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  • Title: On the interaction site of serine acetyltransferase in the cysteine synthase complex from Escherichia coli.
    Author: Zhao C, Moriga Y, Feng B, Kumada Y, Imanaka H, Imamura K, Nakanishi K.
    Journal: Biochem Biophys Res Commun; 2006 Mar 24; 341(4):911-6. PubMed ID: 16442495.
    Abstract:
    Cysteine synthase from Escherichia coli is a bienzyme complex comprised of serine acetyltransferase (SAT) and O-acetylserine sulfhydrylase A. The site of interaction of a SAT molecule was investigated by gel chromatography and surface plasmon technique using various mutant-type SATs, to better understand the mechanism involved in complex formation. The C-terminus of SAT, Ile 273, along with Glu 268 and Asp 271, was found to be essential for complex formation. The effects of O-acetyl-L-serine and sulfide on the affinity for the complex formation were also studied using a surface plasmon technique.
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