AbstractThe first three-dimensional structure of copper amine oxidase demonstrates that one tyrosine residue is converted into 2,4,5-trihydroxyphenylalanine quinone (TPQ). TPQ binds to copper in the inactive form of the enzyme but not in the active form
The mechanism of molecular oxygen activation is the subject of controversy in the copper amine oxida...
Copper amine oxidases (CAOs) are responsible for the oxidative deamination of primary amines to thei...
Copper amine oxidases (CuAOs) are metalloenzymes that reduce molecular oxygen to hydrogen peroxide d...
AbstractThe first three-dimensional structure of copper amine oxidase demonstrates that one tyrosine...
AbstractBackground: Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that cata...
AbstractBackground Copper-containing amine oxidases catalyze the oxidative deamination of primary am...
Copper amine oxidases (CAOs) catalyze the oxidative deamination of primary amines to their correspon...
AbstractBackground Copper-containing amine oxidases catalyze the oxidative deamination of primary am...
Copper amine oxidases are homodimeric enzymes containing one Cu(2+) ion and one 2,4,5-trihydroxyphen...
Copper amine oxidases (CuAOs) are ubiquitous, copper containing, homodimeric enzymes that possess a ...
AbstractBackground: Copper-containing amine oxidases (CAOs) are widespread in nature. These enzymes ...
Adduct I (λmax at ∼430 nm) formed in the reaction of 2-hydrazinopyridine (2HP) and the TPQ cofactor ...
The mechanism of molecular oxygen activation is the subject of controversy in the copper amine oxida...
Copper amine oxidases (CAOs) are a class of enzymes that contain Cu2+ and a tyrosine-derived quinone...
Copper amine oxidases (CAOs) are a class of enzymes that contain Cu2+ and a tyrosine-derived quinone...
The mechanism of molecular oxygen activation is the subject of controversy in the copper amine oxida...
Copper amine oxidases (CAOs) are responsible for the oxidative deamination of primary amines to thei...
Copper amine oxidases (CuAOs) are metalloenzymes that reduce molecular oxygen to hydrogen peroxide d...
AbstractThe first three-dimensional structure of copper amine oxidase demonstrates that one tyrosine...
AbstractBackground: Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that cata...
AbstractBackground Copper-containing amine oxidases catalyze the oxidative deamination of primary am...
Copper amine oxidases (CAOs) catalyze the oxidative deamination of primary amines to their correspon...
AbstractBackground Copper-containing amine oxidases catalyze the oxidative deamination of primary am...
Copper amine oxidases are homodimeric enzymes containing one Cu(2+) ion and one 2,4,5-trihydroxyphen...
Copper amine oxidases (CuAOs) are ubiquitous, copper containing, homodimeric enzymes that possess a ...
AbstractBackground: Copper-containing amine oxidases (CAOs) are widespread in nature. These enzymes ...
Adduct I (λmax at ∼430 nm) formed in the reaction of 2-hydrazinopyridine (2HP) and the TPQ cofactor ...
The mechanism of molecular oxygen activation is the subject of controversy in the copper amine oxida...
Copper amine oxidases (CAOs) are a class of enzymes that contain Cu2+ and a tyrosine-derived quinone...
Copper amine oxidases (CAOs) are a class of enzymes that contain Cu2+ and a tyrosine-derived quinone...
The mechanism of molecular oxygen activation is the subject of controversy in the copper amine oxida...
Copper amine oxidases (CAOs) are responsible for the oxidative deamination of primary amines to thei...
Copper amine oxidases (CuAOs) are metalloenzymes that reduce molecular oxygen to hydrogen peroxide d...
DOI
Add to ORKG