP + O-phospho-L-seryl-tRNASec
-
 ?
2.7.1.164 ATP + L-seryl-tRNASec
-
 Trypanosoma brucei brucei 927/4 GUTat10.1 ADP + O-phospho-L-seryl-tRNASec
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.1.164 phosphoseryl-tRNASec kinase
-
 Trypanosoma brucei brucei
2.7.1.164 PSTK
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 Trypanosoma brucei brucei
2.7.1.164 Tb10.6k15.1110 locus name Trypanosoma brucei brucei
2.7.1.164 TbPSTK
-
 Trypanosoma brucei brucei

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.164 ATP
-
 Trypanosoma brucei brucei

General Information

EC Number General Information Comment Organism
2.7.1.164 malfunction 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 Trypanosoma brucei brucei
2.7.1.164 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) Trypanosoma brucei brucei