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生物催化中的催化多效性:利用旧酶形成新键并遵循新途径。

Catalytic promiscuity in biocatalysis: using old enzymes to form new bonds and follow new pathways.

作者信息

Bornscheuer Uwe T, Kazlauskas Romas J

机构信息

Institute of Chemistry and Biochemistry, Department of Technical Chemistry and Biotechnology, Greifswald University, Soldmannstrasse 16, 17487 Greifswald, Germany.

出版信息

Angew Chem Int Ed Engl. 2004 Nov 19;43(45):6032-40. doi: 10.1002/anie.200460416.

DOI:10.1002/anie.200460416
PMID:15523680
Abstract

Biocatalysis has expanded rapidly in the last decades with the discoveries of highly stereoselective enzymes with broad substrate specificity. A new frontier for biocatalysis is broad reaction specificity, where enzymes catalyze alternate reactions. Although often under-appreciated, catalytic promiscuity has a natural role in evolution and occasionally in the biosynthesis of secondary metabolites. Examples of catalytic promiscuity with current or potential applications in synthesis are reviewed here. Combined with protein engineering, the catalytic promiscuity of enzymes may broadly extend their usefulness in organic synthesis.

摘要

在过去几十年中,随着具有广泛底物特异性的高度立体选择性酶的发现,生物催化迅速发展。生物催化的一个新前沿是广泛的反应特异性,即酶催化交替反应。尽管催化多效性常常未得到充分重视,但它在进化中以及偶尔在次级代谢产物的生物合成中具有天然作用。本文综述了在合成中具有当前或潜在应用的催化多效性实例。结合蛋白质工程,酶的催化多效性可能会广泛扩展其在有机合成中的用途。

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