ArticleACS chemical biology2014
Insights into substrate and metal binding from the crystal structure of cyanobacterial aldehyde deformylating oxygenase with substrate bound.
Article in ACS chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 37 citations in OpenAlex.
- A ferritin-like diiron oxygenase BioE initiates bacterial biotin synthesis, a promising antivirulence target.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Product release and substrate entry of aldehyde deformylating oxygenase revealed by molecular dynamics simulations.Biophysics and physicobiology · 2025Article
- Recent advances in the improvement of cyanobacterial enzymes for bioalkane production.Microbial cell factories · 2022Review
- Ferritin-Like Proteins: A Conserved Core for a Myriad of Enzyme Complexes.Sub-cellular biochemistry · 2022Article
- Hydrocarbon Desaturation in Cyanobacterial Thylakoid Membranes Is Linked With Acclimation to Suboptimal Growth Temperatures.Frontiers in microbiology · 2021Article
- Identification of non-conserved residues essential for improving the hydrocarbon-producing activity of cyanobacterial aldehyde-deformylating oxygenase.Biotechnology for biofuels · 2019Article
- A consensus-guided approach yields a heat-stable alkane-producing enzyme and identifies residues promoting thermostability.The Journal of biological chemistry · 2018Article
- Comparison of orthologous cyanobacterial aldehyde deformylating oxygenases in the production of volatile C3-C7 alkanes in engineeredMetabolic engineering communications · 2017Article
- Divergent mechanisms of iron-containing enzymes for hydrocarbon biosynthesis.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Review
- Identification of residues important for the activity of aldehyde-deformylating oxygenase through investigation into the structure-activity relationship.BMC biotechnology · 2017Article
- Structure-oriented substrate specificity engineering of aldehyde-deformylating oxygenase towards aldehydes carbon chain length.Biotechnology for biofuels · 2016Article
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5 authors at 1 institution in 1 country.
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Abstract
The nonheme diiron enzyme cyanobacterial aldehyde deformylating oxygenase, cADO, catalyzes the highly unusual deformylation of aliphatic aldehydes to alkanes and formate. We have determined crystal structures for the enzyme with a long-chain water-soluble aldehyde and medium-chain carboxylic acid bound to the active site. These structures delineate a hydrophobic channel that connects the solvent with the deeply buried active site and reveal a mode of substrate binding that is different from previously determined structures with long-chain fatty acids bound. The structures also identify a water channel leading to the active site that could facilitate the entry of protons required in the reaction. NMR studies examining 1-[(13)C]-octanal binding to cADO indicate that the enzyme binds the aldehyde form rather than the hydrated form. Lastly, the fortuitous cocrystallization of the metal-free form of the protein with aldehyde bound has revealed protein conformation changes that are involved in binding iron.
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