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Literature summary extracted from

  • Banik, S.D.; Nandi, N.
    Influence of the conserved active site residues of histidyl tRNA synthetase on the mechanism of aminoacylation reaction (2011), Biophys. Chem., 158, 61-72.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.21 Mg2+ required, binding structure, overview Staphylococcus aureus
6.1.1.21 Mg2+ required, binding structure, overview Thermus thermophilus
6.1.1.21 Mg2+ required, binding structure, overview Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.21 ATP + L-histidine + tRNAHis Staphylococcus aureus
-
 AMP + diphosphate + L-histidyl-tRNAHis
-
 ?
6.1.1.21 ATP + L-histidine + tRNAHis Thermus thermophilus
-
 AMP + diphosphate + L-histidyl-tRNAHis
-
 ?
6.1.1.21 ATP + L-histidine + tRNAHis Escherichia coli
-
 AMP + diphosphate + L-histidyl-tRNAHis
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.21 Escherichia coli
-
-
-
6.1.1.21 Staphylococcus aureus
-
-
-
6.1.1.21 Thermus thermophilus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
6.1.1.21 ATP + L-histidine + tRNAHis = AMP + diphosphate + L-histidyl-tRNAHis relation between the conservation of active site residues and the molecular mechanism of aminoacylation reaction, relevant reaction coordinate and the orientation of the catalytic residue, Arg259, model of active site with the substrates, Mg2+ ions and water, overview. Calculation of the transition state structures of the activation step of aminoacylation reaction using the combined ab-initio/semi-empirical calculation Staphylococcus aureus
a
6.1.1.21 ATP + L-histidine + tRNAHis = AMP + diphosphate + L-histidyl-tRNAHis relation between the conservation of active site residues and the molecular mechanism of aminoacylation reaction, relevant reaction coordinate and the orientation of the catalytic residue, Arg259, model of active site with the substrates, Mg2+ ions and water, overview. Calculation of the transition state structures of the activation step of aminoacylation reaction using the combined ab-initio/semi-empirical calculation Thermus thermophilus
a
6.1.1.21 ATP + L-histidine + tRNAHis = AMP + diphosphate + L-histidyl-tRNAHis relation between the conservation of active site residues and the molecular mechanism of aminoacylation reaction, relevant reaction coordinate and the orientation of the catalytic residue, Arg259, model of active site with the substrates, Mg2+ ions and water, overview. Calculation of the transition state structures of the activation step of aminoacylation reaction using the combined ab-initio/semi-empirical calculation Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.21 ATP + L-histidine + tRNAHis
-
 Staphylococcus aureus AMP + diphosphate + L-histidyl-tRNAHis
-
 ?
6.1.1.21 ATP + L-histidine + tRNAHis
-
 Thermus thermophilus AMP + diphosphate + L-histidyl-tRNAHis
-
 ?
6.1.1.21 ATP + L-histidine + tRNAHis
-
 Escherichia coli AMP + diphosphate + L-histidyl-tRNAHis
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.1.1.21 histidyl tRNA synthetase
-
 Staphylococcus aureus
6.1.1.21 histidyl tRNA synthetase
-
 Thermus thermophilus
6.1.1.21 histidyl tRNA synthetase
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.21 ATP
-
 Staphylococcus aureus
6.1.1.21 ATP
-
 Thermus thermophilus
6.1.1.21 ATP
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
6.1.1.21 evolution the conserved active site residues near the reaction center, Thr60, Val62, Pro82, Glu83, Gly84, Arg113, Gln127, Arg259, Gly260, Leu261, Ala284 and Ala306, which have a major role in the reaction mechanism and catalysis, retain their specific position and orientation relative to the substrate in the three species, Escherichia coli, Thermus thermophilus, and Staphylococcus aureus, modelling, reaction emchanism, detailed overview Staphylococcus aureus
6.1.1.21 evolution the conserved active site residues near the reaction center, Thr60, Val62, Pro82, Glu83, Gly84, Arg113, Gln127, Arg259, Gly260, Leu261, Ala284 and Ala306, which have a major role in the reaction mechanism and catalysis, retain their specific position and orientation relative to the substrate in the three species, Escherichia coli, Thermus thermophilus, and Staphylococcus aureus, modelling, reaction emchanism, detailed overview Thermus thermophilus
6.1.1.21 evolution the conserved active site residues near the reaction center, Thr60, Val62, Pro82, Glu83, Gly84, Arg113, Gln127, Arg259, Gly260, Leu261, Ala284 and Ala306, which have a major role in the reaction mechanism and catalysis, retain their specific position and orientation relative to the substrate in the three species, Escherichia coli, Thermus thermophilus, and Staphylococcus aureus, modelling, reaction mechanism, detailed overview Escherichia coli