N-酰基-D-甘露糖胺对N-乙酰-D-神经氨酸醛缩酶的可及性。
Accessibility of N-acyl-D-mannosamines to N-acetyl-D-neuraminic acid aldolase.
作者信息
Pan Yanbin, Ayani Tiffany, Nadas Janos, Wen Shouming, Guo Zhongwu
机构信息
Department of Chemistry, Case Western Reserve University, 10900 Euclid Avenue, Cleveland, OH 44106, USA.
出版信息
Carbohydr Res. 2004 Aug 23;339(12):2091-100. doi: 10.1016/j.carres.2004.05.028.
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.
N-乙酰-D-神经氨酸（NeuNAc）醛缩酶是利用化学修饰的D-甘露糖胺对细胞表面NeuNAc进行代谢工程改造的一种重要酶。为了探索该应用的最佳底物，制备了8种D-甘露糖胺的N-酰基衍生物，并对它们被NeuNAc醛缩酶作用的情况进行了定量研究。结果表明，N-丙酰基-、N-丁酰基-、N-异丁酰基-、N-新戊酰基-和N-苯乙酰基-D-甘露糖胺是与天然N-乙酰-D-甘露糖胺一样好甚至更好的底物，而N-三氟丙酰基和苯甲酰基衍生物则较差。研究提出，电子效应可能对D-甘露糖胺衍生物的酶促醛醇缩合反应有显著影响，缺电子的酰基具有负面影响。结果表明，N-丙酰基-、N-丁酰基-、N-异丁酰基-和N-苯乙酰基-D-甘露糖胺可用于在细胞上对NeuNAc进行生物工程改造。
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