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The effect of replacing the conserved active-site residues His-264, Asp-312 and Arg-314 on the binding and catalytic properties of Escherichia coli citrate synthase.

The first step in the overall catalytic mechanism of citrate synthase is the binding and polarization of oxaloacetate. Active-site residues Arg-314, Asp-312 and His-264 in Escherichia coli citrate synthase, which are involved in oxaloacetate binding, were converted by site-directed mutagenesis to Gl...

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Autors principals: Man, W J, Li, Y, O'Connor, C D, Wilton, D C
Format: Artigo
Idioma:Inglês
Publicat: 1994
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Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC1138232/
https://ncbi.nlm.nih.gov/pubmed/8010958
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