Title of article
Whence topa? Models for the biogenesis of topa quinone in copper amine oxidases
Author/Authors
Williams، نويسنده , , Neal K and Klinman، نويسنده , , Judith P، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2000
Pages
7
From page
95
To page
101
Abstract
Copper amine oxidases are dual function enzymes that first make their own cofactor, and then use this cofactor to catalyze amine oxidation. The cofactor, oxidized 2,4,5-trihydroxyphenylalanine (TPQ), is formed by the addition of cupric ion and dioxygen to precursor protein. Drawing on the mechanism of the oxidative half reaction in the copper amine oxidases, together with knowledge from other metal-containing enzyme systems, a new model is put forth for TPQ biogenesis.
Keywords
Quinone , post-translational modification , Cofactor , Copper , Enzyme
Journal title
Journal of Molecular Catalysis B Enzymatic
Serial Year
2000
Journal title
Journal of Molecular Catalysis B Enzymatic
Record number
1708376
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