Accessibility of N-acyl-D-mannosamines to N-acetyl-D-neuraminic acid aldolase.
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.
Pan
Yanbin
Y
Department of Chemistry, Case Western Reserve University, 10900 Euclid Avenue, Cleveland, OH 44106, USA.
Ayani
Tiffany
T
Nadas
Janos
J
Wen
Shouming
S
Guo
Zhongwu
Z
D002236:Carbohydrate Conformation; D005634:Fructose-Bisphosphate Aldolase / Q000737:chemistry*; D006595:Hexosamines / Q000138:chemical synthesis* / Q000737:chemistry; D009438:Neuraminic Acids / Q000138:chemical synthesis* / Q000737:chemistry; D013997:Time Factors
D006595:Hexosamines; D009438:Neuraminic Acids; C008322:mannosamine; D005634:Fructose-Bisphosphate Aldolase