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  • Metal Selectivity of the Escherichia coli Nickel Metallochaperone, SlyD
    [作者:Kaluarachchi, H; Siebel, JF; Kaluarachchi-Duffy, S; Krecisz, S; Sutherland, DEK; Stillman, MJ; Zamble, DB,期刊:Biochemistry, 页码:10666-10677 , 文章类型: Article,,卷期:2011年50-49]
  • SlyD is a Ni(II)-binding protein that contributes to nickel homeostasis in Escherichia coli. The C-terminal I domain of SlyD contains a rich variety of metal-binding amino acids, suggesting broader metal binding capabili...
  • Substrate Recognition by beta-Ketoacyl-ACP Synthases
    [作者:Borgaro, JG; Chang, A; Machutta, CA; Zhang, XJ; Tonge, PJ,期刊:Biochemistry, 页码:10678-10686 , 文章类型: Article,,卷期:2011年50-49]
  • beta-Ketoacyl-ACP synthase (KAS) enzymes catalyze Claisen condensation reactions in the fatty acid biosynthesis pathway. These reactions follow a ping-pong mechanism in which a donor substrate acylates the active site cy...