EC Number | Cloned (Comment) | Organism |
---|---|---|
2.5.1.47 | expressed in Escherichia coli as a His-tagged fusion protein | Glycine max |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.5.1.47 | 67600 | - |
calculated from cDNA | Glycine max |
2.5.1.47 | 70000 | - |
gel filtration | Glycine max |
2.5.1.47 | 74200 | - |
sedimentation equilibrium ultracentrifugation | Glycine max |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.5.1.47 | Glycine max | Q8W1A0 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.5.1.47 | purified using nickel-affinity and gel filtration. Thrombin digestion is used to remove the His tag from each protein | Glycine max |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.5.1.47 | homodimer | gel filtration | Glycine max |
2.5.1.47 | More | a cysteine synthase complex is formed by association of serine O-acetyltransferase (SAT) and O-acetylserine sulfhydrylase (OASS). Biophysical examination cysteine synthase complex by gel filtration and sedimentation ultracentrifugation indicates that this assembly consists of a single serine O-trimer and three OASS dimers | Glycine max |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.5.1.47 | O-acetylserine sulfhydrylase | - |
Glycine max |
2.5.1.47 | OASS | - |
Glycine max |