ArticleThe Journal of biological chemistry2009
X-ray crystal structure of michaelis complex of aldoxime dehydratase.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 68 citations in OpenAlex.
- Radical Ring-Opening Reaction of Non-Activated Oximes Catalyzed by Aldoxime Dehydratases.Angewandte Chemie (International ed. in English) · 2025Article
- Cyanogenic millipede genome illuminates convergent evolution of cyanogenesis-related enzymes.PLoS genetics · 2025Article
- Aldoxime dehydratases: production, immobilization, and use in multistep processes.Applied microbiology and biotechnology · 2024Review
- Enzymatic properties of a non-classical aldoxime dehydratase capable of producing alkyl and arylalkyl nitriles.Applied microbiology and biotechnology · 2023Article
- Article
- Rationalizing the Unprecedented Stereochemistry of an Enzymatic Nitrile Synthesis through a Combined Computational and Experimental Approach.Angewandte Chemie (International ed. in English) · 2021Article
- Protein engineering of the aldoxime dehydratase from Bacillus sp. OxB-1 based on a rational sequence alignment approach.Scientific reports · 2021Article
- De novo biosynthesis of a nonnatural cobalt porphyrin cofactor inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Synthetic Processes toward Nitriles without the Use of Cyanide: A Biocatalytic Concept Based on Dehydration of Aldoximes in Water.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Effect of Particle Wettability and Particle Concentration on the Enzymatic Dehydration of n-Octanaloxime in Pickering Emulsions.Angewandte Chemie (International ed. in English) · 2021Article
- Understanding molecular enzymology of porphyrin-binding α + β barrel proteins - One fold, multiple functions.Biochimica et biophysica acta. Proteins and proteomics · 2021Review
- X-ray-induced photoreduction of heme metal centers rapidly induces active-site perturbations in a protein-independent manner.The Journal of biological chemistry · 2020Article
- Biocatalytic production of adiponitrile and related aliphatic linear α,ω-dinitriles.Nature communications · 2018Article
- New function of aldoxime dehydratase: Redox catalysis and the formation of an unexpected product.PloS one · 2017Article
- Cytochrome P450 CYP71AT96 catalyses the final step of herbivore-induced phenylacetonitrile biosynthesis in the giant knotweed, Fallopia sachalinensis.Plant molecular biology · 2016Article
- Evolutionary relationships between heme-binding ferredoxin α + β barrels.BMC bioinformatics · 2016Article
- Substrate, product, and cofactor: The extraordinarily flexible relationship between the CDE superfamily and heme.Archives of biochemistry and biophysics · 2015Review
- Generation of complexity in fungal terpene biosynthesis: discovery of a multifunctional cytochrome P450 in the fumagillin pathway.Journal of the American Chemical Society · 2014Article
- Crystal structure of aldoxime dehydratase and its catalytic mechanism involved in carbon-nitrogen triple-bond synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Amino acid substrate specificities and tissue expression profiles of the nine CYP79A encoding genes in Sorghum bicolor.Physiologia plantarumArticle
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6 authors at 3 institutions in 1 country.
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Abstract
Aldoxime dehydratase (Oxd) catalyzes the dehydration of aldoximes (R-CH=N-OH) to their corresponding nitrile (R-C triple bond N). Oxd is a heme-containing enzyme that catalyzes the dehydration reaction as its physiological function. We have determined the first two structures of Oxd: the substrate-free OxdRE at 1.8 A resolution and the n-butyraldoxime- and propionaldoxime-bound OxdREs at 1.8 and 1.6 A resolutions, respectively. Unlike other heme enzymes, the organic substrate is directly bound to the heme iron in OxdRE. We determined the structure of the Michaelis complex of OxdRE by using the unique substrate binding and activity regulation properties of Oxd. The Michaelis complex was prepared by x-ray cryoradiolytic reduction of the ferric dead-end complex in which Oxd contains a Fe(3+) heme form. The crystal structures reveal the mechanism of substrate recognition and the catalysis of OxdRE.
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