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糖基自由基激活酶:结构、机制和底物相互作用。

Glycyl radical activating enzymes: structure, mechanism, and substrate interactions.

机构信息

Department of Chemistry & Biochemistry and the Astrobiology Biogeocatalysis Research Center, Montana State University, Bozeman, MT 59717, United States.

Department of Chemistry & Biochemistry and the Astrobiology Biogeocatalysis Research Center, Montana State University, Bozeman, MT 59717, United States.

出版信息

Arch Biochem Biophys. 2014 Mar 15;546:64-71. doi: 10.1016/j.abb.2014.01.020. Epub 2014 Jan 31.

Abstract

The glycyl radical enzyme activating enzymes (GRE-AEs) are a group of enzymes that belong to the radical S-adenosylmethionine (SAM) superfamily and utilize a [4Fe-4S] cluster and SAM to catalyze H-atom abstraction from their substrate proteins. GRE-AEs activate homodimeric proteins known as glycyl radical enzymes (GREs) through the production of a glycyl radical. After activation, these GREs catalyze diverse reactions through the production of their own substrate radicals. The GRE-AE pyruvate formate lyase activating enzyme (PFL-AE) is extensively characterized and has provided insights into the active site structure of radical SAM enzymes including GRE-AEs, illustrating the nature of the interactions with their corresponding substrate GREs and external electron donors. This review will highlight research on PFL-AE and will also discuss a few GREs and their respective activating enzymes.

摘要

甘氨酰基自由基酶激活酶(GRE-AE)属于自由基 S-腺苷甲硫氨酸(SAM)超家族的一组酶,利用[4Fe-4S]簇和 SAM 来催化其底物蛋白中的 H 原子的提取。GRE-AE 通过产生甘氨酰基自由基来激活称为甘氨酰基自由基酶(GRE)的同源二聚体蛋白。激活后,这些 GRE 通过产生自己的底物自由基来催化各种反应。甘氨酰基自由基酶激活酶(PFL-AE)已被广泛研究,并为包括 GRE-AE 在内的自由基 SAM 酶的活性位点结构提供了深入了解,说明了与相应的底物 GRE 和外部电子供体相互作用的性质。本综述将重点介绍 PFL-AE 的研究,并将讨论一些 GRE 及其各自的激活酶。

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