title: Tyrosinase activity and hemocyanin in the hemolymph of the slipper lobster Scyllarides latus.
abstract: The respiratory protein hemocyanin is present in molluscans and in some species of arthropods, and its dioxygen binding site strongly resembles that of the monophenol-hydroxylating and catechol-quinonising enzyme tyrosinase. Moreover, some hemocyanins show a certain extent of tyrosinase activity, so a common ancestry between the two proteins has been suggested. However, in the case purified hemocyanin of Scyllarides latus any attempts to evoke tyrosinase activity failed. A distinct tyrosinase has been purified to homogeneity from the hemolymph, and kinetically characterised. The purified tyrosinase showed both monophenolase and diphenolase enzyme activity and therefore it could be well defined as a true tyrosinase. This finding suggests that in the case of the studied crustacean the evolutionary functional divergence between dioxygen transport and oxidation of phenolics has already reached its completeness.
authors: Department of Sciences Applied to Biosystems, University of Cagliari, Cittadella Universitaria, 09042, Monserrato (CA), Italy.
authors: Alessandra
authors: A
authors: Olianas
authors: Enrico
authors: E
authors: Sanjust
authors: Mariagiuseppina
authors: M
authors: Pellegrini
authors: Antonio
authors: A
authors: Rescigno
mesh_terms: D000818:Animals; D002850:Chromatography, Gel; D003124:Colorimetry; D033364:Decapoda / Q000737:chemistry* / Q000201:enzymology*; D004587:Electrophoresis, Agar Gel; D005260:Female; D006433:Hemocyanins / Q000737:chemistry* / Q000302:isolation & purification; D006458:Hemolymph / Q000737:chemistry* / Q000378:metabolism*; D007700:Kinetics; D008297:Male; D008970:Molecular Weight; D014442:Monophenol Monooxygenase / Q000097:blood / Q000302:isolation & purification / Q000378:metabolism*; D013053:Spectrophotometry
chemical_list: D006433:Hemocyanins; D014442:Monophenol Monooxygenase