Abstract
N-Acetyl- d-neuraminic acid (NeuNAc) aldolase is an important enzyme for the metabolic engineering of cell-surface NeuNAc using chemically modified d-mannosamines. To explore the optimal substrates for this application, eight N-acyl derivatives of d-mannosamine were prepared, and their accessibility to NeuNAc aldolase was quantitatively investigated. The N-propionyl-, N-butanoyl-, N- iso-butanoyl-, N-pivaloyl-, and N-phenylacetyl- d-mannosamines proved to be as good substrates as, or even better than, the natural N-acetyl- d-mannosamine, while the N-trifluoropropionyl and benzoyl derivatives were poor. It was proposed that the electronic effects might have a significant influence on the enzymatic aldol condensation reaction of d-mannosamine derivatives, with electron-deficient acyl groups having a negative impact. The results suggest that N-propionyl-, N-butanoyl-, N- iso-butanoyl-, and N-phenylacetyl- d-mannosamines may be employed to bioengineer NeuNAc on cells.
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