Tyramine oxidation by copper/TPQ amine oxidase and peroxidase from Euphorbia characias latex |
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Authors: | Mura Anna Pintus Francesca Fais Antonella Porcu Simona Corda Marcella Spanò Delia Medda Rosaria Floris Giovanni |
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Affiliation: | Department of Applied Sciences in Biosystems, University of Cagliari, I-09042 Monserrato, CA, Italy |
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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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Keywords: | Euphorbia characias Amine oxidase Peroxidase Tyramine |
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