期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 20, 期 6, 页码 659-672出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2010.08.006
关键词
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资金
- Biotechnology and Biological Sciences Research Council
- Wellcome Trust
- European Union
- BBSRC [BB/D011523/1, BB/F006349/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/F006349/1, BB/D011523/1] Funding Source: researchfish
2-Oxoglutarate and ferrous iron-dependent oxygenases have emerged as an important family of human enzymes that catalyse hydroxylations and related demethylation reactions. Their substrates in humans include proteins, nucleic acids, lipids and small molecules. They play roles in collagen biosynthesis, hypoxic sensing, regulation of gene expression and lipid biosynthesis/metabolism. Structural analyses, principally employing crystallography, have revealed that all of these oxygenases possess a double-stranded beta-helix core fold that supports a highly conserved triad of iron binding residues and a less well conserved 2-oxoglutarate co-substrate binding site. The 2-oxoglutarate binds to the iron in a bidentate manner via its 1-carboxylate and 2-oxo groups. The primary substrate binding elements are more variable and can involve mobile elements.
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