On the interaction site of serine acetyltransferase in the cysteine synthase complex from Escherichia coli.
Biochem. Biophys. Res. Commun.2006 Mar 24;341(4):911-6. Epub 2006 Jan 23
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摘要
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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基因功能
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原始数据
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文献解读
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