Rehman A, McFadden B A
Department of Biochemistry and Biophysics, Washington State University, Pullman 99164-4660, USA.
Curr Microbiol. 1997 Nov;35(5):267-9. doi: 10.1007/s002849900251.
Cysteine 195 in isocitrate lyase from Escherichia coli has been replaced by directed mutagenesis. Substitution by Ser yields enzyme with a k(cat) 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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