Tyramine oxidase
Tyramine oxidase is an enzyme that catalyzes the oxidation of tyramine, a naturally occurring monoamine compound. This enzyme plays a crucial role in the metabolism of tyramine in the body.
Function[edit | edit source]
Tyramine oxidase is primarily involved in the metabolism of tyramine, a compound found in various foods and beverages. It catalyzes the oxidation of tyramine to p-hydroxyphenylacetaldehyde, ammonia, and hydrogen peroxide. This reaction is part of the body's mechanism for breaking down excess tyramine in the diet.
Structure[edit | edit source]
Like other oxidoreductase enzymes, tyramine oxidase is a protein that contains a cofactor, which is necessary for its catalytic activity. The cofactor for tyramine oxidase is flavin adenine dinucleotide (FAD), a type of flavin that is involved in various oxidation-reduction reactions in the body.
Clinical significance[edit | edit source]
Abnormalities in the function of tyramine oxidase can lead to an excess of tyramine in the body, which can cause a condition known as tyramine intolerance. This condition can result in symptoms such as headaches, high blood pressure, and heart palpitations.
See also[edit | edit source]
References[edit | edit source]
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