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Literature summary for 2.7.1.164 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
Search for more literature for 2.7.1.164

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Trypanosoma brucei brucei

Natural Substrates/ Products (Substrates)

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

Organism

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

Substrates and Products (Substrate)

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

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Trypanosoma brucei brucei

General Information

General Information Comment Organism
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
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