The DOI matches its Crossref record; 168 of the 168 references it cites were found in a registry or an index.
2-Oxoglutarate-Dependent Oxygenases
Abstract
2-Oxoglutarate (2OG)-dependent oxygenases (2OGXs) catalyze a remarkably diverse range of oxidative reactions. In animals, these comprise hydroxylations and N-demethylations proceeding via hydroxylation; in plants and microbes, they catalyze a wider range including ring formations, rearrangements, desaturations, and halogenations. The catalytic flexibility of 2OGXs is reflected in their biological functions. After pioneering work identified the roles of 2OGXs in collagen biosynthesis, research revealed they also function in plant and animal development, transcriptional regulation, nucleic acid modification/repair, fatty acid metabolism, and secondary metabolite biosynthesis, including of medicinally important antibiotics. In plants, 2OGXs are important agrochemical targets and catalyze herbicide degradation. Human 2OGXs, particularly those regulating transcription, are current therapeutic targets for anemia and cancer. Here, we give an overview of the biochemistry of 2OGXs, providing examples linking to biological function, and outline how knowledge of their enzymology is being exploited in medicine, agrochemistry, and biocatalysis.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“A relatively new discovery is the finding that vitamin C is the specific cofactor of 2OGO involved in cellular stress-signalling and epigenetics (reviewed in References [98,101,102,107,108,109]).”
From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [101]
In the citing paper
“The role(s) of vitamin C in this reaction cycle is (are) not fully elucidated, but likely the most important role is to maintain the iron atom in the reduced form [100,101].”
From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [101]
In the citing paper
“Generally, 2OGO catalyze specific hydroxylation of substrates, which, in turn, leads to demethylations via other catalytic cycles or downstream pathway involving thymine-DNA-glycosylase, which catalyzed base excision with DNA base excision repair [101,120].”
From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [101]
Citations
Cites
Wang, G. L., Jiang, B. H., Rue, E. A., & Semenza, G. L. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.12.5510 · Cited by 6,212
Conversion of 5-Methylcytosine to 5-Hydroxymethylcytosine in Mammalian DNA by MLL Partner TET1
Tahiliani, M., Koh, K. P., Shen, Y., Pastor, W. A., Bandukwala, H., Brudno, Y., Agarwal, S., Iyer, L. M., Liu, D. R., Aravind, L., et al. (2009) · Science · doi:10.1126/science.1170116 · Cited by 5,836
Jaakkola, P., Mole, D. R., Tian, Y.-M., Wilson, M. I., Gielbert, J., Gaskell, S. J., Kriegsheim, A. V., Hebestreit, H. F., Mukherji, M., Schofield, C. J., et al. (2001) · Science · doi:10.1126/science.1059796 · Cited by 5,535
Self-citationHIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O 2 Sensing
Ivan, M., Kondo, K., Yang, H., Kim, W., Valiando, J., Ohh, M., Salic, A., Asara, J. M., Lane, W. S., & Kaelin Jr., W. G. (2001) · Science · doi:10.1126/science.1059817 · Cited by 4,735
Collagen Structure and Stability
Shoulders, M. D., & Raines, R. T. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.032207.120833 · Cited by 3,923
Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine
Ito, S., Shen, L., Dai, Q., Wu, S. C., Collins, L. B., Swenberg, J. A., He, C., & Zhang, Y. (2011) · Science · doi:10.1126/science.1210597 · Cited by 3,451
Epstein, A. C. R., Gleadle, J. M., McNeill, L. A., Hewitson, K. S., O'Rourke, J., Mole, D. R., Mukherji, M., Metzen, E., Wilson, M. I., Dhanda, A., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00507-4 · Cited by 3,333
Self-citationOxygen sensing by metazoans: the central role of the HIF hydroxylase pathway.
Kaelin, W. G., & Ratcliffe, P. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.04.009 · Cited by 3,251
Xu, W., Yang, H., Liu, Y., Yang, Y., Wang, P., Kim, S.-H., Ito, S., Yang, C., Wang, P., Xiao, M.-T., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2010.12.014 · Cited by 2,875
Tet-Mediated Formation of 5-Carboxylcytosine and Its Excision by TDG in Mammalian DNA
He, Y., Li, B.-Z., Li, Z., Liu, P., Wang, Y., Tang, Q., Ding, J., Jia, Y., Chen, Z., Li, L., et al. (2011) · Science · doi:10.1126/science.1210944 · Cited by 2,776
Research works printed but not linked: 1
- 10.1038/ncomms12673 · DOI · Paper page
Cited by
Sorted by citations
Ascorbic acid: The chemistry underlying its antioxidant properties
Njus, D., Kelley, P. M., Tu, Y., & Schlegel, H. B. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.07.013 · Cited by 565
Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination
Doseděl, M., Jirkovský, E., Macáková, K., Krčmová, L., Javorská, L., Pourová, J., Mercolini, L., Remião, F., Nováková, L., Mladěnka, P., et al. (2021) · Nutrients · doi:10.3390/nu13020615 · Cited by 553
The role of m6A, m5C and Ψ RNA modifications in cancer: Novel therapeutic opportunities
Nombela, P., Miguel‐López, B., & Blanco, S. (2021) · Molecular Cancer · doi:10.1186/s12943-020-01263-w · Cited by 498
The Origin and Evolution of Plant Flavonoid Metabolism
Yonekura‐Sakakibara, K., Higashi, Y., & Nakabayashi, R. (2019) · Frontiers in Plant Science · doi:10.3389/fpls.2019.00943 · Cited by 494
Metabolic adaptation in hypoxia and cancer
Paredes, F., Williams, H. C., & Martín, A. S. (2021) · Cancer Letters · doi:10.1016/j.canlet.2020.12.020 · Cited by 276
Metadata
- Authors
- Islam, M. S., Leissing, T. M., Chowdhury, R., Hopkinson, R. J., & Schofield, C. J.
- Affiliations
- University of Oxford (GB)
- University of Leicester (GB)
- Corresponding author
- Islam, Md. Saiful
- Leissing, Thomas M.
- Chowdhury, Rasheduzzaman
- Hopkinson, Richard J.
- Schofield, Christopher J.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2018-06-20
- Volume
- 87
- Issue
- 1
- Pages
- 585-620
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2483061037
- Semantic Scholar
- 1f082a9f33c479e0e3ec9bbbf5edfe3f16c04e9d
- Cited by
- 472
- References
- 168
- Citations by year
- 2026: 39 · 2025: 58 · 2024: 76 · 2023: 54 · 2022: 57 · 2021: 70 · 2020: 53 · 2019: 38 · 2018: 18
- FWCI
- 1.57
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Wellcome Trust
- Cancer Research UK
- Biotechnology and Biological Sciences Research Council (BB/L009846/1)
- Topics
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Biochemical Acid Research Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
- Keywords
- 2-oxoglutarate-dependent dioxygenase, hydroxylation, N-demethylation, cyclization, desaturation, halogenation, collagen synthesis, transcriptional regulation, nucleic acid modification, fatty acid metabolism, secondary metabolite biosynthesis, antibiotic biosynthesis, herbicide degradation, anemia, cancer, biocatalysis, enzyme biochemistry
- MeSH terms
- Animals, Collagen, Humans, Hydroxylation, Ketoglutaric Acids, Models, Biological, Models, Molecular, Oxidation-Reduction, Oxygenases, Protein Conformation, Substrate Specificity, Biocatalysis
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
