EC Number   |
Subunits |
Reference |
|---|
    2.5.1.17 | ? |
x * 19230, recombinant enzyme with a 6His-tag, matrix-assisted laser desorption ionization-time-of-flight mass spectroscopy. The 6His-tagged recombinant enzyme can exist as an oligomer in SDS-PAGE |
-, 682763 |
| 2.5.1.17 | ? |
x * 36812, sequence calculation, full length enzyme |
659058 |
| 2.5.1.17 | dimer |
2 * 25000, SDS-PAGE |
636871 |
| 2.5.1.17 | dimer |
2 * 28000, SDS-PAGE |
636868 |
| 2.5.1.17 | homodimer |
2 * 30000, SDS-PAGE |
-, 738536 |
| 2.5.1.17 | More |
approximate molecular weight of full length and truncated mutants |
659058 |
| 2.5.1.17 | More |
each subunit is composed of a bundle of 5 alpha-helices, the active site lies at the junction between the subunits |
652541 |
| 2.5.1.17 | More |
structural comparisons between apo BcPduO and BcPduO in complex with MgATP reveal that the N-terminal strands of both structures are ordered, which is in contrast with the most previously available PduO-type adenosyltransferase structures. Apo BcPduO is bound to additional dioxane molecules causing a side chain conformational change at the Tyr30 residue, which is an important residue that mediates hydrogen bonding with ATP molecules upon binding of cobalamin to the active site |
721492 |
| 2.5.1.17 | trimer |
- |
652541 |
| 2.5.1.17 | trimer |
3 * 20000, revealed by size-exclusion chromatography and crystal structure analysis |
682763 |
