Lipoxygenases: Occurrence, Functions, Catalysis, and Acquisition of Substrate
Open accessAbstract
hydroxyeicosatetraenoic acid hydroperoxyeicosatetraenoic acid lipoxygenase(s) peroxisome proliferator-activated receptor Src homology 3 domain 5-lipoxygenase-activating protein Lipoxygenase reactions may initiate the synthesis of a signaling molecule or be involved in inducing structural or metabolic changes in the cell. For signaling, synthesis of a single fatty acid hydroperoxide is required. For inducing structural changes, synthesis of a particular product may not be so important as the ability to induce what amounts to an enzyme-catalyzed lipid peroxidation. Reflecting these different functions are lipoxygenases with different characteristics in catalysis. There are enzymes that tightly control the reaction with molecular oxygen and others that form mixed products and permit the release of free radicals. In this review the diversity of lipoxygenase expression will be highlighted and the several facets of lipoxygenase function considered, concluding with a discussion of issues related to the acquisition of substrate in a cellular environment. Lipoxygenases are found widely in plants, fungi, and animals (1Grechkin A. Prog. Lipid Res. 1998; 37: 317-352Crossref PubMed Scopus (269) Google Scholar, 2Gerwick W.H. Biochim. Biophys. Acta. 1994; 1211: 243-255Crossref PubMed Scopus (93) Google Scholar, 3De Petrocellis L. Di Marzo V. Prostaglandins Leukotrienes Essent. Fatty Acids. 1994; 51: 215-229Abstract Full Text PDF PubMed Scopus (49) Google Scholar, 4Funk C.D. Biochim. Biophys. Acta. 1996; 1304: 65-84Crossref PubMed Scopus (238) Google Scholar, 5Yamamoto S. Suzuki H. Ueda N. Prog. Lipid Res. 1997; 36: 23-41Crossref PubMed Scopus (101) Google Scholar). The suitable substrates are polyunsaturated fatty acids containing a series of cis double bonds. These are the essential fatty acids in humans. These substrates are not present in most bacteria (cyanobacteria and some marine species excepted (6Gerwick W.H. Bernart M.W. Attaway D.H. Zaborsky O.R. Marine Bio/Technology, Volume I: Pharmaceutical and Bioactive Natural Products. Plenum Publishing Corp., New York1993: 101-152Google Scholar, 7Watanabe K. Ishikawa C. Ohtsuka I. Kamata M. Tomita M. Yazawa K. Muramatsu H. Lipids. 1997; 32: 975-978Crossref PubMed Scopus (22) Google Scholar)), and yeast also lack the necessary desaturases for their synthesis. In accord with this absence of substrate, there is no lipoxygenase in the yeast genome (Saccharomyces cerevisiae), and lipoxygenases are also absent from typical prokaryotes. There is no definitive account of a lipoxygenase in insects, although a typical arachidonic acid-derived lipoxygenase product (hydroxyeicosatetraenoic acid (HETE)1) is identified in the primitive insect Thermobia domestica (8Ragab A. Durand J. Bitsch C. Chap H. Rigaud M. Insect Biochem. 1991; 21: 321-326Crossref Scopus (13) Google Scholar). There is a lipoxygenase in the unicellular Chlorella (9Zimmerman D.C. Lipids. 1973; 8: 264-266Crossref PubMed Scopus (56) Google Scholar) and a partial lipoxygenase cDNA sequence in the data bases from the slime mold Dictyostelium discoideum. Higher plants contain multiple lipoxygenases with at least eight identified in soybean, Glycine max. In the mouse there are seven genes that express lipoxygenase proteins, and five homologues (and an expressed pseudogene) are characterized in humans (10Krieg P. Kinzig A. Heidt M. Marks F. Fürstenberger G. Biochim. Biophys. Acta. 1998; 1391: 7-12Crossref PubMed Scopus (51) Google Scholar, 11Boeglin W.E. Kim R.B. Brash A.R. Proc. Natl. Acad. Sci. U. S. A. 1998; 95: 6744-6749Crossref PubMed Scopus (148) Google Scholar, 12Sun D. Elsea S.H. Patel P.I. Funk C.D. Cytogenet. Cell Genet. 1998; 81: 79-82Crossref PubMed Scopus (21) Google Scholar). Lipoxygenases are expressed in some plant and animal tissues in high levels; they constitute a few percent of the protein in soybeans, and a 15-lipoxygenase (15-LOX) represents one of the main proteins besides hemoglobin in rabbit reticulocytes during anemia (13Rapoport S.M. Schewe T. Wiesner R. Halangk W. Ludwig P. Janicke-Hohne M. Tannert C. Klatt D. Eur. J. Biochem. 1979; 96: 545-561Crossref PubMed Scopus (230) Google Scholar). Lipoxygenase expression may also be more subtle and low level, as in the cell-specific expression of specific isozymes in soybean leaves (14Stephenson L.C. Bunker T.W. Dubbs W.E. Grimes H.D. Plant Physiol. 1998; 116: 923-933Crossref PubMed Scopus (38) Google Scholar) or the discrete expression of distinct lipoxygenases in mammalian skin (e.g. Ref. 15Jisaka M. Kim R.B. Nanney L.B. Boeglin W.E. Brash A.R. J. Biol. Chem. 1997; 272: 24410-24416Abstract Full Text Full Text PDF PubMed Scopus (98) Google Scholar). The phylogenetic tree separates the plant and animal enzymes and forms several subgroups within each kingdom (Fig.1). The formation of a particular lipoxygenase product is not necessarily associated with closely related sequences. For example, the soybean L-1 enzyme, a 15-LOX, has only 25% identity to any mam
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Lipoxygenases catalyze the insertion of oxygen in polyunsaturated fatty acids.
“Lipoxygenases catalyze the insertion of oxygen in polyunsaturated fatty acids (119, 535, 1040) and are also biological sources of superoxide (537).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [119]
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- Authors
- Brash, A. R.
- Affiliations
- Vanderbilt University (US)
- Corresponding author
- Brash, Alan R.
- ORCID
- Brash, Alan R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1999-08
- Volume
- 274
- Issue
- 34
- Pages
- 23679-23682
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2074203890
- Cited by
- 1,335
- References
- 58
- Citations by year
- 2026: 25 · 2025: 33 · 2024: 36 · 2023: 29 · 2022: 49 · 2021: 46 · 2020: 42 · 2019: 51 · 2018: 53 · 2017: 44 · 2016: 52 · 2015: 59 · 2014: 65 · 2013: 59 · 2012: 63
- FWCI
- 4.60
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM-53638, R01GM053638)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Eicosanoids and Hypertension Pharmacology
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Keywords
- lipoxygenase, fatty acid hydroperoxides, hydroxyeicosatetraenoic acids, lipid peroxidation, eicosanoid signaling, substrate specificity, polyunsaturated fatty acids, peroxisome proliferator-activated receptors, enzyme catalysis
- MeSH terms
- Animals, Catalysis, Humans, Lipoxygenase, Membrane Lipids
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