O-phospho-L-seryl-tRNASec:L-selenocysteinyl-tRNA synthase
| O-phospho-L-seryl-tRNASec:L-selenocysteinyl-tRNA synthase | |||||||||
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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 | ||||||||
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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
- ↑ 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. PMC 2857584
. PMID 19608919. doi:10.1126/science.1173755. - ↑ 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. PMC 2275076 . PMID 18158303. doi:10.1093/nar/gkm1122.
- ↑ 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. PMC 2664009 . PMID 19279205. doi:10.1073/pnas.0901575106.
- ↑ 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. PMC 1748153 . PMID 17142313. doi:10.1073/pnas.0609703104.
External links
- O-phospho-L-seryl-tRNASec:L-selenocysteinyl-tRNA synthase at the US National Library of Medicine Medical Subject Headings (MeSH)
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