[Proteolytic activation of prophenoloxidase in the imago of musca domestica].
The enzyme phenoloxidase complex of insects generally localized in cuticle and hemolymph, presents in the form of inactive proenzymes, which may be actitivated under the influence of a range of enzymes, components of the "phenoloxidase activated system" or "prophenoloxidase cascade". Currently the whole chain of the reactions is not clear, but it includes esterases, which activate serine proteinase, including terminal proteinase, acid phosphatase, some dehydrogenase, and protein kinase. The typhoid fly imago has monophenol-monooxygenase (MPMO) in the form of proenzyme, which is activated under the influence of endogenous and exogenous proteases. These results allow to suppose that the form MPMO with REM 0.06 is aggregated derivative of the form with REM 0.23. Relative substrate analysis of proteolytically activated MPMO of phtalophos-sensitive and phtalophos-resistant typhoid fly strains demonstrates that the second one has increased affinity for p-diphenol-hydroquinone.
N M
NM
Kutuzova
D D
DD
Deviatnikov
E A
EA
Ianykina
D000818:Animals; D004789:Enzyme Activation / Q000502:physiology; D004792:Enzyme Precursors / Q000378:metabolism; D006793:Houseflies / Q000201:enzymology*; D019476:Insect Proteins / Q000378:metabolism*; D007814:Larva / Q000201:enzymology; D014442:Monophenol Monooxygenase / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism*
D004792:Enzyme Precursors; D019476:Insect Proteins; D014442:Monophenol Monooxygenase; D010447:Peptide Hydrolases