Enzymatic Synthesis of 3′‐Hydroxyacetaminophen Catalyzed by Tyrosinase

Valero, Edelmira; Lozano, Mms; Varón, R.; García-Carmona, Francisco

doi:10.1021/bp034075t

Cited by 11 publications

(8 citation statements)

References 33 publications

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“…The attainment of the o-diphenol is in agreement with the general behavior of tyrosinase when acting on monophenols under reducing conditions (Valero et al, 2003). To evaluate the possibility that dopaxanthin was a substrate of the diphenolase activity of the enzyme, a solution of the pigment was prepared in phosphate buffer, pH 6.0, and tyrosinase was added.…”

Section: Extraction and Purification Of Dopaxanthin From Yellow Flowesupporting

confidence: 67%

Betaxanthins as Substrates for Tyrosinase. An Approach to the Role of Tyrosinase in the Biosynthetic Pathway of Betalains

Escribano

García-Carmona

2005

Plant Physiology

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Tyrosinase or polyphenol oxidase (EC 1.14.18.1) is the key enzyme in melanin biosynthesis and in the enzymatic browning of fruits and vegetables. The role of tyrosinase in the secondary metabolism of plants still remains unclear, but its implication in betalain biosynthesis has been proposed. Betalains are an important class of water-soluble pigments, characteristic of plants belonging to the order Caryophyllales. In this article, the betaxanthins, tyrosine-betaxanthin (portulacaxanthin II) and dopaxanthin, are reported to be physiological substrates for tyrosinase. The direct activity of tyrosinase on selected betaxanthins is characterized in depth, and conversion of tyrosine-betaxanthin to dopaxanthin and its further oxidation to a series of compounds are described. Identity of the reaction products was studied by high-performance liquid chromatography and electrospray ionization-mass spectrometry. Masses determined for the reaction products were the same in all cases, 389 m/z ([M 1 H] 1 ) and equal to that determined for betanidin. Data indicate that dopaxanthin-quinone is obtained and evolves to more stable species by intramolecular cyclization. Kinetic parameters for tyrosinase acting on dopaxanthin were evaluated, showing a high affinity for this substrate (K m 5 84.3 mM). The biosynthetic scheme of betalains is reviewed and a branch is proposed based on the description of physiological substrates for tyrosinase. Lampranthus productus, Glottiphylum oligocarpum, and Glottiphylum pigmaeum are described as sources of stereopure (2S/S)-dopaxanthin.Tyrosinase or polyphenol oxidase (monophenol, o-diphenol:oxygen oxidoreductase; EC 1.14.18.1) is a copper enzyme that catalyzes two different reactions using molecular oxygen: the hydroxylation of monophenols to o-diphenols (monophenolase activity) and the oxidation of the o-diphenols to o-quinones (diphenolase activity; Sánchez-Ferrer et al., 1995). This enzyme is widely distributed in plants, microorganisms, and animals where tyrosinase is responsible for melanization.A wide variety of plant tyrosinase behaviors has been described and reviewed (Mayer and Harel, 1991;van Gelder et al., 1997). A molecular oxygenscavenging function in the chloroplast (Vaughn et al., 1988) and a role in plant defense (Constabel et al., 1995) have been suggested. Its implication in the secondary metabolism of betalains has been proposed (Steiner et al., 1999), but the physiological function of tyrosinase in higher plants is yet to be fully determined.Betalains are water-soluble nitrogen-containing pigments that are present in plants belonging to the order Caryophyllales (Strack et al., 2003) and in the fungal genera Amanita (Musso, 1979) and Hygrocybe (von Ardenne et al., 1974). All betalain pigments contain betalamic acid as the chromophore. Depending upon the nature of the betalamic acid addition residue, the betalains can be classified as either betacyanins or betaxanthins. Betacyanins contain a cyclo-3,4-dihydroxyphenylalanine (cyclo-DOPA; usually glycosylated) residue and exhibit ...

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Section: Extraction and Purification Of Dopaxanthin From Yellow Flowesupporting

confidence: 67%

Betaxanthins as Substrates for Tyrosinase. An Approach to the Role of Tyrosinase in the Biosynthetic Pathway of Betalains

Escribano

García-Carmona

2005

Plant Physiology

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“…The peak derived from the activity of tyrosinase was assigned to dopaminebetaxanthin by co-elution and comparison of spectral properties with dopamine-betaxanthin directly synthesized from betalamic acid. The o-diphenol obtained is in agreement with the general behavior of tyrosinase when acting on monophenols under reducing conditions (Valero et al 2003) and indicates that the quinone was formed, although it could not be detected in the absence of AA.…”

Section: Enzymatic Conversion Of Tyramine-betaxanthin To Dopamine-betsupporting

confidence: 81%

Characterization of the monophenolase activity of tyrosinase on betaxanthins: the tyramine-betaxanthin/dopamine-betaxanthin pair

Escribano

García-Carmona

2005

Planta

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Tyrosinase or polyphenol oxidase (EC 1.14.18.1) is the key enzyme responsible for melanin biosynthesis and for the enzymatic browning of fruits and vegetables. Although the function of tyrosinase in the secondary metabolism of plants remains unclear, it has been proposed that the enzyme plays a role in the betalain biosynthetic pathway. Betalains are an important class of water-soluble pigments, characteristic of plants belonging to the order Caryophyllales. In the present work, the betaxanthins tyramine-betaxanthin (miraxanthin III) and dopamine-betaxanthin (miraxanthin V) are reported as new natural substrates for tyrosinase. The result of the diphenolase activity of the enzyme on dopamine-betaxanthin was a series of products identified by HPLC and ESI-MS as quinone-derivatives. Data indicate that dopamine-betaxanthin-quinone is obtained and evolves to more stable species by intramolecular cyclization. The kinetic parameters evaluated for the diphenolase activity were V(m) = 74.4 microM min(-1), K(m) = 94.7 microM. Monophenolase activity on tyramine-betaxanthin yielded the same compounds in the absence of a reducing agent, but when ascorbic acid was present enzymatic conversion to dopamine-betaxanthin could be found. For the first time, kinetic characterization of the monophenolase activity of tyrosinase on betaxanthins is provided (V(m) = 10.4 microM min(-1) and K(m) = 126.9 microM) and a lag period is described and analyzed according to the mechanism of action of the enzyme. The high affinity shown by tyrosinase for these substrates may be indicative of a previously unconsidered physiological role in betalain metabolism. A possible mechanism for the formation of 2-descarboxy-betacyanins from tyramine-betaxanthin by tyrosinase is also discussed.

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“…Previously, we reported that similar to levodopa, the potency of α-methyldopa, a catecholic oral drug, was rapidly diminished by enzymes present in bananas [ 3 ]. Meanwhile, mushroom-derived tyrosinase was determined to catalyze the catecholation reaction by the oxidation of acetaminophen [ 8 , 9 ]. In our study, loss of acetaminophen potency in the presence of bananas may be due to the abundance of polyphenol oxidase, which normally catalyzes the conversion of tyrosine ( Fig 1 ).…”

Section: Discussionmentioning

confidence: 99%

“…Indeed, ions derived from the metabolite were confirmed on the LC/ESI/MS spectrum ( Fig 7 ). The oxidation reaction catalyzed by 3-hydroxyacetaminofen tyrosinase activity is reported to be reversibly inhibited by ascorbic acid [ 8 ]. Conversely, to prove that the tyrosinase in bananas causes the interaction, we must show that PPO from bananas converts acetaminophen into APAP oxide.…”

Section: Discussionmentioning

confidence: 99%

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Bananas decrease acetaminophen potency in in vitro assays

Uesawa

Tsuji²

2018

PLoS ONE

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Edible portions of bananas contain high levels of polyphenol oxidase, which catalyzes reactions in the melanin formation pathway. Tyrosine, a physiological substrate of polyphenol oxidase, has an analogous structure to acetaminophen. We investigated whether banana extract causes structural changes in acetaminophen and a decrease in its potency. Acetaminophen concentration in banana extract was measured under different conditions to characterize incompatibility. Reaction products in solution were identified using liquid chromatography/electrospray ionization/mass spectrometry (LC/ESI/MS). Acetaminophen potency decreased with time in the presence of banana extract. The reaction proceeded most efficiently in temperatures 30–37°C and neutral to weakly acidic conditions. Molecular ion peaks derived from the oxidized catechol moiety of acetaminophen were identified in LC/ESI/MS spectra. Our findings suggest that incorporation or simultaneous administration of acetaminophen medication and banana juice may result in decreased efficacy of the clinically important drug. This interaction is likely due to the oxidation of acetaminophen by polyphenol oxidase activity in banana pulp. Therefore, we investigated and characterized a novel interaction between bananas and acetaminophen. To establish a safe and effective antipyretic analgesic regimen using acetaminophen, future studies of this interaction are expected to be performed in humans.

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Enzymatic Synthesis of 3′‐Hydroxyacetaminophen Catalyzed by Tyrosinase

Cited by 11 publications

References 33 publications

Betaxanthins as Substrates for Tyrosinase. An Approach to the Role of Tyrosinase in the Biosynthetic Pathway of Betalains

Betaxanthins as Substrates for Tyrosinase. An Approach to the Role of Tyrosinase in the Biosynthetic Pathway of Betalains

Characterization of the monophenolase activity of tyrosinase on betaxanthins: the tyramine-betaxanthin/dopamine-betaxanthin pair

Bananas decrease acetaminophen potency in in vitro assays

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