The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
The Three-Dimensional Structure of an Arachidonic Acid 15-Lipoxygenase
Abstract
In mammals, the hydroperoxidation of arachidonic acid by lipoxygenases leads to the formation of leukotrienes and lipoxins, compounds that mediate inflammatory responses. Lipoxygenases are dioxygenases that contain a nonheme iron and are present in many animal cells. Soybean lipoxygenase-1 is a single-chain, 839-residue protein closely related to mammalian lipoxygenases. The structure of soybean lipoxygenase-1 solved to 2.6 angstrom resolution shows that the enzyme has two domains: a 146-residue β barrel and a 693-residue helical bundle. The iron atom is in the center of the larger domain and is coordinated by three histidines and the COO - of the carboxyl terminus. The coordination geometry is nonregular and appears to be a distorted octahedron in which two adjacent positions are not occupied by ligands. Two cavities, in the shapes of a bent cylinder and a frustum, connect the unoccupied positions to the surface of the enzyme. The iron, with two adjacent and unoccupied positions, is poised to interact with the 1,4-diene system of the substrate and with molecular oxygen during catalysis.
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Cites
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Leukotrienes: Mediators of Immediate Hypersensitivity Reactions and Inflammation
Samuelsson, B. (1983) · Science · doi:10.1126/science.6301011 · Cited by 2,843
Analytical molecular surface calculation
Connolly, M. L. (1983) · Journal of Applied Crystallography · doi:10.1107/s0021889883010985 · Cited by 2,508
Leukotrienes and Lipoxins: Structures, Biosynthesis, and Biological Effects
Samuelsson, B., Dahlén, S.-E., Lindgren, J. Å., Rouzer, C. A., & Serhan, C. N. (1987) · Science · doi:10.1126/science.2820055 · Cited by 2,233
Crystallographic R Factor Refinement by Molecular Dynamics
Brünger, A. T., Kuriyan, J., & Karplus, M. (1987) · Science · doi:10.1126/science.235.4787.458 · Cited by 1,956
Structure of human pancreatic lipase
Winkler, F. K., D'Arcy, A., & Hunziker, W. (1990) · Nature · doi:10.1038/343771a0 · Cited by 1,224
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[53] Lipoxygenase from soybeans
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Recent investigations into the lipoxygenase pathway of plants
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Cited by
Protein Radicals in Enzyme Catalysis
Stubbe, J., & van der Donk, W. A. (1998) · Chemical Reviews · doi:10.1021/cr9400875 · Cited by 1,377
Lipoxygenases: Occurrence, Functions, Catalysis, and Acquisition of Substrate
Brash, A. R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.34.23679 · Cited by 1,335
Lipoxygenase and leukotriene pathways: biochemistry, biology, and roles in disease
Haeggström, J. Z., & Funk, C. D. (2011) · Chemical Reviews · doi:10.1021/cr200246d · Cited by 875
Papuc, C., Goran, G. V., Predescu, C. N., Nicorescu, V., & Stefan, G. (2017) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12298 · Cited by 561
Role of leukotrienes revealed by targeted disruption of the 5-lipoxygenase gene
Chen, X.-S., Shelter, J. R., Johnson, E. N., & Funk, C. D. (1994) · Nature · doi:10.1038/372179a0 · Cited by 414
Metadata
- Authors
- Boyington, J. C., Gaffney, B. J., & Amzel, L. M.
- Venue
- Science
- Published
- 1993-06-04
- Volume
- 260
- Issue
- 5113
- Pages
- 1482-1486
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2104512614
- Cited by
- 462
- References
- 31
- FWCI
- 33.03
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
