Control of radical chemistry in the AdoMet radical enzymes

被引：54

作者：

Duschene, Kaitlin S. ^{[1
]}

Veneziano, Susan E. ^{[1
]}

Silver, Sunshine C. ^{[1
]}

Broderick, Joan B. ^{[1
]}

机构：

[1] Montana State Univ, Dept Chem & Biochem, Bozeman, MT 59717 USA

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 2009年 / 13卷 / 01期

关键词：

LYASE ACTIVATING ENZYME; PYRUVATE FORMATE-LYASE; SPORE PHOTOPRODUCT LYASE; CLUSTER BINDING-SITES; IRON-SULFUR CENTER; S-ADENOSYLMETHIONINE; BIOTIN SYNTHASE; LYSINE 2,3-AMINOMUTASE; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI;

D O I：

10.1016/j.cbpa.2009.01.022

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The radical AdoMet superfamily comprises a diverse set of >2800 enzymes that utilize iron-sulfur clusters and S-adenosylmethionine (SAM or AdoMet) to initiate a diverse set of radical-mediated reactions. The intricate control these enzymes exercise over the radical transformations they catalyze is an amazing feat of elegance and sophistication in biochemistry. This review focuses on the accumulating evidence for how these enzymes control this remarkable chemistry, including controlling the reactivity between the iron-sulfur cluster and AdoMet, and controlling the subsequent radical transformations.

引用

页码：74 / 83

页数：10

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