Journal
CARBOHYDRATE RESEARCH
Volume 339, Issue 12, Pages 2091-2100Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.carres.2004.05.028
Keywords
N-acyl-D-mannosamine; N-acetyl-D-mannosamine; N-acetyl-D-neuraminic acid; sialic acid; aldolase
Funding
- NCI NIH HHS [R01 CA095142-01, R01 CA095142, R01 CA095142-02, 1R01 CA95142, R01 CA095142-03, R01 CA095142-04] Funding Source: Medline
Ask authors/readers for more resources
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 NcuNAc 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-isobutanoyl-, and N-phenylacetyl-D-mannosamines may be employed to bioengineer NeuNAc on cells. (C) 2004 Elsevier Ltd. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available