LTA4H Human

LTA4H is a bifunctional zinc enzyme that not only acts as a hydrolase but also possesses aminopeptidase activity . The enzyme’s structure includes a zinc-binding domain essential for its catalytic activity. The reaction it catalyzes involves the addition of a water molecule to the epoxide ring of LTA4, resulting in the formation of LTB4 . This reaction is highly specific and stereospecific, ensuring the precise conversion of LTA4 to LTB4 .

Leukotrienes, including LTB4, play significant roles in various physiological and pathological processes. LTB4 is known for its ability to attract and activate leukocytes, contributing to the inflammatory response . Variations in the LTA4H gene have been linked to susceptibility to multiple diseases, including myocardial infarction, stroke, and asthma .

Recombinant human LTA4H is produced using baculovirus expression systems in insect cells, such as Spodoptera frugiperda (Sf21) . This recombinant protein is often used in research to study the enzyme’s function, structure, and potential as a therapeutic target. The recombinant form is typically purified to high levels of purity and tested for specific activity to ensure its functionality in experimental applications .

Research on LTA4H has led to the development of inhibitors that could potentially be used to treat inflammatory diseases. By inhibiting LTA4H, the production of LTB4 can be reduced, thereby mitigating the inflammatory response . This approach holds promise for conditions such as asthma, rheumatoid arthritis, and other inflammatory disorders.