EC Number   |
Subunits |
Reference |
|---|
    2.3.1.30 | monomer |
- |
705594 |
| 2.3.1.30 | trimer |
- |
719916 |
| 2.3.1.30 | monomer |
1 * 34400, SDS-PAGE |
705594 |
| 2.3.1.30 | monomer |
1 * 34800, SDS-PAGE |
705594 |
| 2.3.1.30 | tetramer |
2 * 34000, serine acetyltransferase + 2 * 36000, O-acetylserine (thiol) lyase, forming the cysteine synthase complex, SDS-PAGE |
486766 |
| 2.3.1.30 | trimer |
3 * x, predicted from homology modeling with Escherichia coli enzyme crystal structure |
-, 704098 |
| 2.3.1.30 | tetramer |
4 * 29261, ultracentrifugation, gel filtration, crystallographic data |
-, 486757 |
| 2.3.1.30 | More |
cysteine synthase from Escherichia coli is a bienzyme complex comprised of serine acetyltransferase and O-acetylserine sulfhydrylase A. The C-terminus of SAT, Ile273, along with Glu268 and Asp271, is essential for complex formation |
671743 |
| 2.3.1.30 | hexamer |
enzyme CysE has a trimer-trimer interface, two trimers are stacked on each other in head-to-head position through hydrophobic interactions at the N-terminus |
756960 |
| 2.3.1.30 | More |
enzyme exists in a high-molecular weight enzyme complex with cysteine synthase |
486755 |
