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Literature summary for 2.9.1.2 extracted from

  • Araiso, Y.; Palioura, S.; Ishitani, R.; Sherrer, R.L.; O'Donoghue, P.; Yuan, J.; Oshikane, H.; Domae, N.; Defranco, J.; Söll, D.; Nureki, O.
    Structural insights into RNA-dependent eukaryal and archaeal selenocysteine formation (2008), Nucleic Acids Res., 36, 1187-1199.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.9.1.2

Cloned(Commentary)

Cloned (Comment) Organism
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 Methanococcus maripaludis

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting-drop vapor diffusion method at 20°C, crystal structure of the enzyme complexed with pyridoxal 5'-phosphate at 2.5 A resolution Methanococcus maripaludis

Protein Variants

Protein Variants Comment Organism
H166A the mutant is partially active in forming Sec-tRNASec in vivo. In vitro, the mutant is partially active in forming Cys-tRNASec Methanococcus maripaludis
H166F mutant is inactive in vivo Methanococcus maripaludis
H166Q mutant is inactive in vivo Methanococcus maripaludis
R307A the mutant is significantly less active in L-selenocysteinyl-tRNASec formation in vivo and Cys-tRNASec formation in vitro Methanococcus maripaludis
R72A the mutant enzyme is significantly less active in L-selenocysteinyl-tRNASec formation in vivo and Cys-tRNASec formation in vitro. The mutant enzyme is unable to form L-selenocysteinyl-tRNASec in vitro Methanococcus maripaludis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
O-phospho-L-seryl-tRNASec + selenophosphate Methanococcus maripaludis the micronutrient selenium is present in proteins as selenocysteine. In eukaryotes and archaea, selenocysteine is formed in a tRNA-dependent conversion of O-phosphoserine by O-phosphoseryltRNA:selenocysteinyl-tRNA synthase L-selenocysteinyl-tRNASec + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Methanococcus maripaludis Q6LZM9
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-

Purification (Commentary)

Purification (Comment) Organism
recombinent enzyme Methanococcus maripaludis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
O-phospho-L-seryl-tRNASec + selenophosphate
-
 Methanococcus maripaludis L-selenocysteinyl-tRNASec + phosphate
-
 ?
O-phospho-L-seryl-tRNASec + selenophosphate the micronutrient selenium is present in proteins as selenocysteine. In eukaryotes and archaea, selenocysteine is formed in a tRNA-dependent conversion of O-phosphoserine by O-phosphoseryltRNA:selenocysteinyl-tRNA synthase Methanococcus maripaludis L-selenocysteinyl-tRNASec + phosphate
-
 ?

Subunits

Subunits Comment Organism
tetramer a member of the Fold Type I pyridoxal 5'-phosphate enzyme family, forms an (alpha2)2 homotetramer through its N-terminal extension. The active site lies on the dimer interface with each monomer contributing essential residues Methanococcus maripaludis

Synonyms

Synonyms Comment Organism
MMPSepSecS
-
 Methanococcus maripaludis
O-phosphoseryl-tRNA:selenocysteinyl-tRNA synthase
-
 Methanococcus maripaludis
SepSecS
-
 Methanococcus maripaludis

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate pyridoxal 5'-phosphate is covalently bound to the conserved Lys278 Methanococcus maripaludis