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Kinetic Study on the Slow Inhibition of Epidermis Tyrosinase by M-Coumaric Acid

Kinetic Study on the Slow Inhibition of Epidermis Tyrosinase by M-Coumaric Acid

J Cabanes, F García-Carmona, F García-Cánovas, J L Iborra, J A Lozano

Biochim Biophys Acta. 1984 Oct 23;790(2):101-7.

PMID: 6435675

Abstract:

The inhibition by m-coumaric acid of oxidation of L-dopa by epidermis tyrosinase (monophenol,dihydroxy-L-phenylalanine:oxygen oxidoreductase, EC 1.14.18.1) is characterized by a prolonged transient phase. Kinetic data correspond to that for a postulated mechanism that involves rapid formation of a reduced enzyme-m-coumaric acid complex that subsequently undergoes a relatively slow reversible reaction. An overall inhibition constant for m-coumaric acid of 0.05 mM was calculated. The value of the Ki for the dissociation of m-coumaric acid from the rapidly formed complex was calculated as 0.53 mM. The first-order rate constants for the slow isomerization of the enzyme-inhibitor complex were calculated as 3.0 +/- 0.1 min-1 for the forward step and 0.31 +/- 0.06 min-1 for the reverse step.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP588307	m-Coumaric acid		588-30-7	Price

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