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Research Article

Suicide inactivation of tyrosinase in its action on tetrahydropterines

, , , , , & show all
Pages 728-733 | Received 05 Oct 2010, Accepted 13 Dec 2010, Published online: 08 Feb 2011
 

Abstract

Tetrahydrobiopterin (BH4), methyl-tetrahydropterin (MBH4) and dimethyl-tetrahydropterin (DMBH4) are oxidized by tyrosinase in a process during which the suicide inactivation of tyrosinase may occur. From the kinetic study of this process, (apparent maximum constant for the suicide inactivation), (Michaelis constant for the substrate) and r (number of turnovers that the enzyme makes before the inactivation) can be obtained. From the results obtained, it can be deduced that the velocity of the inactivation governed by () and the potency of the same () follow the order: BH4 > MBH4 > DMBH4.

Acknowledgements

This article was partially supported by grants from the Ministerio de Educación y Ciencia (Madrid, Spain) Project BIO2009–12956, from the Fundación Séneca (CARM, Murcia, Spain) Projects 08856/PI/08 and 08595/PI/08 and from the Consejería de Educación (CARM, Murcia, Spain) BIO-BMC 06/01-0004. F.G.M. and J.L.M.M. have fellowships from Fundación Caja Murcia (Murcia, Spain).

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