PMID:9462957
| Citation |
Rehman, A and McFadden, BA (1997) Cysteine 195 has a critical functional role in catalysis by isocitrate lyase from Escherichia coli. Curr. Microbiol. 35:267-9 |
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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Cysteine 195 in isocitrate lyase from Escherichia coli has been replaced by directed mutagenesis.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 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. |
| Links | |
| Keywords |
Alanine/genetics; Amino Acid Sequence; Amino Acid Substitution; Cysteine/genetics; Escherichia coli/enzymology; Escherichia coli/genetics; Glycine/genetics; Isocitrate Lyase/genetics; Isocitrate Lyase/metabolism; Molecular Sequence Data; Mutagenesis, Site-Directed; Plasmids; Sequence Alignment; Sequence Analysis; Sequence Homology, Amino Acid; Serine/genetics; Threonine/genetics; Valine/genetics |
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