EC Number   |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Reference |
|---|
    6.1.1.4 | -999 |
- |
a series of molecular modeling studies including homology modeling and automated docking simulations are carried out. A 3D structure of Escherichia coli LeuRS is constructed via homology modling using the X-ray structure of Thermus thermophilus as a template because the LeuRS structure of Escherichia coli is not available from X-ray or NMR studies |
663351 |
| 6.1.1.4 | 33500 |
- |
recombinant beta-subunit, gel filtration |
652320 |
| 6.1.1.4 | 34000 |
- |
x * 34000, N-terminal peptide after cleavage of peptide bond E292-A293, SDS-PAGE, x * 63000, C-terminal peptide after cleavage of peptide bond E292-A293, SDS-PAGE, x * 97300, recombinant wild-type enzyme, SDS-PAGE |
649867 |
| 6.1.1.4 | 35000 |
- |
heterodimer in quartenary structure, 2 * 35000, leuS gene product or beta-subunit, + 2 * 65000, leuS gene product or alpha-subunit, SDS-PAGE |
649605 |
| 6.1.1.4 | 35000 |
- |
heterodimer in quartenary structure, 2 * 35000, leuS gene product, + 2 * 65000, leuS gene product, SDS-PAGE |
651299 |
| 6.1.1.4 | 63000 |
- |
2 * 63000, gel electrophoresis, after dissociation, the enzyme exhibits an equilibrium between an active dimeric form and an inactive monomeric form |
274 |
| 6.1.1.4 | 63000 |
- |
x * 34000, N-terminal peptide after cleavage of peptide bond E292-A293, SDS-PAGE, x * 63000, C-terminal peptide after cleavage of peptide bond E292-A293, SDS-PAGE, x * 97300, recombinant wild-type enzyme, SDS-PAGE |
649867 |
| 6.1.1.4 | 65000 |
- |
heterodimer in quartenary structure, 2 * 35000, leuS gene product or beta-subunit, + 2 * 65000, leuS gene product or alpha-subunit, SDS-PAGE |
649605 |
| 6.1.1.4 | 65000 |
- |
heterodimer in quartenary structure, 2 * 35000, leuS gene product, + 2 * 65000, leuS gene product, SDS-PAGE |
651299 |
| 6.1.1.4 | 74000 |
- |
1 * 74000, alpha-subunit, + 1 * 33500, beta-subunit, SDS-PAGE |
652320 |
