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Kinetic study in the transient phase of the suicide inactivation of frog epidermis tyrosinase.

作者信息

Tudela J, Garcia Cánovas F, Varón R, Jiménez M, Garcia-Carmona F, Lozano J A

机构信息

Departamento de Bioquimica y Biologia Molecular, Universidad de Murcia, Spain.

出版信息

Biophys Chem. 1988 Jul 15;30(3):303-10. doi: 10.1016/0301-4622(88)85025-7.

DOI:10.1016/0301-4622(88)85025-7
PMID:3145040
Abstract

This paper deals with the kinetic study of a multisubstrate mechanism with enzyme inactivation induced by a suicide substrate. A transient phase approach has been developed that enables the deduction of explicit equations of product concentration vs. time. From these equations kinetic constants which characterize the suicide substrate can be obtained. This study with tyrosinase enzyme, which acts on L-dopa and catechol allowed us to determine the corresponding kinetic parameters, indicating that catechol is about 8-times more powerful as a suicide substrate than is L-dopa.

摘要

相似文献

1
Kinetic study in the transient phase of the suicide inactivation of frog epidermis tyrosinase.
Biophys Chem. 1988 Jul 15;30(3):303-10. doi: 10.1016/0301-4622(88)85025-7.
2
Kinetic study on the suicide inactivation of tyrosinase induced by catechol.儿茶酚诱导酪氨酸酶自杀失活的动力学研究
Biochim Biophys Acta. 1987 Apr 30;912(3):417-23. doi: 10.1016/0167-4838(87)90047-1.
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引用本文的文献

1
Kinetics of an enzyme reaction in which both the enzyme-substrate complex and the product are unstable or only the product is unstable.酶 - 底物复合物和产物均不稳定或仅产物不稳定的酶促反应动力学。
Biochem J. 1994 Oct 15;303 ( Pt 2)(Pt 2):435-40. doi: 10.1042/bj3030435.