Tyramine oxidation by copper/TPQ amine oxidase and peroxidase from Euphorbia characias latex.
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.
Mura
Anna
A
Department of Applied Sciences in Biosystems, University of Cagliari, I-09042 Monserrato, CA, Italy.
Pintus
Francesca
F
Fais
Antonella
A
Porcu
Simona
S
Corda
Marcella
M
Spanò
Delia
D
Medda
Rosaria
R
Floris
Giovanni
G
D006631:Amine Oxidase (Copper-Containing) / Q000302:isolation & purification / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D019281:Dimerization; D028481:Euphorbia / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D015394:Molecular Structure; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000302:isolation & purification / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet; D014439:Tyramine / Q000737:chemistry*
D010544:Peroxidases; D006631:Amine Oxidase (Copper-Containing); D014439:Tyramine