Autocatalysed oxidative modifications to 2-oxoglutarate dependent oxygenases

作者：Mantri Monica; Zhang Zhihong; McDonough Michael A; Schofield Christopher J^*

来源：FEBS Journal, 2012, 279(9): 1563-1575.

DOI：10.1111/j.1742-4658.2012.08496.x

• ACCO
• auto-oxidation
• ethylene
• histone demethylases
• hypoxia
• JMJD6
• oxidative fragmentation
• reactive oxygen species
• RNA splicing
• self-hydroxylation
• 2-oxoglutarate oxygenase

Ferrous iron and 2-oxoglutarate-dependent oxygenases and related enzymes catalyse a range of oxidative reactions, possibly the widest of any enzyme family. Their catalytic flexibility is proposed to be related to their nonhaem iron-binding site, which utilizes two or three protein-based ligands. A possible penalty for this flexibility is that they may be more prone to oxidative damage than the P450 oxidases, where the iron is arguably located in a more controlled environment. We review the evidence for autocatalysed oxidative modifications to 2-oxoglutarate-dependent oxygenases, including the recently reported studies on human enzymes, as well as the oxidative fragmentations observed in the case of the plant ethylene-forming enzyme (1-aminocyclopropane-1-carboxylic acid oxidase).

• 出版日期2012-5