FeII/α-ketoglutarate hydroxylases involved in nucleobase, nucleoside, nucleotide, and chromatin metabolism

被引：48

作者：

Simmons, Jana M. ^{[1
]}

Mueller, Tina A. ^{[2
]}

Hausinger, Robert P. ^{[1
,2
,3
]}

机构：

[1] Michigan State Univ, Dept Biochem & Mol Biol, E Lansing, MI 48824 USA

[2] Michigan State Univ, Dept Microbiol & Mol Genet, E Lansing, MI 48824 USA

[3] Michigan State Univ, Quantitat Biol Program, E Lansing, MI 48824 USA

来源：

DALTON TRANSACTIONS | 2008年 / 38期

关键词：

D O I：

10.1039/b803512a

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

Fe-II/alpha-ketoglutarate-dependent hydroxylases uniformly possess a double-stranded beta-helix fold with two conserved histidines and one carboxylate coordinating their mononuclear ferrous ions. Oxidative decomposition of the alpha-keto acid is proposed to generate a ferryl-oxo intermediate capable of hydroxylating unactivated carbon atoms in a myriad of substrates. This Perspective focuses on a subgroup of these enzymes that are involved in pyrimidine salvage, purine decomposition, nucleoside and nucleotide hydroxylation, DNA/RNA repair, and chromatin modification. The varied reaction schemes are presented, and selected structural and kinetic information is summarized.

引用

页码：5132 / 5142

页数：11

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