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Literature summary for 6.1.1.11 extracted from

  • McClendon, C.L.; Vaidehi, N.; Kam, V.W.; Zhang, D.; Goddard, W.A.
    Fidelity of seryl-tRNA synthetase to binding of natural amino acids from HierDock first principles computations (2006), Protein Eng. Des. Sel., 19, 195-203.
    View publication on PubMed
Search for more literature for 6.1.1.11

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure analysis for identification of the amino acid substrate discrimination mechanism Thermus thermophilus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information calculated binding energies in the activated mode agrees with kinetic measurements of a covalent bond between the amino acid and ATP, quantitative computational analysis of amino acid binding, overview Saccharomyces cerevisiae
additional information
-
 additional information calculated binding energies in the activated mode agrees with kinetic measurements of a covalent bond between the amino acid and ATP, quantitative computational analysis of amino acid binding, overview Thermus thermophilus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Saccharomyces cerevisiae
Mg2+
-
 Thermus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-serine + tRNASer Saccharomyces cerevisiae
-
 AMP + diphosphate + L-seryl-tRNASer
-
 ?
ATP + L-serine + tRNASer Thermus thermophilus
-
 AMP + diphosphate + L-seryl-tRNASer
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-
Thermus thermophilus P34945
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-serine + tRNASer
-
 Saccharomyces cerevisiae AMP + diphosphate + L-seryl-tRNASer
-
 ?
ATP + L-serine + tRNASer
-
 Thermus thermophilus AMP + diphosphate + L-seryl-tRNASer
-
 ?
ATP + L-serine + tRNASer formation of a seryl adenylate intermediate, mechanism of discrimination between cognate and noncognate amino acids, quantitative computational analysis, overview Saccharomyces cerevisiae AMP + diphosphate + L-seryl-tRNASer
-
 ?
ATP + L-serine + tRNASer formation of a seryl adenylate intermediate, mechanism of discrimination between cognate and noncognate amino acids, quantitative computational analysis, overview Thermus thermophilus AMP + diphosphate + L-seryl-tRNASer
-
 ?
additional information threonine will compete with serine for formation of the activated intermediate while alanine and glycine will not compete significantly, overview, binding of ATP or seryl adenylate leads to the stabilization of a motif 2 loop that interacts with the tRNA acceptor stem Thermus thermophilus ?
-
 ?
additional information threonine will compete with serine for formation of the activated intermediate while alanineand glycine will not compete significantly, overview Saccharomyces cerevisiae ?
-
 ?

Synonyms

Synonyms Comment Organism
SerRS
-
 Saccharomyces cerevisiae
SerRS
-
 Thermus thermophilus
Seryl-tRNA synthetase
-
 Saccharomyces cerevisiae
Seryl-tRNA synthetase
-
 Thermus thermophilus

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Saccharomyces cerevisiae
ATP binding of ATP leads to the stabilization of a motif 2 loop that interacts with the tRNA acceptor stem Thermus thermophilus