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

Glycyl radical activating enzymes: structure, mechanism, and substrate interactions.
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DOI:
10.1016/j.abb.2014.01.020
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发表时间:
2014-03-15
影响因子:
3.9
通讯作者:
Broderick, Joan B.
Broderick, Joan B.
中科院分区:
生物学3区
文献类型:
--
作者:
Shisler, Krista A.;Broderick, Joan B.

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甘氨酰自由基酶激活酶(glycyl radical enzyme activating enzymes,GRE-AEs)是一类属于自由基S-腺苷甲硫氨酸(SAM)超家族的酶,利用[4Fe-4S]簇和SAM催化H原子从其底物蛋白上的提取。GRE-AE通过产生甘氨酰自由基激活被称为甘氨酰自由基酶(GRES)的同型二聚体蛋白。活化后,这些GRES通过产生其自身的底物自由基催化不同的反应。的GRE-AE丙酮酸甲酸裂解酶激活酶(PFL-AE)的广泛的特点,并提供了深入了解自由基SAM酶,包括GRE-AE的活性位点结构,说明其相应的底物GRES和外部电子供体的相互作用的性质。本文将重点介绍PFL-AE的研究,并将讨论几个GREs及其各自的激活酶。
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.
自由基 SAM 酶进行甲基转移的结构基础。
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