Redesign of the coenzyme specificity of a dehydrogenase by protein engineering

Nigel S. Scrutton; Alan Berry; Richard N. Perham

Redesign of the coenzyme specificity of a dehydrogenase by protein engineering

Nigel S. Scrutton, Alan Berry, Richard N. Perham

Research output: Contribution to journal › Article › peer-review

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+.

Original language	English
Pages (from-to)	38-43
Number of pages	5
Journal	Nature
Volume	343
Issue number	6253
Publication status	Published - 4 Jan 1990

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title = "Redesign of the coenzyme specificity of a dehydrogenase by protein engineering",

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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T1 - Redesign of the coenzyme specificity of a dehydrogenase by protein engineering

AU - Scrutton, Nigel S.

AU - Berry, Alan

AU - Perham, Richard N.

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N2 - 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+.

AB - 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+.

M3 - Article

SN - 0028-0836

VL - 343

SP - 38

EP - 43

JO - Nature

JF - Nature

IS - 6253

ER -

Redesign of the coenzyme specificity of a dehydrogenase by protein engineering

Abstract

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