The inhibitory effect of ethylenediamine on mushroom tyrosinase.
The inhibitory effect of ethylenediamine on both activities of mushroom tyrosinase (MT) at 20 °C in a 10 mM phosphate buffer solution (pH 6.8), was studied. L-DOPA and L-tyrosine were used as substrates of catecholase and cresolase activities, respectively. The results showed that ethylenediamine competitively inhibits both activities of the enzyme with inhibition constants (K(i)) of 0.18±0.05 and 0.14±0.01 μM for catecholase and cresolase respectively, which are lower than the reported values for other MT inhibitors. For further insight a docking study between tyrosinase and ethylenediamine was performed. The docking simulation showed that ethylenediamine binds in the active site of the enzyme near the Cu atoms and makes 3 hydrogen bonds with two histidine residues of active site.
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.
Mahdi
M
Alijanianzadeh
Ali Akbar
AA
Saboury
Mohammad Reza
MR
Ganjali
Hamid
H
Hadi-Alijanvand
Ali Akbar
AA
Moosavi-Movahedi
D000363:Agaricales / Q000201:enzymology*; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D005029:Ethylenediamines / Q000494:pharmacology*; D007700:Kinetics; D008958:Models, Molecular; D014442:Monophenol Monooxygenase / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation
D004791:Enzyme Inhibitors; D005029:Ethylenediamines; C031234:ethylenediamine; D014442:Monophenol Monooxygenase