Abstract:
:Fumaric acid (FA), which is naturally found in organisms, is a well known intermediate of the citric acid cycle. We evaluated the effects of FA on tyrosinase activity and structure via enzyme kinetics and computational simulations. FA was found to be a reversible inhibitor of tyrosinase and its induced mechanism was the parabolic non-competitive inhibition type with IC50=13.7±0.25mM and Kislope=12.64±0.75mM. We newly established the equation for the dissociation constant (Kislope) for the parabolic inhibition type in this study. Kinetic measurements and spectrofluorimetry studies showed that FA induced regional changes in the active site of tyrosinase. One possible binding site for FA was identified under the condition without L-DOPA. The computational docking simulations further revealed that FA can interact with HIS263 and HIS85 at the active site. Furthermore, four important hydrogen bonds were found to be involved with the docking of FA on tyrosinase. Our study provides insight into the mechanism by which dicarboxylic acids such as FA inhibit tyrosinase. By inhibiting tyrosinase and its central role in pigment production, FA is a potential natural antipigmentation agent.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Gou L,Lee J,Yang JM,Park YD,Zhou HM,Zhan Y,Lü ZRdoi
10.1016/j.ijbiomac.2016.12.013subject
Has Abstractpub_date
2017-12-01 00:00:00pages
1663-1669issue
Pt 3eissn
0141-8130issn
1879-0003pii
S0141-8130(16)32781-7journal_volume
105pub_type
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