in the complex between serine acetyltransferase and O-acetylserine sulfhydrolase, the C-terminal C10 peptide of serine acetyltransferase binds to the O-acetylserine sulfhydrolase homodimer in a 2:1 complex. Interaction between O-acetylserine sulfhydrolase and C10 peptide is tight over a range of temperature from 10°C to 35°C and NaCl concentrations from 0.02 M to 1.3 M. Binding displays negative cooperativity at higher temperatures, and the enthalpy of interaction has a significant temperature dependence. Hydrophobic interactions drive the formation of the O-acetylserine sulfhydrolase-C10 peptide complex
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
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
serine O-acetyltransferase and cysteine synthase form stable complexes containing two serine O-acetyltransferase trimers and two cysteine synthase dimers
serine O-acetyltransferase and cysteine synthase form stable complexes containing two serine O-acetyltransferase trimers and two cysteine synthase dimers
serine acetyltransferase (SAT, EC 2.3.1.30) and O-acetylserine thiol lyase reversibly form the heterooligomeric Cys synthase complex. SAT from Arabidopsis thaliana expressed in tobacco interacts with endogenous tobacco OAS-TL
at least tetramer, equilibrium between aggregated and disintegrated cysteine synthetase complex can be shifted by various effectors, has consequences for enzyme function, model of structural-functional relationships
all isoforms, but particularly isoenzyme 2 can form cysteine synthetase complex with serine acetyltransferase, as revealed by polyclonal antibody studies