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- W2020451806 abstract "Six enantiomerically pure myo-inositol-monophosphates, including four deoxygenated analogues, have been synthesized by employing catalytic asymmetric phosphorylation methodology. These compounds were then evaluated as substrates for the direct interrogation of the stereospecificity of enzyme−substrate interactions with two inositol-monophosphatases (IMPases), one of which (from Archaeoglobus fulgidus) is characterized by an X-ray crystal structure with its substrate (d-I-1P) bound. The kinetic results lead to the finding that certain hydroxyl group contacts are actually destabilizing, while others have little effect. These new probes also allow a prediction of the active site binding mode of the substrate for the Escherichia coli IMPase for which no crystal structure exists." @default.
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- W2020451806 date "2004-11-02" @default.
- W2020451806 modified "2023-10-09" @default.
- W2020451806 title "Chemistry and Biology of Deoxy-<i>myo</i>-inositol Phosphates: Stereospecificity of Substrate Interactions within an Archaeal and a Bacterial IMPase" @default.
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- W2020451806 doi "https://doi.org/10.1021/ja047360x" @default.
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