Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-isoleucine + tRNAIle | Escherichia coli | - |
AMP + diphosphate + L-isoleucyl-tRNAIle | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-isoleucine + tRNAIle | - |
Escherichia coli | AMP + diphosphate + L-isoleucyl-tRNAIle | - |
? | |
ATP + L-isoleucine + tRNAIle | a two-step reaction, the first of which, the amino acid activation step, is reversible, while the second aminoacylation step is not, the amino acid editing site for LeuRS resides within the homologous CP1 domain containing a conserved threonine conferring amino acid substrate recognition, editing mechanism, some positions of the site are idiosyncratic to IleRS, residues Arg249, Asp251, Thr252, Met336, and Val338 are involved,overview | Escherichia coli | AMP + diphosphate + L-isoleucyl-tRNAIle | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the amino acid editing site for IleRS resides within the homologous CP1 domain: threonine-rich peptide and a second conserved GTG region that are separated by about 100 amino acids comprise parts of the hydrolytic editing site, comparison to LeuRS, some positions of the site are idiosyncratic to IleRS, tertiary and primary structure analysis of the amino acid editing site, overview | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
IleRS | - |
Escherichia coli |
Isoleucyl-tRNA synthetase | - |
Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Escherichia coli |