Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1926785 | Archives of Biochemistry and Biophysics | 2008 | 7 Pages |
Abstract
Tyramine, an important plant intermediate, was found to be a substrate for two proteins, a copper amine oxidase and a peroxidase from Euphorbia characias latex. The oxidation of tyramine took place by two different mechanisms: oxidative deamination to p-hydroxyphenylacetaldehyde by the amine oxidase and formation of di-tyramine by the peroxidase. The di-tyramine was further oxidized at the two amino groups by the amino oxidase, whereas p-hydroxyphenylacetaldehyde was transformed to di-p-hydroxyphenylacetaldehyde by the peroxidase. Data obtained in this study indicate a new interesting scenario in the metabolism of tyramine.
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Authors
Anna Mura, Francesca Pintus, Antonella Fais, Simona Porcu, Marcella Corda, Delia Spanò, Rosaria Medda, Giovanni Floris,