EC Number   |
Subunits |
Reference |
|---|
   4.3.1.7 | dimer |
1 * 32000 + 1 * 49100 |
704185 |
| 4.3.1.7 | dodecamer |
6 * 35200 + 6 * 56900, the small subunit seems to be responsible for cobalamin binding, SDS-PAGE |
34377 |
| 4.3.1.7 | dodecamer |
alpha6beta6, 6 * 35000 + 6 * 50000, SDS-PAGE |
34384 |
| 4.3.1.7 | heterodecamer |
alphabeta, 6*49000, 6*32000, SDS-PAGE |
704362 |
| 4.3.1.7 | hexamer |
functional protein is a hexamer of alpha-beta-dimers (alpha-subunit of 50000 Da and beta-subunit of 31000 Da) |
690905 |
| 4.3.1.7 | oligomer |
8-10 * 57000, equilibrium sedimentation after treatment with guanidinium hydrochloride |
34370 |
| 4.3.1.7 | oligomer |
EutB and EutC monomers form the EutB-EutC heterodimer. Two heterodimers form a (EutB-EutC)2 homodimer, and three (EutB-EutC)2 homodimers form the biologically active oligomer. The model predicts that (EutB2)3 oligomer assembly occurs from isolated EutB, and that this hexameric structure templates the formation of the complete, native [(EutB-EutC)2]3 oligomer |
729228 |
| 4.3.1.7 | oligomer |
Two subunits are present in a EutB6EutC6 stoichiometry, EAL is composed of a 453-residue EutB protein subunit and a 286-residue EutC protein subunit, which are coded by the eutb and eutc genes. The positive charge at the terminus of the R160 side chain of EutB is required to achieve the native EutB protein fold and the oligomeric structure of EAL |
690960 |
| 4.3.1.7 | oligomer |
x * 36000 + x * 51000, the 2 subunits are probably present in equimolar proportions, SDS-PAGE |
34381 |
| 4.3.1.7 | trimer |
determination by gel filtration, freshly prepared protein oligomerizes readily into trimers in the presence or absence of 5 mM beta-mercaptoethanol, monomer consists of 219-amino-acids |
690280 |
