EC Number | Crystallization (Comment) | Organism |
---|---|---|
6.1.1.4 | crystal and cocrystal structures for LeuRS, IleRS, and ValRS suggests that the CP1 domain rotates via its flexible beta-strand linkers relative to the main body along various steps in the enzymes reaction pathway. Computational analysis suggested that the end of the N-terminal beta-strand acted as a hinge. A molecular hinge might specifically direct movement of the CP1 domain relative to the main body | Escherichia coli |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
6.1.1.4 | Mg2+ | - |
Escherichia coli |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.1.1.4 | Escherichia coli | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.1.1.4 | ATP + L-isoleucine + tRNALeu | - |
Escherichia coli | AMP + diphosphate + L-isoleucyl-tRNALeu | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
6.1.1.4 | leucyl-tRNA ligase | - |
Escherichia coli |
6.1.1.4 | LeuRS | - |
Escherichia coli |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
6.1.1.4 | 7.5 | - |
assay at | Escherichia coli |