On the interaction site of serine acetyltransferase in the cysteine synthase complex from Escherichia coli.
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.
Zhao
Chunhui
C
Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University, 3-1-1 Tsushima-naka, Okayama 700-8530, Japan.
Moriga
Yudai
Y
Feng
Bin
B
Kumada
Yoichi
Y
Imanaka
Hiroyuki
H
Imamura
Koreyoshi
K
Nakanishi
Kazuhiro
K
D001665:Binding Sites; D002850:Chromatography, Gel; D003547:Cysteine Synthase / Q000737:chemistry / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D009097:Multienzyme Complexes / Q000737:chemistry* / Q000187:drug effects; D012694:Serine / Q000031:analogs & derivatives / Q000494:pharmacology; D051050:Serine O-Acetyltransferase / Q000737:chemistry* / Q000235:genetics; D020349:Surface Plasmon Resonance
D009097:Multienzyme Complexes; D012694:Serine; D051050:Serine O-Acetyltransferase; D003547:Cysteine Synthase; C043943:O-acetylserine