Abstract
Directed mutagenesis and molecular modelling have been used to identify a set of amino-acid side chains in glutathione reductase that confer specificity for the coenzyme NADP+. Systematic replacement of these amino acids, all of which occur in a 'fingerprint' structural motif in the NADP+-binding domain, leaves the substrate specificity unchanged but converts the enzyme into one displaying a marked preference for the coenzyme NAD+.
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Scrutton, N., Berry, A. & Perham, R. Redesign of the coenzyme specificity of a dehydrogenase by protein engineering. Nature 343, 38–43 (1990). https://doi.org/10.1038/343038a0
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DOI: https://doi.org/10.1038/343038a0
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