期刊
CHEMICAL RECORD
卷 18, 期 12, 页码 1760-1781出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/tcr.201800056
关键词
Epigenetics; 2-oxoglutarate and ferrous iron oxygenases; protein hydroxylation; histone demethylases; hypoxia sensing; JmjC KDM; transcription; penicillin biosynthesis
资金
- Cancer Research UK
- Biotechnological and Biological Research Council
- Medical Research Council
- National Institute of Health
- European Union's Horizon 2020 research and innovation programme under the Marie Skodowska-Curie [657292]
- Wellcome Trust
- Marie Curie Actions (MSCA) [657292] Funding Source: Marie Curie Actions (MSCA)
The 2-oxoglutarate (2OG) dependent oxygenases were first identified as having roles in the post-translational modification of procollagen in animals. Subsequently in plants and microbes, they were shown to have roles in the biosynthesis of many secondary metabolites, including signalling molecules and the penicillin/cephalosporin antibiotics. Crystallographic studies of microbial 2OG oxygenases and related enzymes, coupled to DNA sequence analyses, led to the prediction that 2OG oxygenases are widely distributed in aerobic biology. This personal account begins with examples of the roles of 2OG oxygenases in antibiotic biosynthesis, and then describes efforts to assign functions to other predicted 2OG oxygenases. In humans, 2OG oxygenases have been found to have roles in small molecule metabolism, as well as in the epigenetic regulation of protein and nucleic acid biosynthesis and function. The roles and functions of human 2OG oxygenases are compared, focussing on discussion of their substrate and product selectivities. The account aims to emphasize how scoping the substrate selectivity of, sometimes promiscuous, enzymes can provide insights into their functions and so enable therapeutic work.
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