Mutagenesis of the phosphate‐binding pocket of KDPG aldolase enhances selectivity for hydrophobic substrates

Narrow substrate specificities often limit the use of enzymes in biocatalysis. To further the development of Escherichia coli 2‐keto‐3‐deoxy‐6‐phosphogluconate (KDPG) aldolase as a biocatalyst, the molecular determinants of substrate specificity were probed by mutagenesis. Our data demonstrate that...

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Veröffentlicht in:	Protein science 2007-11, Vol.16 (11), p.2368-2377
Hauptverfasser:	Cheriyan, Manoj, Toone, Eric J., Fierke, Carol A.
Format:	Artikel
Sprache:	eng
Schlagworte:	active site Aldehyde-Lyases - chemistry Aldehyde-Lyases - metabolism aldolase Aminoglycosides - chemistry Binding Sites biocatalysis Catalysis directed evolution Escherichia coli Escherichia coli - metabolism Hydro-Lyases - chemistry KDPG Kinetics Models, Chemical Models, Molecular Molecular Conformation Mutagenesis Mutagenesis, Site-Directed Mutation nikkomycin Phosphates - chemistry protein engineering Protein Engineering - methods rational redesign Substrate Specificity
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