AOAH [SEP] found in taxon
acid sequence of the human enzyme is almost 50% identical to that of the AOAH found in Dictyostelium discoideum, with 100% identity in the GDSL lipase consensus sequences. The enzyme has been found in many invertebrates and all vertebrates studied to date except fish. Although it seems likely that the enzyme has substrates in vivo other than LPS (it can be a phospholipase A1/B and acyl transferase in vitro), none has been identified.
A polymorphism in the gene has been associated with chronic rhinosinusitis in 2 different ethnic
recently been shown that a specific enzyme in the intestine (alkaline phosphatase) can detoxify LPS by removing the two phosphate groups found on LPS carbohydrates. This may function as an adaptive mechanism to help the host manage potentially toxic effects of gram-negative bacteria normally found in the small intestine. A different enzyme may detoxify LPS when it enters, or is produced in, animal tissues. Neutrophils, macrophages, and dendritic cells produce a lipase, acyloxyacyl hydrolase (AOAH), that inactivates LPS by removing the two secondary acyl chains