Titolo:  Tyramine oxidation by copper/TPQ amine oxidase and peroxidase from Euphorbia characias latex
Autori: 
Data di pubblicazione:  2008
Rivista: 
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS  
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.
Handle:  http://hdl.handle.net/11584/104926
Tipologia: 1.1 Articolo in rivista

File in questo prodotto:
Non ci sono file associati a questo prodotto.

Questionario e social

Condividi su: