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Literature summary 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

Crystallization (Commentary)

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.11 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
6.1.1.11 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

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

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.11 Saccharomyces cerevisiae
-
-
-
6.1.1.11 Thermus thermophilus P34945
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.11 ATP + L-serine + tRNASer
-
 Saccharomyces cerevisiae AMP + diphosphate + L-seryl-tRNASer
-
 ?
6.1.1.11 ATP + L-serine + tRNASer
-
 Thermus thermophilus AMP + diphosphate + L-seryl-tRNASer
-
 ?
6.1.1.11 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
-
 ?
6.1.1.11 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
-
 ?
6.1.1.11 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 ?
-
 ?
6.1.1.11 additional information threonine will compete with serine for formation of the activated intermediate while alanineand glycine will not compete significantly, overview Saccharomyces cerevisiae ?
-
 ?

Synonyms

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

Cofactor

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