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Cysteine 195 Has a Critical Functional Role in Catalysis by Isocitrate Lyase from Escherichia coli

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Abstract.

Cysteine 195 in isocitrate lyase from Escherichia coli has been replaced by directed mutagenesis. Substitution by Ser yields enzyme with a kcat that is 0.03% that of wild type, and substitution by Ala, Gly, Thr, or Val yields completely inactive enzyme. The present results are consistent with a functional role of Cys 195.

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Authors and Affiliations

  1. Department of Biochemistry and Biophysics, P.O. Box 644660, Washington State University, Pullman, WA 99164-4660, USA , , , , , , US

    Abdur Rehman & Bruce A. McFadden

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  1. Abdur Rehman
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  2. Bruce A. McFadden
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Received: 26 March 1997 / Accepted: 29 April 1997

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Rehman, A., McFadden, B. Cysteine 195 Has a Critical Functional Role in Catalysis by Isocitrate Lyase from Escherichia coli . Curr Microbiol 35, 267–269 (1997). https://doi.org/10.1007/s002849900251

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  • DOI: https://doi.org/10.1007/s002849900251

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