Benzoic acid inhibition of the α, β, and γ Isozymes of Agaricus bisporus tyrosinase

Menon, Sunitha; Fleck, Robyn W.; Yong, Grace; Strothkamp, Kenneth G.

doi:10.1016/0003-9861(90)90513-x

Cited by 49 publications

(32 citation statements)

References 24 publications

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“…Studies indicate that the flavon-3-ol skeleton with a galloyl moiety at the 3-position is an important structural requirement for optimum inhibition of tyrosinase activity. It is interesting to note that 1,2,3,4,6-Penta-O-galloyl-d-glucose (PGG), the active compound isolated from G. rhois (Kim et al, 1998), has a potent tyrosinase inhibitory activity, although this is not consistent with previous reports that the tyrosinase inhibitory strength of aromatic carboxylic acids decreases with the esterification, hydroxylation or methylation of the benzene ring (Menon et al, 1990;Kermasha et al, 1993). However, gallic acid and its short alkyl (<C10) chain esters were oxidized by tyrosinase as substrates, yielding yellow oxidation products, but the long alkyl (>C10) chain esters inhibited the enzyme without producing pigmented products, indicating that the carbon chain length is related to their tyrosinase inhibitory activity.…”

Section: Tyrosinase Inhibitorsmentioning

confidence: 57%

Naturally occurring tyrosinase inhibitors: mechanism and applications in skin health, cosmetics and agriculture industries

Parvez

Kang

Chung

et al. 2007

Phytotherapy Research

364

260

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Tyrosinase is a copper-containing enzyme, which is widely distributed in microorganisms, animals and plants and is a key enzyme in melanin biosynthesis, involved in determining the color of mammalian skin and hair. In addition, unfavorable enzymatic browning of plant-derived foods by tyrosinase causes a decrease in nutritional quality and economic loss of food products. The inadequacy of current conventional methods to prevent tyrosinase action encourages researchers to seek new potent tyrosinase inhibitors for food and cosmetics. This article presents a study on the importance of tyrosinase, biochemical characteristics, type of inhibitions, activators from various natural sources with its clinical and industrial importance in recent prospects is discussed in this paper.

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Section: Tyrosinase Inhibitorsmentioning

confidence: 57%

Naturally occurring tyrosinase inhibitors: mechanism and applications in skin health, cosmetics and agriculture industries

Parvez

Kang

Chung

et al. 2007

Phytotherapy Research

364

260

View full text Add to dashboard Cite

show abstract

“…Refs. [15][16][17][18][19][20][21][22][23][24]. Yet direct spectroscopic investigations of inhibitor binding to tyrosinases have been few, partly because of the scarcity of suitable spectroscopic probes.…”

mentioning

confidence: 99%

Stopped-flow Fluorescence Studies of Inhibitor Binding to Tyrosinase from Streptomyces antibioticus

Tepper

Bubacco

Canters

2004

Journal of Biological Chemistry

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“…The cloning technique, developed recently, and more detailed kinetic studies (6 -12) have increased the current understanding of Ty mechanism and structure. Additional studies (8,(13)(14)(15)(16) on inhibitors also provided structural information. The importance of the latter studies is related to the considerable interest of Tys from the medical, agricultural, and industrial point of view.…”

mentioning

confidence: 99%

Tyrosinase-catalyzed Oxidation of Fluorophenols

Battaini¹,

Monzani²,

Casella³

et al. 2002

Journal of Biological Chemistry

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The activity of the type 3 copper enzyme tyrosinase toward 2-, 3-, and 4-fluorophenol was studied by kinetic methods and 1 H and 19 F NMR spectroscopy. Whereas 3-and 4-fluorophenol react with tyrosinase to give products that undergo a rapid polymerization process, 2-fluorophenol is not reactive and actually acts as a competitive inhibitor in the enzymatic oxidation of 3,4-dihydroxyphenylalanine (L-dopa). The tyrosinase-mediated polymerization of 3-and 4-fluorophenols has been studied in detail. It proceeds through a phenolic coupling pathway in which the common reactive fluoroquinone, produced stereospecifically by tyrosinase, eliminates an inorganic fluorine ion. The enzymatic reaction studied as a function of substrate concentration shows a prominent lag that is completely depleted in the presence of L-dopa. The kinetic parameters of the reactions can be correlated to the electronic and steric effects of the fluorine substituent position. Whereas the fluorine electron withdrawing effect appears to control the binding of the substrates (K m for 3-and 4-fluorophenols and K I for 2-fluorophenol), the k cat parameters do not follow the expected trend, indicating that in the transition state some additional steric effect rules the reactivity. Tyrosinases (Tys)1 are monooxygenating enzymes that catalyze the ortho-hydroxylation of monophenols and the subsequent oxidation of diphenols to quinones (1). The reaction is widespread in nature, from bacteria to fungi, plants, and mammals. In mammals, when L-tyrosine acts as the substrate, the formed quinones are reactive precursors in the synthesis of melanin pigments. In fruits, vegetables, and mushrooms, Ty is a fundamental enzyme in the browning process that occurs during product storage and upon bruising. Ty contains a dinuclear type 3 copper center, in which two copper ions are closely spaced and coordinated each by three histidines through the N-⑀ nitrogen atoms (1). This type of site has been found and structurally characterized also in hemocyanins, which act as oxygen carriers in arthropods and mollusks (2-4), and in catechol oxidases, which perform the oxidation of o-diphenols to quinones (5). The reasons why these proteins perform different functions, although their catalytic sites appear to be similar both in structure and oxygen binding ability, remains to be clarified (6). During activity, the type 3 site of Ty can exist in three main redox forms: ions are normally bridged by a small ligand (7,8). The cloning technique, developed recently, and more detailed kinetic studies (6 -12) have increased the current understanding of Ty mechanism and structure. Additional studies (8, 13-16) on inhibitors also provided structural information. The importance of the latter studies is related to the considerable interest of Tys from the medical, agricultural, and industrial point of view. For instance, Ty inhibitors are of great concern in the cosmetic industry (17) and in food technology as anti-browning agents (18,19). Moreover, the tyrosinases present in soil have been fo...

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Benzoic acid inhibition of the α, β, and γ Isozymes of Agaricus bisporus tyrosinase

Cited by 49 publications

References 24 publications

Naturally occurring tyrosinase inhibitors: mechanism and applications in skin health, cosmetics and agriculture industries

Naturally occurring tyrosinase inhibitors: mechanism and applications in skin health, cosmetics and agriculture industries

Stopped-flow Fluorescence Studies of Inhibitor Binding to Tyrosinase from Streptomyces antibioticus

Tyrosinase-catalyzed Oxidation of Fluorophenols

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