Polyphenol oxidase produced during encystation of Acanthamoeba castellanii.
Acanthamoeba castellanii has a phenol oxidase activity that is believed to be a laccase. Enzyme activity was found in the outer cyst wall, in the cytoplasm of encysting amoebae and in the encystment medium. Encystment procedures were modified to promote an increase in the amount of soluble enzyme secreted during encystation. Acanthamoeba polyphenol oxidase has a pH optimum of 6.0 and a Km value of 0.21 mM with dihydroxyphenylalanine. The enzyme does not oxidize tyrosine, and it is inhibited by chloride but not by inhibitors of peroxidase. Its synthesis coincides with encystation, and known inhibitors of polyphenol oxidase prevent encystation. Polyphenol oxidase may have a role in making the cyst resistant to mechanical and chemical breakdown.
D000656:Amoeba / Q000201:enzymology* / Q000502:physiology; D000818:Animals; D004156:Catechol Oxidase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D002712:Chlorides / Q000494:pharmacology; D004295:Dihydroxyphenylalanine / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D012995:Solubility; D013696:Temperature
D002712:Chlorides; D004295:Dihydroxyphenylalanine; D004156:Catechol Oxidase