Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytoplasm | - |
Trypanosoma brucei brucei | 5737 | - |
additional information | subcellular localization and complex formation analysis of enzyme PSTK, overview | Trypanosoma brucei brucei | - |
- |
nucleus | - |
Trypanosoma brucei brucei | 5634 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Trypanosoma brucei brucei |
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 | - |
ADP + O-phospho-L-seryl-tRNASec | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Trypanosoma brucei brucei | Q38A45 | - |
- |
Trypanosoma brucei brucei 927/4 GUTat10.1 | Q38A45 | - |
- |
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 | 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 | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Trypanosoma brucei brucei |
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 |