Specificity of the enzyme phenoloxidase and possible metabolic pathway of sclerotization in Paraplerurus sauridae.
Activity of phenoloxidase in Paraplerurus sauridae on various substrates has been studied spectrophotometrically. The enzyme was shown to be nonspecific and capable of oxidizing both mono- and diphenols. It showed greater activity to some of the mono- and diphenols. Substrates with acidic side chain were oxidized less effectively. Based on the activity of the enzyme on different substrates, a possible metabolic pathway of sclerotization has been suggested.
D000818:Animals; D004156:Catechol Oxidase / Q000378:metabolism*; D002396:Catechols / Q000378:metabolism; D004298:Dopamine / Q000378:metabolism; D006873:Hydroquinones / Q000378:metabolism; D007980:Levodopa / Q000378:metabolism; D014442:Monophenol Monooxygenase / Q000378:metabolism; D011520:Protocatechuate-3,4-Dioxygenase / Q000378:metabolism; D013379:Substrate Specificity; D014200:Trematoda / Q000201:enzymology*; D014439:Tyramine / Q000378:metabolism; D014443:Tyrosine / Q000378:metabolism
D002396:Catechols; D006873:Hydroquinones; D014443:Tyrosine; D007980:Levodopa; D004156:Catechol Oxidase; D011520:Protocatechuate-3,4-Dioxygenase; D014442:Monophenol Monooxygenase; D004298:Dopamine; D014439:Tyramine