EC Number   |
Subunits |
Reference |
|---|
    6.3.4.15 | ? |
x * 35000, recombinant enzyme, SDS-PAGE |
664436 |
| 6.3.4.15 | ? |
x * 73000, recombinant His9-tagged BPL, SDS-PAGE |
-, 690627 |
| 6.3.4.15 | ? |
x * about 35000, SDS-PAGE |
-, 728734 |
| 6.3.4.15 | dimer |
- |
672175 |
| 6.3.4.15 | dimer |
2 * 26000, calculated. Equilibrium analytical ultracentrifugation measurements performed on the apoenzyme and its complexes with biotin and bio-5'-AMP all yield molecular weights for the protein consistent with a dimer. Regardless of ligation state the Pyrococcus horikoshii enzyme is a dimer |
714197 |
| 6.3.4.15 | dimer |
2 * 26071 recombinant enzyme, SDS-PAGE and amino acid sequence calculation |
-, 663526 |
| 6.3.4.15 | dimer |
2 * 29500, SDS-PAGE and dynamic light scattering |
689712 |
| 6.3.4.15 | dimer |
dimerization upon biotin binding |
691104 |
| 6.3.4.15 | dimer |
the functional unit is a dimer, a subunit contains a catalytic N-terminal domain and a C-terminal domain, structure analysis |
-, 666059 |
| 6.3.4.15 | dimer |
the protein is a constitutive dimer, i.e. dimerises independently of biotin binding |
-, 691104 |
