Sevostyanova IA, et al. (2009) Cooperative binding of substrates to transketolase from Saccharomyces cerevisiae. Biochemistry (Mosc) 74(7):789-92
Abstract: Catalytic activity of two active sites of transketolase and their affinity towards the substrates (xylulose-5-phosphate and ribose-5-phosphate) has been studied in the presence of Ca2+ and Mg2+. In the presence of Ca2+, the active sites exhibit negative cooperativity in binding both xylulose-5-phosphate (donor substrate) and ribose-5-phosphate (acceptor substrate) and positive cooperativity in the catalytic transformation of the substrates. In the presence of Mg2+, nonequivalence of the active sites is not observed.
|Status: Published||Type: Journal Article | Research Support, Non-U.S. Gov't||PubMed ID: 19747100|
Topics addressed in this paper
Number of different genes curated to this paper: 2
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