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 no.2.9.1.2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

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 RL, Steitz TA, Söll D, Simonovic M (July 2009). "The human SepSecS-tRNASec complex reveals the mechanism of selenocysteine formation". Science. 325 (5938): 321–5. Bibcode:2009Sci...325..321P. doi:10.1126/science.1173755. PMC 2857584. PMID 19608919.
  2. ^ Araiso Y, Palioura S, Ishitani R, Sherrer RL, O'Donoghue P, Yuan J, Oshikane H, Domae N, Defranco J, Söll D, Nureki O (March 2008). "Structural insights into RNA-dependent eukaryal and archaeal selenocysteine formation". Nucleic Acids Research. 36 (4): 1187–99. doi:10.1093/nar/gkm1122. PMC 2275076. PMID 18158303.
  3. ^ Aeby E, Palioura S, Pusnik M, Marazzi J, Lieberman A, Ullu E, Söll D, Schneider A (March 2009). "The canonical pathway for selenocysteine insertion is dispensable in Trypanosomes". Proceedings of the National Academy of Sciences of the United States of America. 106 (13): 5088–92. Bibcode:2009PNAS..106.5088A. doi:10.1073/pnas.0901575106. PMC 2664009. PMID 19279205.
  4. ^ Yuan J, Palioura S, Salazar JC, Su D, O'Donoghue P, Hohn MJ, Cardoso AM, Whitman WB, Söll D (December 2006). "RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea". Proceedings of the National Academy of Sciences of the United States of America. 103 (50): 18923–7. Bibcode:2006PNAS..10318923Y. doi:10.1073/pnas.0609703104. PMC 1748153. PMID 17142313.