EC Number   |
Subunits |
Reference |
|---|
    5.4.3.3 | ? |
x * 60000, gel filtration, sulfhydryl component, x * about approximately 150000, gel filtration, cobamide protein component |
3396 |
| 5.4.3.3 | heterodimer |
- |
714347 |
| 5.4.3.3 | heterotetramer |
alpha2beta2 |
702340, 747193 |
| 5.4.3.3 | heterotetramer |
alpha2beta2, subunits alpha and beta are encoded by genes kamD and kamE |
747510 |
| 5.4.3.3 | More |
protein KamDE comprised of the 30 and 51 kDa subunits of the E1 component of D-alpha-lysine aminomutase is catalytically active in absence of the third 12.8 kDa subunit, but ATP no longer has a regulatory effect on it. The S subunit of D-ornithine aminomutase, OraS, is capable of forming a complex with KamDE and restores the enzymes ATP-dependent allosteric regulation |
679913 |
| 5.4.3.3 | More |
the beta-Rossmann subunit binds dAdoCbl in a base-off mode with the axial 5,6-dimethylbenzimidazole ligand displaced by His133beta. The alpha-triosephosphate isomerase barrel binds pyridoxal 5'-phosphate, which is also covalently bound as a Schiff base (internal aldimine) to Lys144beta, forming a cross-link between the subunits. The distance between dAdoCbl and pyridoxal 5'-phosphate is 24 A. This configuration represents the open state of the enzyme |
747510 |
| 5.4.3.3 | More |
the enzyme comprises two protein components, the core enzyme E1 and an auxiliary activating protein E2. E1 is a 170 kDa heterotetramer composed of 55 kDa alpha-subunits and 30 kDa beta-subunits and formulated as alpha2beta2, whereas the molecular mass of E2 is about 80 kDa. E2 shows dAdoCbl synthetase activity when isolated separately. A large-scale domain movement is required for interconversion between the catalytically inactive open form and the catalytically active closed form |
727644 |
| 5.4.3.3 | tetramer |
2 * 32000 + 2 * 52000, SDS-PAGE |
3397 |
| 5.4.3.3 | tetramer |
2 * 55000, alpha-subunit + 2 * 300000, beta-subunit, alpha2beta2 |
727644 |
| 5.4.3.3 | tetramer |
alpha2,beta2, 2 * 55000 + 2 * 30000, SDS-PAGE |
651982 |
