Catalysis and inhibition of tyrosinase in the presence of cinnamic acid and some of its derivatives

Garcia-Jimenez, Antonio, García-Molina, Francisco, Teruel-Puche, Jose, Saura-Sanmartin, Adrian, Garcia-Ruiz, Pedro, Ortiz-Lopez, Antonio, Rodríguez-López, Jose, Garcia-Canovas, Francisco and Munoz, Jose (2018) Catalysis and inhibition of tyrosinase in the presence of cinnamic acid and some of its derivatives. International Journal of Biological Macromolecules, 119. pp. 548-554. ISSN 0141-8130

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Abstract

The kinetic action of tyrosinase on l-tyrosine and l-Dopa as substrates in the presence of cinnamic acid and some of its derivatives has been characterized. Cinnamic acid, 2-hydroxycinnamic, 2,3 and 4-methoxycinnamic acids were seen to be inhibitors of tyrosinase being determined the type of inhibition and inhibition constants of all of them. However, 3-hydroxycinnamic, 4-hydroxycinnamic and 3,4-dihydroxycinnamic acids were seen to be substrates of tyrosinase at the same time. The kinetic constants of the catalysis of these substrates were determined and found to be perfectly correlated with the chemical shifts of the carbon with the phenolic hydroxyl group revealed by NMR. Docking studies of 2-hydroxycinnamic and 3-hydroxycinnamic acids showed that tyrosinase is able to hydroxylate 3-hydroxycinnamic acid but is unable to hydroxylate 2-hydroxycinnamic acid.

Item Type:	Article
Uncontrolled Keywords:	Tyrosinase inhibition, Cinnamic acid alternative substrate, Docking
Subjects:	C700 Molecular Biology, Biophysics and Biochemistry
Department:	Faculties > Health and Life Sciences > Applied Sciences
Depositing User:	Becky Skoyles
Date Deposited:	28 Jan 2019 13:13
Last Modified:	11 Oct 2019 14:16
URI:	http://nrl.northumbria.ac.uk/id/eprint/37768

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