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Literature summary for 6.1.1.21 extracted from
- The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase (1997), Proc. Natl. Acad. Sci. USA, 8, 7144-7149.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure of enzyme-substrate complex with histidyl-tRNA synthetase, ATP, and the amino acid analog histidinyl | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| R259H | mutant Arg259His, with 1000fold decreased second order rate constant kcat/Km for the ATP-diphosphate exchange, and 500fold decreased kcat/Km for aminoacylation | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
wild-type and mutant Arg259His | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-histidine + tRNAHis | - |
Escherichia coli | AMP + diphosphate + L-histidyl-tRNAHis | - |
? |  |
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Release 2023.1 (January 2023)
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