Xiao-Xin Chen, Jian Zhang,

Wei-Ming Chai, Hui-Ling Feng,Zhi-Hao Xiang, Dong-Yan Shen, Qing-Xi Chen.International

Journal of Biological Macromolecules, 2013. 62: 726-733.

In the present work, we investigated the inhibitory effects of

amoxicillin, a bacteriolytic -lactam antibiotic drug, on the rate of monophenol

hydroxylation and o-diphenol oxidation catalyzed by mushroomtyrosinase. The

results showed that amoxicillin could inhibit both monophenolase and

diphenolase activities. For monophenolase activity, the inhibition on reaction

rate was dose-dependent, while the influenceon lag period was not obvious. For

diphenolase activity, amoxicillin was found to be a reversible inhibitor,with

an IC50value of 9.0±1.8

mM. Kinetics analysis showed that amoxicillin was a mixed type inhibitorof the

enzyme with KIand KISvalues of 8.30 mM and 44.79 mM, respectively. Further, the

molecularmechanism underlying the inhibition of tyrosinse by amoxicillin was

investigated by means of fluorescence quenching and molecular docking

techniques. The results showed that amoxicillin could formstatic interaction

with the catalytic pocket of the enzyme through the interaction of amoxicillin

with thedicopper irons and amino acid residues in the enzyme active center. Our

results contributed to the usageof amoxicillin as a potential tyrosinase

inhibitor in the field of medicinal industry and could also provideguidance in

the design of novel tyrosinase inhibitors.

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