Lipoxygenases: Occurrence, Functions, Catalysis, and Acquisition of Substrate

Lipoxygenases: Occurrence, Functions, Catalysis, and Acquisition of Substrate

August 20, 1999 | Alan R. Brash
Lipoxygenases are enzymes that catalyze the oxidation of polyunsaturated fatty acids, playing roles in signaling, structural changes, and metabolic processes in plants, fungi, and animals. They are found in various tissues and have different catalytic properties, with some forming mixed products and others producing specific hydroperoxides. Lipoxygenases are classified based on their substrate specificity and product formation, such as 12-LOX, 15-LOX, and others. The phylogenetic tree separates plant and animal lipoxygenases into subgroups, with some enzymes showing low sequence identity but similar functions. Lipoxygenases are involved in the synthesis of signaling molecules like leukotrienes and HETEs, which have roles in inflammation and immune responses. They also contribute to membrane peroxidation, which can induce structural changes in cells. Lipoxygenase activity is regulated by various factors, including substrate availability and enzyme structure. The enzyme structure includes a non-heme iron center and a β-barrel domain, with different lipoxygenases having distinct catalytic mechanisms. Some lipoxygenases, like 5-LOX, are involved in the production of leukotrienes and require interactions with other proteins, such as FLAP, for substrate acquisition. Recent discoveries include manganese lipoxygenases and R-lipoxygenases, which may provide new insights into lipoxygenase function and stereospecificity. The study of lipoxygenases continues to reveal their diverse roles in cellular processes and their potential applications in understanding disease mechanisms.Lipoxygenases are enzymes that catalyze the oxidation of polyunsaturated fatty acids, playing roles in signaling, structural changes, and metabolic processes in plants, fungi, and animals. They are found in various tissues and have different catalytic properties, with some forming mixed products and others producing specific hydroperoxides. Lipoxygenases are classified based on their substrate specificity and product formation, such as 12-LOX, 15-LOX, and others. The phylogenetic tree separates plant and animal lipoxygenases into subgroups, with some enzymes showing low sequence identity but similar functions. Lipoxygenases are involved in the synthesis of signaling molecules like leukotrienes and HETEs, which have roles in inflammation and immune responses. They also contribute to membrane peroxidation, which can induce structural changes in cells. Lipoxygenase activity is regulated by various factors, including substrate availability and enzyme structure. The enzyme structure includes a non-heme iron center and a β-barrel domain, with different lipoxygenases having distinct catalytic mechanisms. Some lipoxygenases, like 5-LOX, are involved in the production of leukotrienes and require interactions with other proteins, such as FLAP, for substrate acquisition. Recent discoveries include manganese lipoxygenases and R-lipoxygenases, which may provide new insights into lipoxygenase function and stereospecificity. The study of lipoxygenases continues to reveal their diverse roles in cellular processes and their potential applications in understanding disease mechanisms.
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