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Literature summary for 6.1.1.11 extracted from

  • Borel, F.; Vincent, C.; Leberman, R.; Härtlein, M.
    Seryl-tRNA synthetase from Escherichia coli: implication of its N-terminal domain in aminoacylation activity and specificity (1994), Nucleic Acids Res., 22, 2963-2969.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.11

Protein Variants

Protein Variants Comment Organism
SerRSDELTA35-97 truncated mutants with a deletion of the N-terminal arm of the enzyme: SerRSDELTA35-97 and SerRSDELTA56-72. Both mutant have lost their specificity for tRNASer and charge also non-cognate type 1 tRNAs. The deletion has no effect on the amino acid activation step of the reaction, but reduces aminoacylation activity dramatically Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.000068
-
 ATP seryl-AMP formation, wild-type enzyme Escherichia coli
0.00034
-
 Ser seryl-AMP formation, wild-type enzyme Escherichia coli
0.00056
-
 tRNASer aminoacylation, wild-type enzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 wild-type and truncated mutants with a deletion of the N-terminal arm of the enzyme: SerRSDELTA35-97 and SerRSDELTA56-72
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and mutant enzymes Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-serine + tRNASer
-
 Escherichia coli AMP + diphosphate + L-seryl-tRNASer
-
 ?