EC Number   |
Subunits |
Reference |
|---|
    2.5.1.22 | ? |
x * 38998, calculated from amino acid sequence |
737608 |
| 2.5.1.22 | ? |
x * 39000, SDS-PAGE |
737608 |
| 2.5.1.22 | ? |
x * 39700, calculated |
689690 |
| 2.5.1.22 | dimer |
- |
708060 |
| 2.5.1.22 | dimer |
2 * 41000, each monomer has three domains: an N-terminal domain, which contains most of the dimer contacts; a central domain made up of four beta-strands that serves as a lid for the C-terminal domain, and a C-terminal catalytic domain |
708060 |
| 2.5.1.22 | dimer |
2 * 45000, kidney, SDS-PAGE |
489868 |
| 2.5.1.22 | dimer |
2 * 45000, SDS-PAGE |
489863, 489864 |
| 2.5.1.22 | homodimer |
- |
738421, 739338 |
| 2.5.1.22 | homodimer |
2 identical subunits, each monomer has 3 domains: a C-terminal domain, which contains the active site, a central domain made up of 4 beta-strands and an N-terminal domain with structural similarity to S-adenosylmethionine decarboxylase. Dimerization occurs mainly through interactions between the N-terminal domains. The structures provide an outline of the active site and a plausible model for catalysis. The active site is similar to those of spermidine synthases but has a larger substrate-binding pocket able to accommodate longer substrates. Asp201 and 276, conserved in aminopropyltransferases, play a key part in the catalytic mechanism. By separate expression of both domains, enzymes are inactive and possess rigid tertiary structure, suggesting that human SpmSyn is a fusion protein. |
692270 |
| 2.5.1.22 | homodimer |
x-ray crystallography |
739497 |
