关于大肠杆菌半胱氨酸合酶复合物中丝氨酸乙酰转移酶的相互作用位点。
On the interaction site of serine acetyltransferase in the cysteine synthase complex from Escherichia coli.
作者信息
Zhao Chunhui, Moriga Yudai, Feng Bin, Kumada Yoichi, Imanaka Hiroyuki, Imamura Koreyoshi, Nakanishi Kazuhiro
机构信息
Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University, 3-1-1 Tsushima-naka, Okayama 700-8530, Japan.
出版信息
Biochem Biophys Res Commun. 2006 Mar 24;341(4):911-6. doi: 10.1016/j.bbrc.2006.01.054. Epub 2006 Jan 23.
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.
来自大肠杆菌的半胱氨酸合酶是一种双酶复合物，由丝氨酸乙酰转移酶（SAT）和O-乙酰丝氨酸巯基酶A组成。为了更好地理解复合物形成所涉及的机制，使用各种突变型SAT通过凝胶色谱法和表面等离子体技术研究了SAT分子的相互作用位点。发现SAT的C末端Ile 273以及Glu 268和Asp 271对于复合物的形成至关重要。还使用表面等离子体技术研究了O-乙酰-L-丝氨酸和硫化物对复合物形成亲和力的影响。
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