o-Diphenol oxidase activity of molluscan hemocyanins.
Diphenoloxidase activities of two molluscan hemocyanins, isolated from the marine snails Rapana venosa and garden snails Helix vulgaris were studied using o-diphenol and L-Dopa as substrates. The dimers of H. vulgaris Hc show both, diphenol (K(m)=2.86 mM and K(cat)=4.48) and L-Dopa activity due to a more open active sites of the enzyme and better access of the substrates. The K(m) value of molluscan H. vulgaris Hc is very close to those of Helix pomatia and Sepia officinalis Hcs, but several times higher compared to those of Rapana and Octopus Hcs. Also HvH has a very high enzyme activity compared with other molluscan Hcs. Kinetic measurements with native RvH and both structural subunits, RvH1 and RvH2, show that RvH and only one structural subunit, RvH2, exhibited only o-diphenol activity, but no L-Dopa oxidizing activity.
Hristova
Rumyana
R
Institute of Organic Chemistry, Bulgarian Academy of Sciences, G. Bonchev 9, Sofia 1113, Bulgaria.
Dolashki
Alexandar
A
Voelter
Wolfgang
W
Stevanovic
Stefan
S
Dolashka-Angelova
Pavlina
P
D000595:Amino Acid Sequence; D000818:Animals; D002384:Catalysis; D004156:Catechol Oxidase / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D006433:Hemocyanins / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D007700:Kinetics; D008969:Molecular Sequence Data; D008974:Mollusca / Q000201:enzymology*; D010084:Oxidation-Reduction; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism
D021122:Protein Subunits; D006433:Hemocyanins; D004156:Catechol Oxidase