EC Number   |
Subunits |
Reference |
|---|
    2.3.1.57 | ? |
x * ? + x * 13000, catalytic subunit, at least 2 subunits, gel filtration of enzyme precipitated by (NH4)2SO4 |
487259 |
| 2.3.1.57 | dimer |
2 * 60000, SDS-PAGE |
487257, 487258 |
| 2.3.1.57 | dimer |
two dimer conformations are observed: a symmetric form with two open surface channels capable of binding substrate or cofactor, and an asymmetric form in which only one of the surface channels appears capable of binding and acetylating polyamines |
676840 |
| 2.3.1.57 | dodecamer |
12 * 21900, X-ray crystallography |
755723 |
| 2.3.1.57 | dodecamer |
substrate-induced allosteric change of quaternary structure of spermidine N-acetyltransferase SpeG, overview. The enzyme possesses unique open dodecameric state exists in solution |
-, 736641 |
| 2.3.1.57 | dodecamer |
three-dimensional structure in several ligand-free and ligand-bound structures, overview. The enzyme monomer has a mixed alpha/beta architecture |
-, 736639 |
| 2.3.1.57 | dodecamer |
X-ray crystallography, the dodecamer is organized as a hexamer of dimers |
-, 756930 |
| 2.3.1.57 | homodimer |
2 * 20000, subunit size of 171 amino acids |
487268 |
| 2.3.1.57 | homodimer |
structure analysis, overview |
701622 |
| 2.3.1.57 | More |
the enzyme occurs in open and closed conformations |
-, 736639 |
