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Effect of the insect phenoloxidase on the metabolism of l ‐DOPA
Author(s) -
Wu Kai,
Han Fang,
Yuan Yi,
Liu Yining,
Ling Erjun,
Wang Qian,
Huang Wuren
Publication year - 2018
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.21457
Subject(s) - prophenoloxidase , proteases , biochemistry , biology , cetylpyridinium chloride , serine , serine protease , activator (genetics) , insect , enzyme , protease , microbiology and biotechnology , innate immune system , receptor , botany , pulmonary surfactant
Insect prophenoloxidase (PPO) induces melanization around pathogens. Before melanization, PPO is cleaved into phenoloxidase (PO) by serine proteases. Insect PPO can also be activated by exogenous proteases secreted by pathogens as well as by other compounds, such as ethanol and cetylpyridinium chloride (CPC). However, the effect of these activators on the activity of PO is unclear. In this study, the insect endogenous serine protease AMM1, α‐chymotrypsin, and ethanol were used to activate recombinant Drosophila PPO1 (rPPO1), and the PO activity differed depending on the activator applied. The PO‐induced intermediates during melanization also varied markedly in their numbers and abundances. Therefore, this study indicates that the mechanism of PPO activation influences PO activity. It also suggests that PO‐induced different intermediates may affect the antibacterial activity during melanization due to their toxicity.