Lablog4-14:On the interaction site of serine acetyltransferase in the cysteine synthase complex from Escherichia coli

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Chunhui Zhao, Yudai Moriga, Bin Feng, Yoichi Kumada, Hiroyuki Imanaka, Koreyoshi Imamura, Kazuhiro Nakanishi

First author

Chunhui Zhao

Corresponding author

Kazuhiro Nakanishi

Publication Style

Journal name Biochemical and biophysical research communications


Volume, issue, pages

341(4) 911-6


 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.