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1. Full Text Structure–function relationships of human JmjC oxygenases—demethylases versus hydroxylases
by Markolovic, Suzana and Leissing, Thomas M and Chowdhury, Rasheduzzaman and Wilkins, Sarah E and Lu, Xin and Schofield, Christopher J
Current Opinion in Structural Biology, ISSN 0959-440X, 12/2016, Volume 41, pp. 62 - 72
The Jumonji-C (JmjC) subfamily of 2-oxoglutarate (2OG)-dependent oxygenases are of biomedical interest because of their roles in the regulation of gene... 
HYPOXIA-INDUCIBLE FACTOR | HISTONE DEMETHYLASE | SUBSTRATE-SPECIFICITY | INHIBITING-HIF FIH | 2-OXOGLUTARATE-DEPENDENT OXYGENASES | JUMONJI FAMILY | DOMAIN-CONTAINING PROTEIN | LYSYL-HYDROXYLATION | ASPARAGINYL HYDROXYLASE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL BIOLOGY | Animals | Biocatalysis | Humans | Protein Multimerization | Jumonji Domain-Containing Histone Demethylases - chemistry | Mixed Function Oxygenases - metabolism | Structure-Activity Relationship | Jumonji Domain-Containing Histone Demethylases - metabolism | Oxidases | Oligomers | Catalysis | Hydroxylases
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2. Full Text Inhibition of 2-oxoglutarate dependent oxygenases
by Rose, Nathan R and McDonough, Michael A and King, Oliver N. F and Kawamura, Akane and Schofield, Christopher J
Chemical Society Reviews, ISSN 0306-0012, 08/2011, Volume 40, Issue 8, pp. 4364 - 4397
2-Oxoglutarate (2OG) dependent oxygenases are ubiquitous iron enzymes that couple substrate oxidation to the conversion of 2OG to succinate and carbon dioxide.... 
CLEFT LIP/CLEFT PALATE | HIF-PROLYL HYDROXYLASE | DOMAIN-CONTAINING PROTEINS | LINKED MENTAL-RETARDATION | COLLAGEN PROLINE HYDROXYLASE | GAMMA-BUTYROBETAINE HYDROXYLASE | HYPOXIA-INDUCIBLE-FACTOR | TAURINE/ALPHA-KETOGLUTARATE DIOXYGENASE | CHEMISTRY, MULTIDISCIPLINARY | ENDOTHELIAL GROWTH-FACTOR | ANKYRIN REPEAT DOMAIN | gamma-Butyrobetaine Dioxygenase - antagonists & inhibitors | Humans | Enzyme Inhibitors - pharmacology | Mixed Function Oxygenases - metabolism | Mixed Function Oxygenases - antagonists & inhibitors | Mixed Function Oxygenases - chemistry | Procollagen-Proline Dioxygenase - metabolism | Gibberellins - metabolism | Succinic Acid - metabolism | Enzyme Inhibitors - chemistry | Ethylenes - biosynthesis | Procollagen-Proline Dioxygenase - antagonists & inhibitors | Collagen - biosynthesis | Ketoglutaric Acids - metabolism | Metals - pharmacology
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3. Full Text Protein hydroxylation catalyzed by 2-oxoglutarate-dependent oxygenases
by Markolovic, Suzana and Wilkins, Sarah E and Schofield, Christopher J
Journal of Biological Chemistry, ISSN 0021-9258, 08/2015, Volume 290, Issue 34, pp. 20712 - 20722
The post-translational hydroxylation of prolyl and lysyl residues, as catalyzed by 2-oxoglutarate (2OG)-dependent oxygenases, was first identified in collagen... 
VON-HIPPEL-LINDAU | DOMAIN-CONTAINING PROTEINS | SUBSTRATE-SPECIFICITY | PROLYL-HYDROXYLATION | LYSYL-HYDROXYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | HYPOXIA-INDUCIBLE-FACTOR | ASPARAGINYL HYDROXYLATION | HISTONE DEMETHYLATION | 6 JMJD6 | ANKYRIN REPEAT DOMAIN | Dioxygenases - metabolism | Gene Expression | Biocatalysis | Hydroxylation | Humans | Hypoxia-Inducible Factor-Proline Dioxygenases - genetics | Models, Molecular | Mixed Function Oxygenases - metabolism | Bacteria - genetics | Histone Demethylases - genetics | Iron - metabolism | Histone Demethylases - metabolism | Dioxygenases - genetics | Hypoxia-Inducible Factor-Proline Dioxygenases - metabolism | Bacteria - enzymology | Collagen - biosynthesis | Protein Processing, Post-Translational | Histones - metabolism | Ketoglutaric Acids - metabolism | Mixed Function Oxygenases - genetics | post-translational modification (PTM) | chemical biology | hydroxylation | protein chemical modification | Minireviews | dioxygenase | enzyme catalysis | protein synthesis | 2-oxoglutarate | hydroxylase | gene expression
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4. Full Text Discovery and industrial applications of lytic polysaccharide mono-oxygenases
by Johansen, Katja S
Biochemical Society Transactions, ISSN 0300-5127, 02/2016, Volume 44, Issue 1, pp. 143 - 149
The recent discovery of copper-dependent lytic polysaccharide mono-oxygenases (LPMOs) has opened up a vast area of research covering several fields of... 
Lytic polysaccharide mono-oxygenase (LPMO) | Ethanol | Copper | Cellulase | Industrial saccharification | Glycoside hydrolase family 61 (GH61) | lytic polysaccharide mono-oxygenase (LPMO) | OXIDATION | GLYCOSIDE HYDROLASE FAMILY | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | cellulase | BINDING PROTEIN CBP21 | SERRATIA-MARCESCENS | MONOOXYGENASE | ethanol | glycoside hydrolase family 61 (GH61) | CELLULOSE DEGRADATION | ENZYME | CELLOBIOSE DEHYDROGENASE | STRUCTURAL BASIS | copper | industrial saccharification | Industry | Substrate Specificity | Mixed Function Oxygenases - metabolism | Ethanol - metabolism | Biofuels | Polysaccharides - metabolism | Kemi | Chemical Sciences
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5. Full Text Physiological and biochemical aspects of hydroxylations and demethylations catalyzed by human 2-oxoglutarate oxygenases
by Loenarz, Christoph and Schofield, Christopher J
Trends in Biochemical Sciences, ISSN 0968-0004, 2011, Volume 36, Issue 1, pp. 7 - 18
Pioneering work in the 1960s defined prolyl and lysyl hydroxylations as physiologically important oxygenase-catalyzed modifications in collagen biosynthesis;... 
AMINO-ACID-SEQUENCE | INHIBITING-HIF FIH | HUMAN PROLYL 4-HYDROXYLASE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | HYPOXIA-INDUCIBLE-FACTOR | CLAVAMINATE SYNTHASE 2 | HUMAN ALKB HOMOLOG | BETA-HYDROXYASPARTIC ACID | NONHEME IRON ENZYME | ANKYRIN REPEAT DOMAIN | Collagen - metabolism | Animals | Hydroxylation | Humans | Mixed Function Oxygenases - metabolism | Mixed Function Oxygenases - chemistry | Catalysis | Methylation
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6. Full Text Amazing Diversity in Biochemical Roles of Fe(II)/2-Oxoglutarate Oxygenases
by Herr, Caitlyn Q and Hausinger, Robert P
Trends in Biochemical Sciences, ISSN 0968-0004, 07/2018, Volume 43, Issue 7, pp. 517 - 532
Since their discovery in the 1960s, the family of Fe(II)/2-oxoglutarate-dependent oxygenases has undergone a tremendous expansion to include enzymes catalyzing... 
translation | biodegradation | Nonheme iron oxygenase | chromatin modification | transcription | biosynthesis | SUBSTRATE-SPECIFICITY | STRUCTURAL BASIS | WOBBLE POSITION | MECHANISTIC INSIGHTS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | DIOXYGENASE | BIOSYNTHETIC-PATHWAY | CATALYTIC MECHANISM | ENZYME FAMILY | NONHEME FE(II) | Protein Biosynthesis | Species Specificity | Humans | Ribosomes - metabolism | Substrate Specificity | Mixed Function Oxygenases - metabolism | Isoenzymes - chemistry | Mixed Function Oxygenases - chemistry | RNA, Messenger - metabolism | Ketoglutaric Acids - chemistry | DNA-Binding Proteins - metabolism | Ribosomes - enzymology | Isoenzymes - metabolism | Ketoglutaric Acids - metabolism | RNA, Transfer - chemistry | Binding Sites | Hydroxylation | RNA Processing, Post-Transcriptional | Isoenzymes - genetics | RNA, Transfer - metabolism | Iron - chemistry | Ribosomes - chemistry | Models, Molecular | Terminology as Topic | DNA-Binding Proteins - chemistry | Iron - metabolism | Animals | Halogenation | RNA, Messenger - chemistry | Protein Processing, Post-Translational | Mixed Function Oxygenases - genetics | Oxidases | Physiological aspects | Genetic translation | non-heme iron oxygenase
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7. Full Text Structure function and engineering of multifunctional non-heme iron dependent oxygenases in fungal meroterpenoid biosynthesis
by Nakashima, Yu and Mori, Takahiro and Nakamura, Hitomi and Awakawa, Takayoshi and Hoshino, Shotaro and Senda, Miki and Senda, Toshiya and Abe, Ikuro
Nature Communications, ISSN 2041-1723, 12/2018, Volume 9, Issue 1, pp. 104 - 104
Non-heme iron and alpha-ketoglutarate (alpha KG) oxygenases catalyze remarkably diverse reactions using a single ferrous ion cofactor. A major challenge in... 
FOLD | ISOPENICILLIN N-SYNTHASE | SUBSTRATE-BINDING | MECHANISM | STRUCTURE REFINEMENT | AUSTINOL | PATHWAY | MULTIDISCIPLINARY SCIENCES | DIOXYGENASE | PHENIX | MODEL | Oxidation-Reduction | Substrate Specificity | Mixed Function Oxygenases - metabolism | Structure-Activity Relationship | Penicillium - metabolism | Catalytic Domain - physiology | Aspergillus nidulans - metabolism | Ketoglutaric Acids - chemistry | Terpenes - chemistry | Terpenes - metabolism | Penicillium - classification | Aspergillus nidulans - enzymology | Mixed Function Oxygenases - genetics | Penicillium - enzymology | Nonheme Iron Proteins - chemistry | Residues | Penicillium | Chemical reactions | Homology | Iron | Biosynthesis | Biocatalysts | Substrates | Mutants | Fungi | Mutagenesis | Heme | Catalysis | Active control | Structure-function relationships | Index Medicus
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8. Full Text Two Distinct Mechanisms for C-C Desaturation by Iron(II)- and 2-(Oxo)glutarate-Dependent Oxygenases: Importance of α-Heteroatom Assistance
by Dunham, Noah P and Chang, Wei-Chen and Mitchell, Andrew J and Martinie, Ryan J and Zhang, Bo and Bergman, Jonathan A and Rajakovich, Lauren J and Wang, Bo and Silakov, Alexey and Krebs, Carsten and Boal, Amie K and Bollinger, J. Martin and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Journal of the American Chemical Society, ISSN 0002-7863, 06/2018, Volume 140, Issue 23, pp. 7116 - 7126
Hydroxylation of aliphatic carbons by nonheme Fe(IV)-oxo (ferryl) complexes proceeds by hydrogen-atom (H center dot) transfer (HAT) to the ferryl and... 
METHANE MONOOXYGENASE | CARBAPENEM SYNTHASE | SPECTROSCOPIC EVIDENCE | STRUCTURAL BASIS | VIOMYCIN BIOSYNTHESIS | HALOGENASE SYRB2 | ALIPHATIC HALOGENASE | KETOGLUTARATE DIOXYGENASE TAUD | NONHEME-IRON | SPIN FE(IV) COMPLEX | CHEMISTRY, MULTIDISCIPLINARY | Hydroxylation | Models, Chemical | Oxidation-Reduction | Stereoisomerism | Homoarginine - chemistry | Iron - chemistry | Deuterium - chemistry | Mixed Function Oxygenases - chemistry | Kinetics | Binding Sites | Ketoglutaric Acids - chemistry
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9. Full Text Discovery and characterization of a new family of lytic polysaccharide monooxygenases
by Hemsworth, Glyn R and Henrissat, Bernard and Davies, Gideon J and Walton, Paul H
Nature chemical biology, ISSN 1552-4450, 2014, Volume 10, Issue 2, pp. 122 - 126
Lytic polysaccharide monooxygenases (LPMOs) are a recently discovered class of enzymes capable of oxidizing recalcitrant polysaccharides. They are attracting... 
GLYCOSIDE HYDROLASE FAMILY | RECOGNITION | CARBOHYDRATE-BINDING MODULES | BIOCHEMISTRY & MOLECULAR BIOLOGY | DEGRADATION | OXYGENASES | PROTEINS | CLEAVAGE | CELLULOSE | NEUROSPORA-CRASSA | INSIGHTS | Protein Structure, Tertiary | Catalytic Domain | Electron Spin Resonance Spectroscopy | Crystallography, X-Ray | Mixed Function Oxygenases - metabolism | Mixed Function Oxygenases - chemistry | Polysaccharides - metabolism | Sequence Alignment | Copper - chemistry | Aspergillus oryzae - enzymology | Base Sequence | Polysaccharides - chemistry | Mixed Function Oxygenases - genetics | Chitinase | Enzymes | Biomass | Bioinformatics | Biodiesel fuels | Substrates
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10. Full Text Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans
by Ge, Wei and Wolf, Alexander and Feng, Tianshu and Ho, Chia-Hua and Sekirnik, Rok and Zayer, Adam and Granatino, Nicolas and Cockman, Matthew E and Loenarz, Christoph and Loik, Nikita D and Hardy, Adam P and Claridge, Timothy D.W and Hamed, Refaat B and Chowdhury, Rasheduzzaman and Gong, Lingzhi and Robinson, Carol V and Trudgian, David C and Jiang, Miao and MacKeen, Mukram M and McCullagh, James S and Gordiyenko, Yuliya and Thalhammer, Armin and Yamamoto, Atsushi and Yang, Ming and Liu-Yi, Phebee and Zhang, Zhihong and Schmidt-Zachmann, Marion and Kessler, Benedikt M and Ratcliffe, Peter J and Preston, Gail M and Coleman, Mathew L and Schofield, Christopher J
Nature Chemical Biology, ISSN 1552-4450, 2012, Volume 8, Issue 12, pp. 960 - 962
The finding that oxygenase-catalyzed protein hydroxylation regulates animal transcription raises questions as to whether the translation machinery and... 
LUNG-CANCER | MDIG | MINA53 | PROTEIN | RNA | BIOCHEMISTRY & MOLECULAR BIOLOGY | MYC TARGET GENE | IDENTIFICATION | JMJC-DOMAIN | EXPRESSION | CELL CARCINOMA | Chromosomal Proteins, Non-Histone - metabolism | Hydroxylation | Magnetic Resonance Spectroscopy | Humans | Enzyme Inhibitors - pharmacology | Ribosomes - metabolism | Escherichia coli Proteins - metabolism | Mixed Function Oxygenases - metabolism | Nuclear Proteins - metabolism | Mixed Function Oxygenases - antagonists & inhibitors | Histidine - metabolism | Oxygenases - antagonists & inhibitors | Ribosomal Proteins - metabolism | Animals | Prokaryotic Cells - metabolism | Histone Demethylases | Oxygenases - metabolism | Escherichia coli - metabolism | Escherichia coli Proteins - antagonists & inhibitors | Arginine - metabolism | Proteins | Antigens | E coli | Prokaryotes | Catalysis | Ribonucleic acid--RNA | Bioinformatics
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11. Full Text Oxidative cleavage of cellulose by fungal copper-dependent polysaccharide monooxygenases
by Beeson, William T and Phillips, Christopher M and Cate, Jamie H. D and Marletta, Michael A
Journal of the American Chemical Society, ISSN 0002-7863, 01/2012, Volume 134, Issue 2, pp. 890 - 892
Fungal-derived, copper-dependent polysaccharide monooxygenases (PMOs), formerly known as GH61 proteins, have recently been shown to catalyze the O-2-dependent... 
GLYCOSIDE HYDROLASE FAMILY | MYCELIOPHTHORA-THERMOPHILA | CELLOBIOSE DEHYDROGENASE | CONVERSION | ENZYMES | DEGRADATION | CHEMISTRY, MULTIDISCIPLINARY | NEUROSPORA-CRASSA | Neurospora crassa - enzymology | Copper - chemistry | Oxidation-Reduction | Mixed Function Oxygenases - metabolism | Mixed Function Oxygenases - chemistry | Carbohydrate Conformation | Dextrins - chemistry | Mixed Function Oxygenases - genetics | Cellulose - analogs & derivatives | Cellulose - metabolism | Polysaccharides | Glycosidic bonds | Analysis | Cellulose | Catalysis | Chemical properties | Elimination reactions
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