| Literature DB >> 16442495 |
Chunhui Zhao1, Yudai Moriga, Bin Feng, Yoichi Kumada, Hiroyuki Imanaka, Koreyoshi Imamura, Kazuhiro Nakanishi.
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.Entities:
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Year: 2006 PMID： 16442495 DOI： 10.1016/j.bbrc.2006.01.054
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575