EC Number   |
Subunits |
Reference |
|---|
    4.1.1.18 | homodecamer |
a pentamer of homodimers, 10 * 82000, recombinant His6-tagged wild-type enzyme, SDS-PAGE |
-, 747369 |
| 4.1.1.18 | homodimer |
2 * 44000, recombinant His-tagged enzyme, SDS-PAGE |
749097, 749101 |
| 4.1.1.18 | monomer |
1 * 95000, SDS-PAGE |
37297 |
| 4.1.1.18 | More |
a mixture of dimers (about 158 kDa) and decamers (about 780 kDa) is present for the enzyme at pH 7.5. Decamers are dominant for AsLdc, dependent on the pH: the highest proportion of decamer for AsLdc (78%) is observed at pH 7.5, while it is reduced to 30% and 57% at pH 5.0 and pH 8.5, respectively |
748418 |
| 4.1.1.18 | More |
enzyme interacts strongly with regulatory ATPase variant A, RavA, forming a cage-like structure consisting of two enzyme decamers linked by up to five RavA oligomers. Enzyme activity is not affected by binding to RavA, but complex formation results in stimulation of RavA ATPase activity |
665713 |
| 4.1.1.18 | More |
SrLDC functions as a dimer and each monomer consists of two distinct domains, a pyridoxal 5'-phosphate-binding-barrel domain and a sheet domain. A shallow substrate-binding hole is formed at the interface between the sheet domains of two monomers |
749097 |
| 4.1.1.18 | More |
three-dimensional structure analysis of enzyme CadA, overview |
747396 |
| 4.1.1.18 | tetramer |
isozyme TT1887, crystallization data |
-, 666850 |
