Insights into mechanism of oxidative deamination catalyzed by DOPA decarboxylase

Authors :: Bertoldi, Mariarita
Cellini, Barbara
Montioli, Riccardo
Voltattorni, Carla Borri
Source :: Biochemistry. July 8, 2008, Vol. 47 Issue 27, 7187-7195
Publication Year :: 2008
Abstract: The unusual oxygen-consuming oxidative deamination reaction catalyzed by the pyridoxal 5'-phosphate (PLP) enzyme DOPA decarboxylase (DDC) is examined. The catalytic properties of the T246A DDC mutant has shown that the Thr246-His192 dyad could act as a general base in promoting the first step of the oxidative deamination of aromatic amines.

Subjects :: Catalysis -- Analysis
Mutation (Biology) -- Analysis
Oxidation-reduction reaction -- Analysis
Vitamin B6 -- Chemical properties
Biological sciences
Chemistry

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