Literature DB >> 9462957

Cysteine 195 has a critical functional role in catalysis by isocitrate lyase from Escherichia coli.

A Rehman1, B A McFadden.   

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Cysteine 195 in isocitrate lyase from Escherichia coli has been replaced by directed mutagenesis.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.

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Year:  1997        PMID： 9462957     DOI： 10.1007/s002849900251

Source DB:  PubMed          Journal:  Curr Microbiol        ISSN： 0343-8651            Impact factor:   2.188


  3 in total

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Journal:  J Bacteriol       Date:  2014-06-16       Impact factor: 3.490

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Authors:  T L Grimek; H Holden; I Rayment; J C Escalante-Semerena
Journal:  J Bacteriol       Date:  2003-08       Impact factor: 3.490

3.  Regulation by glutathionylation of isocitrate lyase from Chlamydomonas reinhardtii.

Authors:  Mariette Bedhomme; Mirko Zaffagnini; Christophe H Marchand; Xing-Huang Gao; Mathieu Moslonka-Lefebvre; Laure Michelet; Paulette Decottignies; Stéphane D Lemaire
Journal:  J Biol Chem       Date:  2009-10-21       Impact factor: 5.157
  3 in total

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