NAD(P)-Dependent 葡萄糖脱氢酶:被低估的多功能生物催化剂。

IF 2.6 4区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY
ChemBioChem Pub Date : 2024-11-12 DOI:10.1002/cbic.202400716
Guangde Jiang, Rohit Kumar, Samantha J Tambrini
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引用次数: 0

摘要

过去十年见证了生物催化领域的巨大进步。依赖 NAD(P)的葡萄糖脱氢酶(GDHs)是各种生物催化应用中最常用的酶之一。传统上,这些酶的作用是在利用葡萄糖的各种酶促反应中再生 NAD(P)H。然而,最近的研究已将 GDHs 的作用范围扩大到辅助因子再生之外,凸显了它们在各种化学转化中作为生物催化剂的潜力。GDHs 在催化合成各种药物分子和中间体的关键反应方面表现出了多功能性,包括酮还原生成醇、C=N 键的亚胺还原生成胺、醛还原成醇以及环己醇衍生物的脱氢反应。本综述重点介绍了在阐明依赖 NAD(P) 的葡萄糖脱氢酶(GDHs)在生物催化中的多功能作用方面取得的最新进展,并着重介绍了它们在小分子合成中不断增长的应用和巨大潜力。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
NAD(P)-Dependent Glucose Dehydrogenases: Underestimated Multifunctional Biocatalysts.

The last decade has witnessed tremendous progress in the field of biocatalysis. One of the most frequently utilized enzymes in diverse biocatalytic applications is NAD(P)-dependent glucose dehydrogenases (GDHs). Traditionally, these enzymes are employed for their role in regenerating NAD(P)H in various enzymatic reactions utilizing glucose. However, recent studies have expanded the scope of GDHs beyond cofactor regeneration, highlighting their potential as biocatalysts in diverse chemical transformations. GDHs have demonstrated versatility in catalyzing key reactions in the synthesis of various drug molecules and intermediates, including ketone reduction to produce alcohols, imine reduction of C=N bonds to yield amines, reduction of aldehydes to alcohols, and dehydrogenation of cyclohexanol derivatives. This review highlights recent advancements in elucidating the multifunctional roles of NAD(P)-dependent glucose dehydrogenases (GDHs) in biocatalysis, with an emphasis on their growing applications and significant potential in small molecule synthesis.

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来源期刊
ChemBioChem
ChemBioChem 生物-生化与分子生物学
CiteScore
6.10
自引率
3.10%
发文量
407
审稿时长
1 months
期刊介绍: ChemBioChem (Impact Factor 2018: 2.641) publishes important breakthroughs across all areas at the interface of chemistry and biology, including the fields of chemical biology, bioorganic chemistry, bioinorganic chemistry, synthetic biology, biocatalysis, bionanotechnology, and biomaterials. It is published on behalf of Chemistry Europe, an association of 16 European chemical societies, and supported by the Asian Chemical Editorial Society (ACES).
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