Cited by 492Metal-Catalyzed Oxygenation MechanismsBiochemical Acid Research StudiesMicrobial metabolism and enzyme function

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

Islam, Md. Saiful, Leissing, Thomas M., Chowdhury, Rasheduzzaman, Hopkinson, Richard J., Schofield, Christopher J.·2018·Annual Review of Biochemistry

DOI 10.1146/annurev-biochem-061516-044724

Open this paper in CoChat — free account

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.

Integrity signals

Registry

Crossref · 10.1146/annurev-biochem-061516-044724

Cites

168 of 168 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension.
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
Targeting of HIF-α to the von Hippel-Lindau Ubiquitylation Complex by O 2 -Regulated Prolyl Hydroxylation
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-citation
HIFα 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
C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation
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-citation
Oxygen 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
Oncometabolite 2-Hydroxyglutarate Is a Competitive Inhibitor of α-Ketoglutarate-Dependent Dioxygenases
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

Show all 168 references

Research works printed but not linked: 1

10.1038/ncomms12673 · DOI · Paper page

Sorted by citations

Items 301–400 of 492

Comprehensive Analysis of 13C6 Glucose Fate in the Hypoxia-Tolerant Blind Mole Rat Skin Fibroblasts
Miskevich, D. A., Chaban, A., Dronina, M. A., Abramovich, I., Gottlieb, E., & Shams, I. (2021) · Metabolites · doi:10.3390/metabo11110734 · Cited by 6
Rational Engineering of the Nonheme Iron- and 2-Oxoglutarate-Dependent Oxygenase SptF
Mori, T., Yu, Z., Tao, H., & Abe, I. (2022) · Organic Letters · doi:10.1021/acs.orglett.2c00409 · Cited by 6
Pathway from N‐Alkylglycine to Alkylisonitrile Catalyzed by Iron(II) and 2‐Oxoglutarate‐Dependent Oxygenases
Chen, T., Chen, J., Tang, Y., Zhou, J., Guo, Y., & Chang, W. (2020) · Angewandte Chemie · doi:10.1002/ange.201914896 · Cited by 6
Investigating the active site of human trimethyllysine hydroxylase
Wang, Y., Reddy, Y. V., Temimi, A. H. K. A., Venselaar, H., Nelissen, F. H. T., Lenstra, D. C., & Mecinović, J. (2019) · Biochemical Journal · doi:10.1042/bcj20180857 · Cited by 6
Microgliosis, neuronal death, minor behavioral abnormalities and reduced endurance performance in alpha-ketoglutarate dehydrogenase complex deficient mice
Kokas, M., Budai, A., Kádár, A., Mozaffaritabar, S., Zhou, L., Téglás, T., Orova, R. S., Gáspár, D., Németh, K., Toth, D. M., et al. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103743 · Cited by 6
Streamlining enzyme discovery and development through data analysis and computation
Kumar, A., Taubitz, J., Meyer, F., Imstepf, N., Peng, J., Tassano, E., Moore, C. M., Lochmann, T., Šnajdrová, R., & Buller, R. (2025) · Chem Catalysis · doi:10.1016/j.checat.2025.101445 · Cited by 4
Hydroxylation of HPPD facilitates its PUB11-mediated ubiquitination and degradation in response to oxidative stress in Arabidopsis
Yu, X., Wen, X., Dong, J., Hu, Y., Wang, X.-L., Zhu, D.-Y., Ling, Q., Lin, H., & Yang, G. (2025) · Plant Communications · doi:10.1016/j.xplc.2025.101521 · Cited by 5
Enzymatic Strategies for Nitrogen–Nitrogen Bond Formation in Natural Product Biosynthesis
Shi, J., Zhao, G., & Du, Y. (2026) · Chemical Reviews · doi:10.1021/acs.chemrev.5c01091 · Cited by 6
Biochemical investigations using mass spectrometry to monitor JMJD6-catalysed hydroxylation of multi-lysine containing bromodomain-derived substrates
Corner, T. P., Salah, E., Tumber, A., Brewitz, L., & Schofield, C. J. (2025) · RSC Chemical Biology · doi:10.1039/d4cb00311j · Cited by 6
Self-citation
Characterization of an α‐ketoglutarate‐dependent oxygenase involved in converting 2‐(2‐phenylethyl)chromones into 2‐styrylchromones in agarwood
Zhang, M., Fan, J., Zhang, Z., Niu, M., Mi, X., Qiu, H., Li, J., Liu, X., Wang, J., Wang, X., et al. (2025) · The Plant Journal · doi:10.1111/tpj.70068 · Cited by 5
Preliminary Multi-Omics Insights into Green Alternatives to Antibiotics: Effects of Pulsatilla chinensis, Acer truncatum, and Clostridium butyricum on Gut Health and Metabolic Regulation in Chickens
Sun, L., Wang, Z., Qin, S., Liang, C., Zhao, A., & He, K. (2025) · Animals · doi:10.3390/ani15091262 · Cited by 5
Genomic and Epigenomic Plasticity in the Hypoxic Environment
Cricchi, E., Bertozzo, A., Minisini, M., & Brancolini, C. (2025) · DNA · doi:10.3390/dna5020022 · Cited by 6
Evolution‐guided engineering of non‐heme iron enzymes involved in nogalamycin biosynthesis
Wandi, B. N., Siitonen, V., Dinis, P., Vukić, V., Salminen, T. A., & Metsä‐Ketelä, M. (2019) · FEBS Journal · doi:10.1111/febs.15192 · Cited by 5
Structure and mutation of deoxypodophyllotoxin synthase (DPS) from Podophyllum hexandrum
Ingold, Z., Grogan, G., & Lichman, B. R. (2023) · Frontiers in Catalysis · doi:10.3389/fctls.2023.1178345 · Cited by 5
The unequal functional redundancy of Arabidopsis INCURVATA11 and CUPULIFORMIS2 is not dependent on genetic background
Nadi, R., Juan-Vicente, L., Mateo‐Bonmatí, E., & Micol, J. L. (2023) · Frontiers in Plant Science · doi:10.3389/fpls.2023.1239093 · Cited by 5
Oxygen-Dependent Histone Lysine Demethylase 4 Restricts Hepatitis B Virus Replication
Harris, J. M., Magri, A., Faria, A. R., Tsukuda, S., Balfe, P., Wing, P. A. C., & McKeating, J. A. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.105724 · Cited by 5
Reading and erasing of the phosphonium analogue of trimethyllysine by epigenetic proteins
Belle, R., Kamps, J. J. A. G., Poater, J., Kumar., K., V, Pieters, B. J. G. E., Salah, E., Claridge, T. D. W., Paton, R. S., Bickelhaupt, F. M., Kawamura, A., et al. (2022) · Communications Chemistry · doi:10.1038/s42004-022-00640-4 · Cited by 5
Self-citation
Metabolic characteristics of transmembrane prolyl 4-hydroxylase (P4H-TM) deficient mice
Ala‐Nisula, T., Halmetoja, R., Leinonen, H., Kurkela, M., Lipponen, H.-R., Sakko, S., Karpale, M., Salo, A. M., Sissala, N., Röning, T., et al. (2024) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-024-02920-5 · Cited by 5
Molecular Components of the RCC Grade
Ishimaru, T. (2020) · Seminars in Nephrology · doi:10.1016/j.semnephrol.2019.12.003 · Cited by 5
Radical Ring Expansion Catalyzed by an α-Ketoglutarate-Dependent Dioxygenase in the Biosynthesis of Tropolones
Liu, M., Liu, J.-W., Bai, S., Chen, Z., Wu, Y., Du, D., Qi, X., He, X., & Hu, Y. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c11241 · Cited by 4
Alpha-ketoglutarate restores oral epithelial homeostasis via FOXM1-mediated cell cycle regulation
Wang, Y., Cai, Y., Yin, Q., Cao, S., Li, Y., Li, Y., Li, Q., Wang, Q., Lin, P., Li, M., et al. (2025) · Science China Life Sciences · doi:10.1007/s11427-024-2984-1 · Cited by 4
Harnessing Fe(II)/α-ketoglutarate-dependent oxygenases for sustainable synthesis
Wang, H., Mori, T., & Abe, I. (2026) · Current Opinion in Green and Sustainable Chemistry · doi:10.1016/j.cogsc.2026.101059 · Cited by 4
Clioquinol as an inhibitor of JmjC-histone demethylase exhibits common and unique histone methylome and transcriptome between clioquinol and hypoxia
Moon, Y., Chae, S., Yim, S., Yang, E. G., Choe, J., Hyun, J., Chang, R., Hwang, D., & Park, H. (2022) · iScience · doi:10.1016/j.isci.2022.104517 · Cited by 4
Binding versus Enzymatic Processing of ε-Trimethyllysine Dioxygenase Substrate Analogues
Zelencova-Gopejenko, D., Grandāne, A., Loža, E., Loļa, D., Sipola, A., Liepinsh, E., Arsenyan, P., & Jaudzems, K. (2022) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.2c00261 · Cited by 4
Review of the Potential Role of Ascorbate in the Prevention and Treatment of Gynecological Cancers
Shen, X., Wang, J., Deng, B., Zhao, Z., Chen, S., Kong, W., Zhou, C., & Bae-Jump, V. L. (2024) · Antioxidants · doi:10.3390/antiox13050617 · Cited by 5
Identification and characterization of the siderochelin biosynthetic gene cluster via coculture
Schaenzer, A. J., Wang, W., Hackenberger, D., & Wright, G. D. (2024) · mBio · doi:10.1128/mbio.01871-24 · Cited by 4
Metagenomic time series reveals a Western English Channel viral community dominated by members with strong seasonal signals
Bolaños, L. M., Michelsen, M. L., & Temperton, B. (2024) · The ISME Journal · doi:10.1093/ismejo/wrae216 · Cited by 6
Two Plus Four Equals Three–Iron(II)/Iron(IV) Comproportionation as an Additional Pathway for Iron(IV)-Oxido Reactions
Jonasson, N. S. W., Menke, A., Senft, L., Squarcina, A., Schmidl, D., Fisher, K. R., Demeshko, S., Kruse, J. C., Josephy, T., Mayer, P., et al. (2025) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.4c04518 · Cited by 4
Substrate selectivity and inhibition of histidine JmjC hydroxylases MINA53 and NO66
Türkmen, V. A., Hintzen, J. C. J., Tumber, A., Moesgaard, L., Salah, E., Kongsted, J., Schofield, C. J., & Mecinović, J. (2023) · RSC Chemical Biology · doi:10.1039/d2cb00182a · Cited by 4
Self-citation
The structure of the Drosophila melanogaster sex peptide: Identification of hydroxylated isoleucine and a strain variation in the pattern of amino acid hydroxylation
Sturm, S., Dowle, A., Audsley, N., & Isaac, R. E. (2020) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2020.103414 · Cited by 4
Fe(2)OG: an integrated HMM profile-based web server to predict and analyze putative non-haem iron(II)- and 2-oxoglutarate-dependent dioxygenase function in protein sequences
Kundu, S. (2021) · BMC Research Notes · doi:10.1186/s13104-021-05477-z · Cited by 5
Analysis of the cryptic biosynthetic gene cluster encoding the RiPP curacozole reveals a phenylalanine-specific peptide hydroxylase
Hollands, S., Tasch, J., Simon, D. J., Wassouf, D., Barber, I., Gessner, A., Bechthold, A., & Zechel, D. L. (2024) · Chemical Science · doi:10.1039/d4sc02262a · Cited by 3
Characterization of the Biosynthesis of Pimprinine-Type Indolyloxazoles Unravels an Unusual d -Configurational Substrate Metabolic Streamline
Zhang, Y., Zhao, Y., Wang, N., Wang, H., Pan, Y., Zhai, Y., Hou, L., & Li, W. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c01705 · Cited by 3
Three distinct strategies lead to programmable aliphatic C−H oxidation in bicyclomycin biosynthesis
Wu, L., He, J., Wei, W., Pan, H., Wang, X., Yang, S., Liang, Y. F., Tang, G., & Zhou, J. (2025) · Nature Communications · doi:10.1038/s41467-025-58997-8 · Cited by 3
BioIron: Origin, Chemical Properties, and Biological Functions
Pantopoulos, K. (2025) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-92033-2_1 · Cited by 5
Unusual O–H Activation-Initiated C–C Bond Cleavage Reaction by a Nonheme Fe Enzyme in Antifungal Nucleoside Biosynthesis
Du, Y., Dong, J., Draelos, M. M., Collazo-Perez, L. N., Majer, S. H., Boal, A. K., & Yokoyama, K. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c08400 · Cited by 3
Hydrogen Atom Abstraction via Hydride-Coupled Electron Transfer and Its Origin
Wojdyła, Z., Gopinath, J. S., & Srnec, M. (2025) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.5c03613 · Cited by 3
The Interplay Between Bone Biology and Iron Metabolism: Molecular Mechanisms and Clinical Implications
Correnti, M., Gammella, E., Cairo, G., & Recalcati, S. (2026) · Biomedicines · doi:10.3390/biomedicines14020301 · Cited by 4
αKG-mediated carnitine synthesis drives DNA repair via histone acetylation
Uboveja, A., Yang, B., Buj, R., Amalric, A., Wang, H., Tangudu, N. K., Cole, A. R., Disharoon, J. A., Fang, R. S., Levasseur, E., et al. (2026) · Nature · doi:10.1038/s41586-026-10584-7 · Cited by 10
R97 at “Handlebar” Binding Mode in Active Pocket Plays an Important Role in Fe(II)/α-Ketoglutaric Acid-Dependent Dioxygenase cis-P3H-Mediated Selective Synthesis of (2S,3R)-3-Hydroxypipecolic Acid
Guan, J., Lu, Y., Dai, Z., Zhao, S., Xu, Y., & Nie, Y. (2023) · Molecules · doi:10.3390/molecules28041854 · Cited by 3
Methylation of the JMJD2B epigenetic regulator differentially affects its ability to coactivate the ETV1 and JUN transcription factors.
Kim, T., Gu, R., & Janknecht, R. (2023) · PubMed Central · Cited by 3
Enzymatic one-step synthesis of natural 2-pyrones and new-to-nature derivatives from coenzyme A esters
Manoilenko, S., Dippe, M., Fuchs, T., Eisenschmidt‐Bönn, D., Ziegler, J., Bauer, A., & Wessjohann, L. A. (2024) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2024.04.006 · Cited by 3
Cellular Iron Homeostasis
Philpott, C. C., & Meyron‐Holtz, E. G. (2025) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-92033-2_2 · Cited by 3
Glutarate L-2-hydroxylase (CsiD/GlaH) is an archetype Fe(II)/2-oxoglutarate-dependent dioxygenase
Herr, C. Q., Macomber, L., Kalliri, E., & Hausinger, R. P. (2019) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2019.05.001 · Cited by 3
Measurement of kinetic isotope effects on peptide hydroxylation using MALDI-MS
Mingroni, M. A., Chaplin, V. D., Barlow, A. N., Maisonet, I. J., & Knapp, M. J. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.08.019 · Cited by 3
N6-methyladenine: A Rare and Dynamic DNA Mark
O’Brown, Z. K., & Greer, E. L. (2022) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-11454-0_8 · Cited by 3
OGFOD1 modulates the transcriptional and proteomic landscapes to alter isoproterenol-induced hypertrophy susceptibility
Rodriguez, R., Harris, M., Murphy, E., & Kennedy, L. (2023) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2023.04.002 · Cited by 3
Pangenomic Analysis of Nucleo-Cytoplasmic Large DNA Viruses. I: The Phylogenetic Distribution of Conserved Oxygen-Dependent Enzymes Reveals a Capture-Gene Process
Campillo-Balderas, J. A., Lazcano, A., Cottom-Salas, W., Jácome, R., & Becerra, A. (2023) · Journal of Molecular Evolution · doi:10.1007/s00239-023-10126-z · Cited by 3
Expression, purification, and biochemical characterization of micro- and macroalgal kainoid synthases
Hopiavuori, A. R., Huffman, R., & McKinnie, S. M. K. (2024) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2024.05.017 · Cited by 3
2-Oxoglutarate-dependent dioxygenases as oxygen sensors: their importance in health and disease
Lee, P. W. T., Kobayashi, M., Dohkai, T., Takahashi, I., Yoshida, T., & Harada, H. (2024) · The Journal of Biochemistry · doi:10.1093/jb/mvae087 · Cited by 4
Prediction of the reaction mechanisms of sesquiterpene coumarin synthases supports a direct evolutionary link with triterpene biosynthesis
Stephenson, M. J., & Brodelius, P. E. (2025) · Phytochemistry Reviews · doi:10.1007/s11101-024-10055-9 · Cited by 3
Enzymatic Synthesis of l - threo -β-Hydroxy-α-Amino Acids via Asymmetric Hydroxylation Using 2-Oxoglutarate-Dependent Hydroxylase from Sulfobacillus thermotolerans Strain Y0017
Hara, R., Nakajima, Y., Yanagawa, H., Gawasawa, R., Hirasawa, I., & Kino, K. (2021) · Applied and Environmental Microbiology · doi:10.1128/aem.01335-21 · Cited by 3
Characterization of a Citrulline 4‐Hydroxylase from Nonribosomal Peptide GE81112 Biosynthesis and Engineering of Its Substrate Specificity for the Chemoenzymatic Synthesis of Enduracididine
Zwick, C. R., Sosa, M. B., & Renata, H. (2019) · Angewandte Chemie · doi:10.1002/ange.201910659 · Cited by 3
m6A RNA modifications: Key regulators of normal and malignant hematopoiesis
Sommerkamp, P., Brown, J. A., Haltalli, M. L. R., Mercier, F., Vu, L., & Kranc, K. R. (2022) · Experimental Hematology · doi:10.1016/j.exphem.2022.04.006 · Cited by 3
Overlapping roles of Arabidopsis INCURVATA11 and CUPULIFORMIS2 as Polycomb Repressive Complex 2 accessory proteinsPreprint
Nadi, R., Juan-Vicente, L., Lup, S. D., Fernández, Y., Rubio, V., & Micol, J. L. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.15.585069 · Cited by 3
Perfluorinated compounds linked to central precocious puberty in girls during COVID-19: an untargeted metabolomics study
Li, H., Xie, M., Luo, H., Cai, Y., Liu, L., Li, H., Hai, Y., Ren, Y., Xue, J., He, X., et al. (2024) · Frontiers in Endocrinology · doi:10.3389/fendo.2024.1491411 · Cited by 2
Multiple Catalytic Branch Points in the Mechanism of Pyrrolidine Formation During Kainoid Biosynthesis Leads to Diverse Reaction Outcomes
Chen, T., Ruszczycky, M. W., Yao, A., Li, X., Chien, T., & Chang, W. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c07226 · Cited by 2
Metabolomics Reveals Abnormal Citrate Cycle and Phenylalanine Metabolism in Testes from Infertile Hybrid Dzo
Ding, J., Dao, Y., Liang, L., Hong, R., Chen, H., Yi, Y., Wang, L., Zuo, F., & Zhang, G. (2025) · Animals · doi:10.3390/ani15203023 · Cited by 2
Genome mining-driven discovery of enzymes catalyzing stereodivergent transformations
Yu, J., & Ushimaru, R. (2025) · The Journal of Antibiotics · doi:10.1038/s41429-025-00881-0 · Cited by 2
Vitamin C as an epigenetic gatekeeper of osteogenesis and skeletal health: a new perspective on an ancient molecule
Thaler, R. (2025) · Journal of Bone and Mineral Research · doi:10.1093/jbmr/zjaf174 · Cited by 2
A new role for PHYHD1 and related dioxygenases: demethylation of 2′- O -methylated nucleosides
Stonkus, J., Rutkienė, R., Meškienė, R., Jasiūnienė, M., Aučynaitė, A., Kalinienė, L., Lazutka, J., Balciunas, D., Vilkaitis, G., & Meškys, R. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf1379 · Cited by 2
CURE-ating the Substrate Scope and Functional Residues of Nonheme Iron(II) α-Ketoglutarate-Dependent Hydroxylase BesE
Hopiavuori, A. R., Andre, B. S., Avalos, E. D., Beal, S. L., Beck, G. R., Choi, C. J., Dolzhansky, E. M., Du, M. X., Gallardo, I. S., Ghorbani, C. J., et al. (2025) · Journal of Natural Products · doi:10.1021/acs.jnatprod.5c01272 · Cited by 2
MdCoL regulating columnar growth in apple trees positively mediates drought stress responses
Wang, M., Han, T., Hua, T., Liu, R. Y., Feng, Y., Sun, Z., Zhang, Y., & Sun, X. (2026) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2026.111039 · Cited by 2
Identification of Key Genes Associated with Feed Utilization Efficiency in Penaeus vannamei Fed a Plant-Based Diet Using WGCNA
Zhang, H. S., Xu, Y., Sui, J., Fu, Q., Liu, M.-Y., Tan, J., Kong, J., Luo, K., Meng, X., Luan, S., et al. (2026) · Animals · doi:10.3390/ani16101480 · Cited by 2
Beyond Histone Demethylation: Mechanisms of N -Alkyl Consecutive Oxidations by the Non-Heme Fe(II)/2-Oxoglutarate Oxygenase KDM6B
Rifayee, S. B. J. S., Devadas, S., Thomas, M. G., Varada, B., Sommer, E., Talaba, C., Schofield, C. J., & Christov, C. Z. (2026) · JACS Au · doi:10.1021/jacsau.6c00575 · Cited by 4
Self-citation
The structural chemistry and biosynthesis of chlorophylls
Hunter, C. N., & Morey-Burrows, F. S. (2026) · RSC Chemical Biology · doi:10.1039/d6cb00082g · Cited by 3
Mechanistic Basis of Bifunctional Oxidation by a Non-Heme Fe(II)/2-Oxoglutarate-Dependent Enzyme CcTET toward N 6-Methyladenine and 5-Methylcytosine in Double-Stranded DNA
Varada, B., Rifayee, S. B. J. S., Thomas, M. G., Sommer, E., Davis, C., Waheed, S. O., Devadas, S., Kalita, S., Melayikandy, S., Karabencheva‐Christova, T. G., et al. (2026) · ACS Catalysis · doi:10.1021/acscatal.6c02591 · Cited by 4
Biochemical and Structural Insights into an Fe(II)/α-Ketoglutarate/O2-Dependent Dioxygenase, Kdo 3-Hydroxylase (KdoO)
Joo, S. H., Pemble, C. W., IV, Yang, E. G., Raetz, C. R. H., & Chung, H. S. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.07.029 · Cited by 2
The MdCo gene encodes a putative 2OG-Fe (II) oxygenase that positively regulates salt tolerance in transgenic tomato and apple
Yuan, P., Tian, J., Wei, Y., Wang, M., Song, C., Jiao, J., Wang, M., Zhang, K., Hao, P., Zheng, X., et al. (2024) · Plant Science · doi:10.1016/j.plantsci.2024.112267 · Cited by 2
Substrate selectivity and inhibition of the human lysyl hydroxylase JMJD7
Bilgin, N., Tumber, A., Dhingra, S., Salah, E., Al‐Salmy, A., Martín, S. P., Wang, Y., Schofield, C. J., & Mecinović, J. (2024) · Protein Science · doi:10.1002/pro.5162 · Cited by 2
Self-citation
Computational Stabilization of a Non‐Heme Iron Enzyme Enables Efficient Evolution of New Function
King, B. R., Sumida, K. H., Caruso, J. L., Baker, D. A., & Zalatan, J. G. (2024) · Angewandte Chemie · doi:10.1002/ange.202414705 · Cited by 2
C–C Bond Cleavage in the Late-Stage Biosynthesis of Huperzine Alkaloids Occurs via Enzymatic Retro-Aza-Prins Reaction
Payer, S. E., Prejanò, M., Kögl, P., Reiter, T. C., Pferschy‐Wenzig, E., Himo, F., & Kroutil, W. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.4c10410 · Cited by 2
Nucleobase Modifiers Identify TET Enzymes as Bifunctional DNA Dioxygenases Capable of Direct N‐Demethylation
Ghanty, U., Wang, T., & Kohli, R. M. (2020) · Angewandte Chemie · doi:10.1002/ange.202002751 · Cited by 2
Properties, biosynthesis, and catalytic mechanisms of hydroxy-amino-acids
daoxuan, S. U. N., Cheng, X., Gao, D. K., Xu, P., Guo, Q., Zhu, Z., Zhu, M. L., Wang, X. Y., Qin, H., & Lu, F. (2018) · IOP Conference Series Earth and Environmental Science · doi:10.1088/1755-1315/188/1/012084 · Cited by 2
Genetic and Epigenetic Biomarkers Related to 2-Oxoglutarate/Fe(II)-Dependent Oxygenases and Implications for Disease and Toxicology
Wang, J., Qi, R., Li, H., Christov, C. Z., Lehnert, N., & Li, D. (2023) · Biomarkers in disease · doi:10.1007/978-3-031-07392-2_19 · Cited by 2
Semi-Rational Design of L-Isoleucine Dioxygenase Generated Its Activity for Aromatic Amino Acid Hydroxylation
An, J., Guan, J., & Nie, Y. (2023) · Molecules · doi:10.3390/molecules28093750 · Cited by 1
Molecular Basis of Response to Hypoxia
Krishnan, A., & Ansari, H. K. (2023) · Springer eBooks · doi:10.1007/978-981-99-7652-2_2 · Cited by 2
A glycogenin homolog controls Toxoplasma gondii growth via glycosylation of an E3 ubiquitin ligasePreprint
Mandalasi, M., Kim, H. W., Thieker, D. F., Sheikh, M. O., Gas‐Pascual, E., Rahman, K., Zhao, P., Daniel, N. G., van der Wel, H., Ichikawa, H. T., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/764241 · Cited by 2
Iron and 2‐Oxoglutarate‐Dependent Isonitrile‐Forming Enzymes
Chen, T., Guo, Y., & Chang, W. (2023) · Encyclopedia of Inorganic and Bioinorganic Chemistry · doi:10.1002/9781119951438.eibc2838 · Cited by 2
A serine metabolic enzyme is flexing its muscle to help repair skeletal musclePreprint
Baráth, B. R., & Nagy, L. (2024) · Genes & Development · doi:10.1101/gad.351666.124 · Cited by 2
Deleting the ribosomal prolyl hydroxylase OGFOD1 protects mice against diet-induced obesity and insulin resistance
Rodriguez, R., Harris, M., & Kennedy, L. (2024) · PLoS ONE · doi:10.1371/journal.pone.0304761 · Cited by 1
Unravelling 2-oxoglutarate turnover and substrate oxidation dynamics in 5-methylcytosine-oxidising TET enzymes
Šimelis, K., Belle, R., & Kawamura, A. (2024) · Communications Chemistry · doi:10.1038/s42004-024-01382-1 · Cited by 1
Iron content of glioblastoma tumours and role of ferrous iron in the hypoxic response in vitro
Praditi, C., Beverley-Stone, E., Reid, M., Burgess, E. R., Crake, R., Vissers, M. C. M., Royds, J. A., Slatter, T. L., Dachs, G. U., & Phillips, E. (2025) · Frontiers in Oncology · doi:10.3389/fonc.2025.1536549 · Cited by 1
Role and mechanisms of m6A demethylases in digestive system tumors
Jiang, L. (2025) · American Journal of Cancer Research · doi:10.62347/xmaf1290 · Cited by 1
Demethylation of methylguanidine by a stepwise dioxygenase and lyase reaction
Sinn, M., Funck, D., Gamer, F., Blumenthal, C., Kramp, C., & Hartig, J. S. (2025) · Nature Communications · doi:10.1038/s41467-025-64776-2 · Cited by 1
Mitochondrial ABHD11 inhibition drives sterol metabolism to modulate T-cell effector function
Jenkins, B. J., Jenkins, Y. R., Ponce-Garcia, F. M., Moscrop, C., Perry, I. A., Hitchings, M. D., Uribe, A. H., Bernuzzi, F., Eastham, S., Cronin, J., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-65417-4 · Cited by 2
Structure-Guided Engineering of 2-Oxoglutarate-Dependent Oxygenases: Principles, Case Studies, and Emerging Opportunities
Nakashima, Y. (2025) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.c25-00652 · Cited by 1
Structural Aspects of Proline Methanologues in Drug Design, Optimization, and Development
Hanessian, S., & Meanwell, N. A. (2026) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.5c03173 · Cited by 1
VvGA2ox8-Like from grape confers drought tolerance by activating the antioxidant defense system
Yang, W., Yang, J., Lu, S., Gou, H., Wang, N., Yuan, M., Ma, W., Zeng, B., Liang, G., & Mao, J. (2026) · Plant Cell Reports · doi:10.1007/s00299-026-03823-8 · Cited by 1
The biodegradation of phosphonates
Pallitsch, K., Murray, L., & Chin, J. P. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-44447-0.00003-8 · Cited by 1
Total Synthesis of (+)-12- epi -Fischerindole U Isonitrile and Its Activity as a Substrate of the Halogenase WelO5
Narva, S., Vedantham, P., Walters, K. A., Lloyd, C. T., Silakov, A., & Grossman, R. B. (2026) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.6c00185 · Cited by 1
Clinically approved HIF-PHIs modulate redox metabolism, cell growth, and angiogenesis independent of HIF-1α/HIF-2α
Mennerich, D., Khoder‐Agha, F., Beter, M., Dimova, E. Y., Ylä-Herttuala, S., & Kietzmann, T. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104206 · Cited by 1
How Fe(II)/2-Oxoglutarate Oxygenase Chooses Chlorination over Hydroxylation: Electric Field-Driven Ligand Exchange Governs C–Cl Formation
Rifayee, S. B. J. S., Thomas, M. G., Krishnan, A., Gupta, K., Davis, C., Karabencheva‐Christova, T. G., & Christov, C. Z. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c22369 · Cited by 1
Alpha-Ketoglutarate Attenuates UVB-Induced Skin Photoaging by Restoring Mitochondrial Redox Homeostasis
Zhang, W., Zhang, Y., Wang, X., Chen, Y., Li, Y., & Sun, Y. (2026) · Antioxidants · doi:10.3390/antiox15070845 · Cited by 1
Harnessing the potential of oxygenases in plant specialized metabolism
Dinday, S., Yadav, S. K., & Ghosh, S. (2026) · Critical Reviews in Plant Sciences · doi:10.1080/07352689.2026.2713963 · Cited by 1
A postreplicative C5-cytosine hypermodification triggered by bacteriophage methyltransferase and hydroxylase
Chen, T., & Chang, W. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2109992118 · Cited by 1
An Unusual Oxidative Rearrangement Catalyzed by a Divergent Member of the 2‐Oxoglutarate‐Dependent Dioxygenase Superfamily during Biosynthesis of Dehydrofosmidomycin
Parkinson, E. I., Lakkis, H. G., Alwali, A. A., Metcalf, M. E., Modi, R., & Metcalf, W. W. (2022) · Angewandte Chemie · doi:10.1002/ange.202206173 · Cited by 1
Genetic and Epigenetic Biomarkers Related to 2-Oxoglutarate/Fe(II)-Dependent Oxygenases and Implications for Disease and Toxicology
Wang, J., Qi, R., Li, H., Christov, C. Z., Lehnert, N., & Li, D. (2022) · Biomarkers in disease · doi:10.1007/978-3-030-87225-0_19-1 · Cited by 1
Targeting 2-Oxoglutarate–Dependent Dioxygenases Promotes Metabolic Reprogramming That Protects against Lethal SARS-CoV-2 Infection in the K18-hACE2 Transgenic Mouse Model
Jessop, F., Schwarz, B. H., Bohrnsen, E., Miltko, M., Shaia, C., & Bosio, C. M. (2023) · ImmunoHorizons · doi:10.4049/immunohorizons.2300048 · Cited by 1
Radical fluorine transfer catalysed by an engineered nonheme iron enzyme
Zhao, Q., Chen, Z., Rui, J., & Huang, X. (2024) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2024.03.004 · Cited by 1

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.
ORCID: Islam, Md. Saiful
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
DOI: 10.1146/annurev-biochem-061516-044724
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

2-Oxoglutarate-Dependent Oxygenases

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks