Journal
BIOCHEMISTRY-MOSCOW
Volume 68, Issue 4, Pages 487-491Publisher
MAIK NAUKA/INTERPERIODICA/SPRINGER
DOI: 10.1023/A:1023620501702
Keywords
mushroom tyrosinase; flavonoids; inhibitory mechanism
Categories
Ask authors/readers for more resources
Mushroom tyrosinase (EC 1.14.18.1) is a copper containing oxidase that catalyzes both the hydroxylation of tyrosine into o-diphenols and the oxidation of o-diphenols into o-quinones, and then forms brown or black pigments. In the present study, the effects of some flavonoids on the oxidation of L-3,4-dihydroxyphenylalanine (L-DOPA) have been studied. The results show that flavonoids can lead to reversible inhibition of the enzyme. A kinetic analysis showed that the flavonols are competitive inhibitors, whereas luteolin is an uncompetitive inhibitor. The rank order of inhibition was: quercetin>galangin>morin; fisetin >3,7,4'-trihydroxyflavone; luteolin>apigenin>chrysin.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available