EC Number   |
Subunits |
Reference |
|---|
    1.13.11.31 | ? |
x * 60000-80000, SDS-PAGE |
686330 |
| 1.13.11.31 | ? |
x * 72000, SDS-PAGE |
395404, 395408 |
| 1.13.11.31 | ? |
x * 75000, SDS-PAGE, x * 75155, calculated from sequence |
764230 |
| 1.13.11.31 | ? |
x * 75000, SDS-PAGE, x * 75205, calculated from sequence |
764230 |
| 1.13.11.31 | ? |
x * 75305, calculation of nucleotide sequence |
395427 |
| 1.13.11.31 | ? |
x * 80000, SDS-PAGE, x * 79800, calculated from sequence, recombinant His-tagged protein |
765361 |
| 1.13.11.31 | dimer |
2 * 76500, recombinant His-tagged enzyme, SDS-PAGE |
688398 |
| 1.13.11.31 | dimer |
binding of allosteric effector [13(S)-hydroxyoctadeca-9(Z),11(E)-dienoic acid] shifts the monomer-dimer equilibrium toward dimer formation. Enzyme dimerization may protect the enzyme from kinetic substrate inhibition by shielding the hydrophobic alpha2 helixes |
728776 |
| 1.13.11.31 | dimer |
modeling of the protein dimer shows a TOP-to-TOP dimeric arrangement with the alpha-helices containing a Leu-rich region (L172, L183, L187, and L194). Four nonoverlapping peptides within helix alpha2 of the TOP subdomain of wild-type are stabilizing, consistent with the dimer interface |
764187 |
| 1.13.11.31 | monomer |
1 * 74700, dynamic light scattering |
701926 |
