Transketolase - Aldolase Symbiosis for the Stereoselective Preparation of Aldoses and Ketoses of Biological Interest
Transketolase - Aldolase Symbiosis for the Stereoselective Preparation of Aldoses and Ketoses of Biological Interest
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DOI：
10.1002/adsc.201700209
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发表时间：
2017-06
影响因子：
5.4
通讯作者：
C. Guérard‐Hélaine;M. E. S. Moreira;Nadia Touisni;L. Hecquet;M. Lemaire;V. Hélaine
中科院分区：
文献类型：
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作者：
C. Guérard‐Hélaine;M. E. S. Moreira;Nadia Touisni;L. Hecquet;M. Lemaire;V. Hélaine
以转酮醇酶（TK）为生物催化剂制备醛糖酶亲电试剂制备具有生物学意义的单糖。不同寻常的是，TK是在合成途径中实现的，如在代谢中，即没有使用特殊设计的亲核试剂，如羟丙酮酸来改变平衡。不同寻常的是，甲醛被作为一般的TK受体底物来生成醛。结果表明，该方法具有推广意义，可以成功地改变底物和醛缩酶，并与其他酶结合，实现四种酶的一锅一步绿色级联反应，具有原子经济性。此外，还开发了新的检测方法来监测反应的进展和评估合成产物的纯度。
Transketolase (TK) was used as biocatalyst to produce useful aldoses as aldolase electrophiles to prepare monosaccharides of biological interest. Unconventionally, TK was implemented in a synthetic pathway, as in metabolism, ie without using a specially designed nucleophile such as hydroxypyruvate to shift the equilibrium. Unusually, formaldehyde was taken as the general TK acceptor substrate to generate aldehydes. Here was demonstrated that this method can be generalized: the substrates and the aldolase were successfully varied, coupled with other enzymes in a one-pot one-step green cascade reaction process involving four enzymes with atom economy. In addition, new assays were developed for both monitoring the progress of the reactions and assessing the purity of the synthesized products.