Inhibition of tyrosinase activity by N,N-unsubstituted selenourea derivatives.
This study investigated inhibitory effects of N,N-unsubstituted selenourea derivatives on tyrosinase activity. Three types of N,N-unsubstituted selenoureas derivatives exhibited inhibitory effect on dopa (3,4-dihydroxyphenylalanine) oxidase activity of mushroom tyrosinase. Compound D at a concentration of 200 microM exhibited 55.5% of inhibition on dopa oxidase activity of mushroom tyrosinase. This inhibitory effect was higher than that of kojic acid (39.4%), a well known tyrosinase inhibitor. Moreover, the compound D identified as a noncompetitive inhibitor by Lineweaver-Burk plot analysis. In addition, compound D also inhibited the melanin production in melan-a cells.
Ha
Sang Keun
SK
Graduate School of East-West Medical Science, Kyung Hee University, Suwon 449-701, Korea.
Koketsu
Mamoru
M
Lee
Kunho
K
Choi
Sang Yoon
SY
Park
Ji-Ho
JH
Ishihara
Hideharu
H
Kim
Sun Yeou
SY
D002460:Cell Line; D004305:Dose-Response Relationship, Drug; D004789:Enzyme Activation / Q000187:drug effects / Q000502:physiology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006801:Humans; D014442:Monophenol Monooxygenase / Q000037:antagonists & inhibitors* / Q000378:metabolism; D016566:Organoselenium Compounds / Q000737:chemistry / Q000494:pharmacology*; D014508:Urea / Q000031:analogs & derivatives* / Q000737:chemistry / Q000494:pharmacology
D004791:Enzyme Inhibitors; D016566:Organoselenium Compounds; C081959:selenourea; D014508:Urea; D014442:Monophenol Monooxygenase