Protein Hydroxylation Catalyzed by 2-Oxoglutarate-dependent Oxygenases.
Protein Hydroxylation Catalyzed by 2-Oxoglutarate-dependent Oxygenases.
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DOI：
10.1074/jbc.r115.662627
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发表时间：
2015-08-21
期刊：
影响因子：
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通讯作者：
Schofield CJ
中科院分区：
文献类型：
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作者：
Markolovic S;Wilkins SE;Schofield CJ
脯氨酰和赖氨酰残基的翻译后羟基化，由 2-酮戊二酸 (2OG) 依赖性加氧酶催化，首次在胶原蛋白生物合成中被发现。 2OG加氧酶还催化缺氧诱导因子的脯氨酰和天冬酰胺酰羟基化，这些因子在对缺氧的适应性反应中发挥重要作用。随后，它们被证明可以催化 Nϵ-甲基化组蛋白赖氨酰残基的 N-去甲基化（通过羟基化），以及多个其他残基的羟基化。最近的工作已经确定了 2OG 加氧酶在翻译相关蛋白修饰中的作用，在某些情况下，这些蛋白似乎从微生物到人类都是保守的。在这里，我们概述了 2OG 加氧酶催化的蛋白质羟基化，重点介绍了最新的发现。
The post-translational hydroxylation of prolyl and lysyl residues, as catalyzed by 2-oxoglutarate (2OG)-dependent oxygenases, was first identified in collagen biosynthesis. 2OG oxygenases also catalyze prolyl and asparaginyl hydroxylation of the hypoxia-inducible factors that play important roles in the adaptive response to hypoxia. Subsequently, they have been shown to catalyze N-demethylation (via hydroxylation) of Nϵ-methylated histone lysyl residues, as well as hydroxylation of multiple other residues. Recent work has identified roles for 2OG oxygenases in the modification of translation-associated proteins, which in some cases appears to be conserved from microorganisms through to humans. Here we give an overview of protein hydroxylation catalyzed by 2OG oxygenases, focusing on recent discoveries.