Horseradish peroxidase-catalyzed conjugation of eugenol with basic amino acids
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Preparation and In Vivo Use of an Activity-based Probe for N-acylethanolamine Acid Amidase
Published on: November 23, 2016
M H Medeiros1, P Di Mascio, A P Pinto
1Instituto de Química da Universidade de Säo Paulo, Brazil. mhgdmede@quim.iq.usp.br
Abstract:
L-Lysine is shown to yield an adduct with the quinone methide intermediate formed during the horseradish peroxidase (HRP)-catalyzed aerobic oxidation of eugenol (4-allyl-2-methoxyphenol). Adduct formation is evidenced by (i) lysine quenching of the characteristic quinone methide absorption band measured at 350 nm; arginine and gamma-aminobutyric acid, but not alanine or propionic acid showed similar behaviour (ii) lysine-promoted a 400 mV decrease of the eugenol oxidation voltammetric wave (1.00 V), concomitantly with an increase in current intensity and (iii) reverse phase HPLC isolation of the lysine eugenol adduct, followed by GC-MS analysis. The MS spectrum is consistent with a 2:1 lysine:eugenol adduct (MW = 455). If operative in vivo, binding of lysine to eugenol might lead to protein inactivation and possibly be involved in eugenol toxicity.
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