The Effect of D-(−)-arabinose on Tyrosinase: An Integrated Study Using Computational Simulation and Inhibition Kinetics. (23rd December 2012)

• Record Type: Journal Article
• Authors: Liu, Hong-Jian; Ji, Sunyoung; Fan, Yong-Qiang; Yan, Li; Yang, Jun-Mo; Zhou, Hai-Meng; Lee, Jinhyuk; Wang, Yu-Long
• Other Names: Saboury Ali-Akbar Academic Editor.
• Is Part Of: Enzyme research. Volume 2012(2012)
• Publication Date: 2012-12-23
• Subjects: Enzymes -- Periodicals; 572.7
• DOI: 10.1155/2012/731427
• Languages: English
• ISSNs: 2090-0406

Abstract

Abstract : Tyrosinase is a ubiquitous enzyme with diverse physiologic roles related to pigment production. Tyrosinase inhibition has been well studied for cosmetic, medicinal, and agricultural purposes. We simulated the docking of tyrosinase and D-(−)-arabinose and found a binding energy of −4.5 kcal/mol for theup-formof D-(−)-arabinose and −4.4 kcal/mol for thedown-form of D-(−)-arabinose. The results of molecular dynamics simulation suggested that D-(−)-arabinose interacts mostly with HIS85, HIS259, and HIS263, which are believed to be in the active site. Our kinetic study showed that D-(−)-arabinose is a reversible, mixed-type inhibitor of tyrosinase (α -value = 6.11 ± 0.98, K i = 0.21 ± 0.19 M). Measurements of intrinsic fluorescence showed that D-(−)-arabinose induced obvious tertiary changes to tyrosinase (binding constantK = 1.58 ± 0.02 M −1, binding numbern = 1.49 ± 0.06 ). This strategy of predicting tyrosinase inhibition based on specific interactions of aldehyde and hydroxyl groups with the enzyme may prove useful for screening potential tyrosinase inhibitors.