ArticleNature communications2019
Aspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
30 citing papers in PubMed, 50 citations in OpenAlex.
- Structural and Functional Validation of Pseudomonas Savastanoi Ethylene Forming Enzymes Reveals Flexibility in 2-Oxoglutarate Binding Mode and Conformation.Chembiochem : a European journal of chemical biology · 2026Article
- Structural basis of the promiscuity of the unusual Fe(II) and 2-oxoglutarate dependent human aspartate/asparagine-β-hydroxylase.Nature communications · 2026Article
- Nonheme Fe Enzyme-Catalyzed Enantiodivergent Nitrogen Migration: Directed Evolution and Computational Study of Isopenicillin N Synthases for Biocatalytic Synthesis of Arylglycines.Angewandte Chemie (International ed. in English) · 2026Article
- Profiling Inhibitor Scaffolds for the Cancer Target Jumonji-C Domain-Containing Protein 6.ChemMedChem · 2025Article
- Derivatives of the Clinically Used HIF Prolyl Hydroxylase Inhibitor Desidustat Are Efficient Inhibitors of Human γ-Butyrobetaine Hydroxylase.Journal of medicinal chemistry · 2025Article
- Effects of Clinical Mutations in the Second Coordination Sphere and Remote Regions on the Catalytic Mechanism of Non-Heme Fe(II)/2-Oxoglutarate-Dependent Aspartyl Hydroxylase AspH.Chemphyschem : a European journal of chemical physics and physical chemistry · 2024Article
- Unusual catalytic strategy by non-heme Fe(ii)/2-oxoglutarate-dependent aspartyl hydroxylase AspH.Chemical science · 2024Article
- Structure-guided optimisation ofChemical science · 2023Article
- Catalysis by KDM6 Histone Demethylases - A Synergy between the Non-Heme Iron(II) Center, Second Coordination Sphere, and Long-Range Interactions.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- 5-Substituted Pyridine-2,4-dicarboxylate Derivatives Have Potential for Selective Inhibition of Human Jumonji-C Domain-Containing Protein 5.Journal of medicinal chemistry · 2023Article
- Kinetic and inhibition studies on human Jumonji-C (JmjC) domain-containing protein 5.RSC chemical biology · 2023Article
- Substrate selectivity and inhibition of histidine JmjC hydroxylases MINA53 and NO66.RSC chemical biology · 2023Article
- Natural and synthetic 2-oxoglutarate derivatives are substrates for oncogenic variants of human isocitrate dehydrogenase 1 and 2.The Journal of biological chemistry · 2023Article
- Exploring links between 2-oxoglutarate-dependent oxygenases and Alzheimer's disease.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2022Review
- 2-Oxoglutarate derivatives can selectively enhance or inhibit the activity of human oxygenases.Nature communications · 2021Article
- Fluorinated derivatives of pyridine-2,4-dicarboxylate are potent inhibitors of human 2-oxoglutarate dependent oxygenases.Journal of fluorine chemistry · 2021Article
- Human Oxygenase Variants Employing a Single Protein FeAngewandte Chemie (International ed. in English) · 2021Article
- Human Oxygenase Variants Employing a Single Protein FeAngewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021Article
- 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.BMC research notes · 2021Article
- Current Views on the Roles ofBiomolecules · 2021Review
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Authors and funding
15 authors at 2 institutions in 2 countries.
Funding
Abstract
AspH is an endoplasmic reticulum (ER) membrane-anchored 2-oxoglutarate oxygenase whose C-terminal oxygenase and tetratricopeptide repeat (TPR) domains present in the ER lumen. AspH catalyses hydroxylation of asparaginyl- and aspartyl-residues in epidermal growth factor-like domains (EGFDs). Here we report crystal structures of human AspH, with and without substrate, that reveal substantial conformational changes of the oxygenase and TPR domains during substrate binding. Fe(II)-binding by AspH is unusual, employing only two Fe(II)-binding ligands (His679/His725). Most EGFD structures adopt an established fold with a conserved Cys1-3, 2-4, 5-6 disulfide bonding pattern; an unexpected Cys3-4 disulfide bonding pattern is observed in AspH-EGFD substrate complexes, the catalytic relevance of which is supported by studies involving stable cyclic peptide substrate analogues and by effects of Ca(II) ions on activity. The results have implications for EGFD disulfide pattern processing in the ER and will enable medicinal chemistry efforts targeting human 2OG oxygenases.
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