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- W2004809453 abstract "D-Glyceraldehyde is accepted as an electrophile by 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase (EC 4.1.2.14) at 1% the rate of natural substrate, D-glyceraldehyde 3-phosphate. Accordingly, it was expected that addition of a phosphate moiety at C3 or C4 of unnatural aldehydes would enhance their activity as electrophilic substrates. Furthermore, phosphate would act as a useful protecting group during synthetic manipulations of the aldol adduct. A variety of phosphorylated and non-phosphorylated aldehydes were synthesized and evaluated as substrates for KDPG aldolase. Although small variations in reaction rate were observed, phosphorylation failed to provide a universal rate enhancement. Evaluation of substrate kinetic parameters revealed that the high rate of reaction of D-glyceraldehyde 3-phosphate compared to related electrophiles is entirely due to the efficiency of turnover with little change in binding exhibited among various substrates." @default.
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- W2004809453 date "1998-01-01" @default.
- W2004809453 modified "2023-10-16" @default.
- W2004809453 title "Effect of phosphorylation on the reaction rate of unnatural electrophiles with 2-keto-3-deoxy-6-phosphogluconate aldolase" @default.
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- W2004809453 doi "https://doi.org/10.1039/a706764j" @default.
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