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Updated: Jul 15, 2026

The Multifaceted Benefits of Protein Co-expression in Escherichia coli
Published on: February 5, 2015
One protein, two enzymes
Y Dai1, P C Wensink, R H Abeles
1Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02453-2728, USA.
Abstract:
Two enzymes, designated, E-2 and E-2', catalyze different oxidation reactions of an aci-reductone intermediate in the methionine salvage pathway. E-2 and E-2', overproduced in Escherichia coli from the same gene, have the same protein component. E-2 and E-2' are separable on an anion exchange column or a hydrophobic column. Their distinct catalytic and chromatographic properties result from binding different metals. The apo-enzyme, obtained after metal is removed from either enzyme, is catalytically inactive. Addition of Ni2+ or Co2+ to the apo-protein yields E-2 activity. E-2' activity is obtained when Fe2+ is added. Production in intact E. coli of E-2 and E-2' depends on the availability of the corresponding metals. These observations suggest that the metal component dictates reaction specificity.
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