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Literature summary for 2.9.1.1 extracted from

  • Forchhammer, K.; Böck, A.
    Selenocysteine synthase from Escherichia coli. Analysis of the reaction sequence (1991), J. Biol. Chem., 266, 6324-6328.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-Seryl-tRNASec + selenophosphate Escherichia coli the enzyme is involved in the biosynthesis of selenocysteine ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
L-seryl-tRNASec + selenophosphate = L-selenocysteinyl-tRNASec + phosphate the formyl group of pyridoxal phosphate forms a Schiff base with the alpha-amino group of L-Ser with the subsequent 2,3-elimination of a water molecule and the generation of an aminoacrylyl-tRNASecUCA intermediate Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Seryl-tRNASec + selenophosphate
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Escherichia coli L-Selenocysteinyl-tRNASec + H2O + phosphate
-
?
L-Seryl-tRNASec + selenophosphate the enzyme is involved in the biosynthesis of selenocysteine Escherichia coli ?
-
?

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate enzyme contains pyridoxal-phosphate Escherichia coli