The effect of polyamines on tyrosinase activity
Galindo, J.D.; Martinez, J.H.; Lopez-Ballester, J.A.; Peñafiel, R.; Solano, F.; Lozano, J.A.
Biochemistry International 15(6): 1151-1158
1987
ISSN/ISBN: 0158-5231 PMID: 3125836 Document Number: 304581
The effect of several polyamines on the activity of tyrosinase from different sources has been studied. Diaminoethane, 1,3-diaminopropane and putrescine activated tyrosinase from Harding-Passey mouse melanoma but did not activate frog epidermis or mushroom tyrosinases, 1,3-diaminopropane was the strongest activator (K.alpha. = 0.23mM). The activation was saturable and dependent on the ionic strength. Cadaverine, 1,6-diaminohexane and spermidine had no effect on any tyrosinase. However, spermine inhibited melanoma tyrosinase more than the mushroom and frog epidermis enzymes. These results show that the effect of polyamines on mammalian tyrosinase is due to direct enzyme-oligoamine interactions rather than to a nonspecific action on L-dopa oxidation products, and suggest that physiological polyamines might play a modulatory role on mammalian melanogenesis.