Inhibitory effects of salicylic acid family compounds on the diphenolase activity of mushroom tyrosinase

Zhang, Jiping; Chen, Qing‐Xi; Song, Kangkang; Jin-jin, Xie

doi:10.1016/j.foodchem.2005.01.042

Cited by 85 publications

(45 citation statements)

References 12 publications

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“…Tyrosinase is a key enzyme in the melanin biosynthesis; it plays an important role in catalyzing hydroxylation of monophenol to o-diphenol and the oxidation of diphenol to o-quinones [4]. Its abnormal expression is responsible for the various dermatological disorders, such as melasma, freckles, senile lentigines, age spots, and sites of actinic damage [1,5] and it also contributes to the browning of some fruits and vegetables during handling and storage which will debase the taste and nutrition value of them [6]. For the import role of tyrosinase in the melanin biosynthesis, the control of the tyrosinase activity is of great importance in preventing formation of the unfavorable darkening.…”

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confidence: 99%

Inhibitory Effects of Fatty Acids on the Activity of Mushroom Tyrosinase

Guo

Pan

Chen

et al. 2010

Appl Biochem Biotechnol

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The effects of fatty acids, octanoic acid, (2E, 4E)-hexa-2,4-dienoic acid, hexanoic acid, (2E)-but-2-enoic acid, and butyric acid on the activities of mushroom tyrosinase have been investigated. The results showed that the fatty acids can potently inhibit both monophenolase activity and diphenolase activity of tyrosinase, and that the unsaturated fatty acids exhibited stronger inhibitory effect against tyrosinase than the corresponding saturated fatty acids, and the inhibitory effects were enhanced with the extendability of the fatty acid chain. For the monophenolase activity, the fatty acids could not only lengthen the lag period, but also decrease the steady-state activities. For the diphenolase activity, fatty acids displayed reversible inhibition. Kinetic analyses showed that octanoic acid and hexanoic acid were mixed-type inhibitors and (2E,4E)-hexa-2,4-dienoic acid and (2E)-but-2-enoic acid were noncompetitive inhibitors. The inhibition constants have been determined and compared.

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confidence: 99%

Inhibitory Effects of Fatty Acids on the Activity of Mushroom Tyrosinase

Guo

Pan

Chen

et al. 2010

Appl Biochem Biotechnol

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“…These two constants were determined from the second plots of LineweaverBurk plots, the slopes of the straight lines or vertical intercept (1/V max ) versus the concentration of each inhibitor. These parameters are given in Equations (1)-(3) [17,18] …”

Section: Kinetic Assay Of Hne and Progress Linear Determinationmentioning

confidence: 99%

Prenylated Flavonoids from Epimedium koreanum Nakai and their Human Neutrophil Elastase Inhibitory Effects

Lee¹,

Song²,

Uddin³

et al. 2017

Rec.Nat.Prod.

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Human neutrophil elastase (HNE) has been linked to immune system functions, including inflammation, as well as the development of skin wrinkles, suggesting that HNE inhibitors have many practical applications. In this study, the methanol extract of Epimedium koreanum Nakai contained potent HNE inhibitory flavonoids (1-4) with IC 50 values of 6.06-125.80 μM. Prenyl groups within these flavonoids were critical for the inhibitory effects. For example, epimedokoreanin B (1) (IC 50 = 6.06 μM) showed 6-fold higher efficacy than that of its parent luteolin (IC 50 = 36.01 μM). A similar trend was observed for compound 2 (IC 50 = 6.28 μM) and its parent, apigenin (IC 50 = 37.94 μM). Lineweaver-Burk plots showed that the compounds exhibit mixed-type inhibition. In a detailed kinetic study, compound 1 was assigned to mixed type I and exhibited the greatest binding to the free enzyme (K I = 11.7 μM, K IS = 40.9 μM).

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“…Previously reported in vitro data from one series of benzaldehydes (CQ1-CQ19) [17,18], one series of benzoic acids (CS1-CS26) [19][20][21], and one series of cinnamic acids (CS27-CS29) [22] were used in the study (see the structures in Chart shown in Table 1). The IC 50 values of 48 molecules were segregated into groups of 38 and 10 as a training and test set, respectively.…”

Section: Data Set and Structuresmentioning

confidence: 99%

Quantitative structure–activity relationship studies of mushroom tyrosinase inhibitors

Xue

Luo

Ding³

et al. 2008

J Comput Aided Mol Des

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Here, we report our results from quantitative structure-activity relationship studies on tyrosinase inhibitors. Interactions between benzoic acid derivatives and tyrosinase active sites were also studied using a molecular docking method. These studies indicated that one possible mechanism for the interaction between benzoic acid derivatives and the tyrosinase active site is the formation of a hydrogen-bond between the hydroxyl (aOH) and carbonyl oxygen atoms of Tyr98, which stabilized the position of Tyr98 and prevented Tyr98 from participating in the interaction between tyrosinase and ORF378. Tyrosinase, also known as phenoloxidase, is a key enzyme in animals, plants and insects that is responsible for catalyzing the hydroxylation of tyrosine into o-diphenols and the oxidation of o-diphenols into o-quinones. In the present study, the bioactivities of 48 derivatives of benzaldehyde, benzoic acid, and cinnamic acid compounds were used to construct three-dimensional quantitative structure-activity relationship (3D-QSAR) models using comparative molecular field (CoMFA) and comparative molecular similarity indices (CoMSIA) analyses. After superimposition using common substructure-based alignments, robust and predictive 3D-QSAR models were obtained from CoMFA (q2 = 0.855, r2 = 0.978) and CoMSIA (q2 = 0.841, r2 = 0.946), with 6 optimum components. Chemical descriptors, including electronic (Hammett sigma), hydrophobic (pi), and steric (MR) parameters, hydrogen bond acceptor (H-acc), and indicator variable (I), were used to construct a 2D-QSAR model. The results of this QSAR indicated that pi, MR, and H-acc account for 34.9, 31.6, and 26.7% of the calculated biological variance, respectively. The molecular interactions between ligand and target were studied using a flexible docking method (FlexX). The best scored candidates were docked flexibly, and the interaction between the benzoic acid derivatives and the tyrosinase active site was elucidated in detail. We believe that the QSAR models built here provide important information necessary for the design of novel tyrosinase inhibitors.

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Inhibitory effects of salicylic acid family compounds on the diphenolase activity of mushroom tyrosinase

Cited by 85 publications

References 12 publications

Inhibitory Effects of Fatty Acids on the Activity of Mushroom Tyrosinase

Inhibitory Effects of Fatty Acids on the Activity of Mushroom Tyrosinase

Prenylated Flavonoids from Epimedium koreanum Nakai and their Human Neutrophil Elastase Inhibitory Effects

Quantitative structure–activity relationship studies of mushroom tyrosinase inhibitors

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