ArticleBiomolecules2026
Tyrosinase-Mediated Oxidation of Endocannabinoid and Endovanilloid N-Arachidonoyl Dopamine and N-Arachidonoyl Tyrosine.
Article in Biomolecules, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Endocannabinoids are lipid mediators consisting of esters, amides and ethers of long-chain polyunsaturated fatty acids. In this work, attention was focused on N-arachidonoyl tyrosine (NA-Tyr) and N-arachidonoyl dopamine (NADA), the amides of arachidonic acid with tyrosine and dopamine, respectively. NADA is an endogenous ligand of both type 1 cannabinoid receptors and type 1 vanilloid channel receptors. NADA is considered an endogenous compound with capsaicin-like activity and is distributed in several brain areas. The metabolic fate of endocannabinoids involves numerous enzymatic activities, which are only partially characterized. In particular, the biological activity of these biomolecules is terminated by enzymes with hydrolytic or oxygenase/oxidase activity. As part of this problem, we studied the oxidation of NADA and NA-Tyr mediated by mushroom tyrosinase. Our experimental data show that tyrosinase can oxidize both NADA and NA-Tyr. The oxidation of these biomolecules was also carried out in the presence of cysteine, allowing us to observe the formation of endocannabinoid/endovanilloid adducts with cysteine. These results were derived from chromatographic analyses and mass spectral experiments. During the tyrosinase-mediated oxidation in the presence of cysteine, it was possible to observe the production of a melanin-like pigment. The spectral characteristics of this pigment are consistent with those of pheomelanin, the pigment that contributes to the structure of neuromelanin. While mushroom tyrosinase serves here as a convenient biomimetic model to investigate the oxidative susceptibility of NADA and NA-Tyr, extrapolating these in vitro findings to mammalian physiology requires caution. Nevertheless, considering the neuronal distribution of these precursors and the documented, albeit debated, presence of tyrosinase-like activity in the central nervous system (CNS), these results offer a chemical rationale to further investigate whether similar oxidative pathways occur in vivo and potentially contribute to neurodegenerative mechanisms.
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