ArticleThe Journal of biological chemistry2010
Crystal structures of ethanolamine ammonia-lyase complexed with coenzyme B12 analogs and substrates.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 100 citations in OpenAlex.
- Gut Microbial Choline TMA-Lyase CutC: From Metabolic Mechanism to a Novel Therapeutic Target for Diseases.Nutrients · 2026Review
- Many paths, similar destinations: viruses and bacterial microcompartments form polyhedra inside cells.Journal of virology · 2026Review
- Novel chemistry and structural perspectives in vitamin BChemical science · 2026Review
- A Multi-Functional Heterogeneous Biocatalyst for the Oxygen-Free Oxidative Condensation of Primary Alcohols into β‑Hydroxy Acids.ACS catalysis · 2026Article
- Chymotrypsin digestion analysis of glycyl radical and B12-dependent radical enzymes indicates common substrate-induced structural shifts.Scientific reports · 2025Article
- Spectroscopic and Computational Insights into the Mechanism of Cofactor Cobalt-Carbon Bond Homolysis by the Adenosylcobalamin-Dependent Enzyme Ethanolamine Ammonia-Lyase.Journal of the American Chemical Society · 2025Article
- Mechanistic Insights from the Crystal Structure and Computational Analysis of the Radical SAM Deaminase DesII.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- IntegrativemSystems · 2024Article
- Native and nonnative reactions in ethanolamine ammonia-lyase are actuated by different dynamics.Biophysical journal · 2023Article
- Reactivity Tracking of an Enzyme Progress Coordinate.The journal of physical chemistry letters · 2023Article
- Confinement dependence of protein-associated solvent dynamics around different classes of proteins, from the EPR spin probe perspective.Physical chemistry chemical physics : PCCP · 2022Article
- Structure-Based Demystification of Radical Catalysis by a Coenzyme BAngewandte Chemie (International ed. in English) · 2022Article
- Structure-Based Demystification of Radical Catalysis by a Coenzyme BAngewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022Article
- Chemical probing provides insight into the native assembly state of a bacterial microcompartment.Structure (London, England : 1993) · 2022Article
- Resolution and characterization of contributions of select protein and coupled solvent configurational fluctuations to radical rearrangement catalysis in coenzyme BMethods in enzymology · 2022Article
- Molecular basis of C-S bond cleavage in the glycyl radical enzyme isethionate sulfite-lyase.Cell chemical biology · 2021Article
- Role of the CarH photoreceptor protein environment in the modulation of cobalamin photochemistry.Biophysical journal · 2021Article
- Energy Conservation in Fermentations of Anaerobic Bacteria.Frontiers in microbiology · 2021Review
- Article
- Mobile loop dynamics in adenosyltransferase control binding and reactivity of coenzyme BProceedings of the National Academy of Sciences of the United States of America · 2020Article
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
N-terminal truncation of the Escherichia coli ethanolamine ammonia-lyase beta-subunit does not affect the catalytic properties of the enzyme (Akita, K., Hieda, N., Baba, N., Kawaguchi, S., Sakamoto, H., Nakanishi, Y., Yamanishi, M., Mori, K., and Toraya, T. (2010) J. Biochem. 147, 83-93). The binary complex of the truncated enzyme with cyanocobalamin and the ternary complex with cyanocobalamin or adeninylpentylcobalamin and substrates were crystallized, and their x-ray structures were analyzed. The enzyme exists as a trimer of the (alphabeta)(2) dimer. The active site is in the (beta/alpha)(8) barrel of the alpha-subunit; the beta-subunit covers the lower part of the cobalamin that is bound in the interface of the alpha- and beta-subunits. The structure complexed with adeninylpentylcobalamin revealed the presence of an adenine ring-binding pocket in the enzyme that accommodates the adenine moiety through a hydrogen bond network. The substrate is bound by six hydrogen bonds with active-site residues. Argalpha(160) contributes to substrate binding most likely by hydrogen bonding with the O1 atom. The modeling study implies that marked angular strains and tensile forces induced by tight enzyme-coenzyme interactions are responsible for breaking the coenzyme Co-C bond. The coenzyme adenosyl radical in the productive conformation was modeled by superimposing its adenine ring on the adenine ring-binding site followed by ribosyl rotation around the N-glycosidic bond. A major structural change upon substrate binding was not observed with this particular enzyme. Glualpha(287), one of the substrate-binding residues, has a direct contact with the ribose group of the modeled adenosylcobalamin, which may contribute to the substrate-induced additional labilization of the Co-C bond.
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