O-phospho-L-seryl-tRNASec:L-selenocysteinyl-tRNA synthase

O-phospho-L-seryl-tRNASec:L-selenocysteinyl-tRNA synthase

Selenocysteine synthase tetramer, Mus musculus
Identifiers
EC number 2.9.1.2
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

O-phospho-L-seryl-tRNASec:L-selenocysteinyl-tRNA synthase (EC 2.9.1.2, MMPSepSecS, SepSecS, SLA/LP, O-phosphoseryl-tRNA:selenocysteinyl-tRNA synthase, O-phospho-L-seryl-tRNA:L-selenocysteinyl-tRNA synthase) is an enzyme with systematic name selenophosphate:O-phospho-L-seryl-tRNASec selenium transferase.[1][2][3][4] This enzyme catalyses the following chemical reaction

O-phospho-L-seryl-tRNASec + selenophosphate L-selenocysteinyl-tRNASec + phosphate

This enzyme is pyridoxal-phosphate protein.

References

  1. Palioura, S.; Sherrer, R.L.; Steitz, T.A.; Soll, D.; Simonovic, M. (2009). "The human SepSecS-tRNASec complex reveals the mechanism of selenocysteine formation". Science. 325: 321–325. doi:10.1126/science.1173755. PMID 19608919.
  2. Araiso, Y.; Palioura, S.; Ishitani, R.; Sherrer, R.L.; O'Donoghue, P.; Yuan, J.; Oshikane, H.; Domae, N.; Defranco, J.; Soll, D.; Nureki, O. (2008). "Structural insights into RNA-dependent eukaryal and archaeal selenocysteine formation". Nucleic Acids Res. 36: 1187–1199. doi:10.1093/nar/gkm1122. PMID 18158303.
  3. Aeby, E.; Palioura, S.; Pusnik, M.; Marazzi, J.; Lieberman, A.; Ullu, E.; Soll, D.; Schneider, A. (2009). "The canonical pathway for selenocysteine insertion is dispensable in Trypanosomes". Proc. Natl. Acad. Sci. USA. 106: 5088–5092. doi:10.1073/pnas.0901575106. PMID 19279205.
  4. Yuan, J.; Palioura, S.; Salazar, J.C.; Su, D.; O'Donoghue, P.; Hohn, M.J.; Cardoso, A.M.; Whitman, W.B.; Soll, D. (2006). "RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea". Proc. Natl. Acad. Sci. USA. 103: 18923–18927. doi:10.1073/pnas.0609703104. PMC 1748153Freely accessible. PMID 17142313.
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