Refine search

Search Reaction

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 2 of 2
EC Number
O-phospho-L-seryl-tRNASec + selenophosphate + H2O = L-selenocysteinyl-tRNASec + 2 phosphate
O-phospho-L-seryl-tRNASec + selenophosphate + H2O = L-selenocysteinyl-tRNASec + 2 phosphate
proposed pyridoxal 5'-phosphate mechanism of L-phosphoseryl-tRNA to L-selenocysteinyl-tRNA conversion: the reaction begins by the covalently attached O-phospho-L-serine being brought into the proximity of the Schiff base when L-phosphoseryl-tRNASec binds to the enzyme. The amino group of O-phospho-L-serine can then attack the Schiff base formed between Lys284 and pyridoxal 5'-phosphate, which yields an external aldimine. The reoriented side chain of Lys284 abstracts the Calpha proton from O-phospho-L-serine, and the electron delocalization by the pyridine ring assists in rapid beta-elimination of the phosphate group, which produces an intermediate dehydroalanyl-tRNASec. After phosphate dissociation and binding of selenophosphate, the concomitant attack of water on the selenophosphate group and of the nucleophilic selenium onto the highly reactive dehydroalanyl moiety yield an oxidized form of L-phosphoseryl-tRNASec. The protonated Lys284, returns the proton to the Calpha carbon and then attacks pyridoxal 5'-phosphate to form an internal aldimine. Finally, Sec-tRNASec is released from the active site
Results 1 - 2 of 2