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Literature summary for 6.1.1.21 extracted from
- Influence of the conserved active site residues of histidyl tRNA synthetase on the mechanism of aminoacylation reaction (2011), Biophys. Chem., 158, 61-72.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required, binding structure, overview | Staphylococcus aureus |  |
| Mg2+ | required, binding structure, overview | Thermus thermophilus | |
| Mg2+ | required, binding structure, overview | Escherichia coli | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-histidine + tRNAHis | Staphylococcus aureus | - |
AMP + diphosphate + L-histidyl-tRNAHis | - |
? | |
| ATP + L-histidine + tRNAHis | Thermus thermophilus | - |
AMP + diphosphate + L-histidyl-tRNAHis | - |
? | |
| ATP + L-histidine + tRNAHis | Escherichia coli | - |
AMP + diphosphate + L-histidyl-tRNAHis | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
| Staphylococcus aureus | - |
- |
- |
| Thermus thermophilus | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 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 | |
| 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 | |
| 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 |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-histidine + tRNAHis | - |
Staphylococcus aureus | AMP + diphosphate + L-histidyl-tRNAHis | - |
? | |
| ATP + L-histidine + tRNAHis | - |
Thermus thermophilus | AMP + diphosphate + L-histidyl-tRNAHis | - |
? | |
| ATP + L-histidine + tRNAHis | - |
Escherichia coli | AMP + diphosphate + L-histidyl-tRNAHis | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| histidyl tRNA synthetase | - |
Staphylococcus aureus |
| histidyl tRNA synthetase | - |
Thermus thermophilus |
| histidyl tRNA synthetase | - |
Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Staphylococcus aureus | |
| ATP | - |
Thermus thermophilus | |
| ATP | - |
Escherichia coli | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
| 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 |
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