A new type of uncompetitive inhibition of tyrosinase induced by Cl- binding.
A new type of Cl- induced inhibition of mushroom derived tyrosinase has been detected in this study, and it is defined as the reversible partial hyperbolic uncompetitive inhibition. The Cl- binding site was only induced at the state of the enzyme-substrate complex, and this was confirmed with the intrinsic fluorescence changes. As the oxygen bridge is broken by L-DOPA binding, Cl- simultaneously binds to the ES state to form the ESI complex. It is worth noticing that tyrosinase reacts sensitively to Cl- in the manner of a complex interaction, and this indicates that Cl- might be physiologically involved in the regulation of tyrosinase activity.
Park
Yong-Doo
YD
Department of Dermatology, Sungkyunkwan University School of Medicine, Samsung Medical Center, 50 Ilwon-dong, Kangnam-Ku, 135-710 Seoul, South Korea.
Kim
So-Yeon
SY
Lyou
You-Jeong
YJ
Lee
Jin-Young
JY
Yang
Jun-Mo
JM
D000643:Ammonium Chloride / Q000494:pharmacology; D001665:Binding Sites; D002712:Chlorides / Q000737:chemistry / Q000494:pharmacology*; D020128:Inhibitory Concentration 50; D007700:Kinetics; D014442:Monophenol Monooxygenase / Q000037:antagonists & inhibitors* / Q000737:chemistry; D011189:Potassium Chloride / Q000494:pharmacology; D012965:Sodium Chloride / Q000494:pharmacology; D013050:Spectrometry, Fluorescence
D002712:Chlorides; D000643:Ammonium Chloride; D012965:Sodium Chloride; D011189:Potassium Chloride; D014442:Monophenol Monooxygenase