Lysine 194 Is Functional in Isocitrate Lyase from Escherichia coli

@article{Rehman1997Lysine1I,
  title={Lysine 194 Is Functional in Isocitrate Lyase from Escherichia coli},
  author={Abdur Rehman and Bruce A. McFadden},
  journal={Current Microbiology},
  year={1997},
  volume={35
},
  pages={14
-17
}
}
Abstract. Lysine 194 in conserved stretch 1 of tetrameric isocitrate lyase from Escherichia coli has been replaced by using the restriction-enzyme-site elimination method of directed mutagenesis. Expression of subunits of each variant and of wild-type (wt) enzyme was equivalent and all variants assembled into tetrameric proteins. The variants K194R and K194H had kcat values relative to that of wt enzyme taken as 100 of 11 and 7, respectively. Km values for Mg2+-Ds-isocitrate (in mM units) were… 
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