Effect of Cd2+ on tyrosinase: Integration of inhibition kinetics with computational simulation

Yue, Li-Mei; Lee, Jinhyuk; Lu, Ziwen; Yang, Jun‐Mo; Ye, Zhuo-Ming; Park, Yong‐Doo

doi:10.1016/j.ijbiomac.2016.09.001

Cited by 9 publications

(3 citation statements)

References 26 publications

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“…Except the inhibitors listed above, other compounds have also been registered for their tyrosinase inhibitory activity by different researchers such as: two Keggin-type polyoxometalates containing glycine as potent inorganic reversible inhibitors 429 , cadmium ions with an IC 50 of 2.92 ± 0.16 mM 48 and rifampicin with an IC 50 = 90 ± 0.6 µM 9 as reversible and noncompetitive inhibitors, ammonium tetrathiotungstate 430 , amoxicillin (IC 50 = 9.0 ± 1.8 mM) 431 , mallotophilippen A and B 432 α-naphthol and β-naphthol 433 , red koji extracts (IC 50 of 5.57 mg/mL) 434 and alpha-hydrazinophloretic acid 435 as competitive inhibitors and rottlerin as a mixed inhibitor 432 . Furthermore, n -alkyl sulfates 436 , sericin extracted from tasar silk fiber waste 437 , 2-hydroxy-3-methylcyclopent-2-enone (IC 50 = 721.91 µg mL −1 ) isolated from ribose-histidine Maillard reaction products 438 , three natural compounds from safflower 439 and mimosine 386 and ethylenediamine 440 are other kinds of tyrosinase inhibitors.…”

Section: Other Tyrosinase Inhibitorsmentioning

confidence: 99%

A comprehensive review on tyrosinase inhibitors

Zolghadri

Bahrami

Khan³

et al. 2019

Journal of Enzyme Inhibition and Medicinal Chemistry

735

471

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Tyrosinase is a multi-copper enzyme which is widely distributed in different organisms and plays an important role in the melanogenesis and enzymatic browning. Therefore, its inhibitors can be attractive in cosmetics and medicinal industries as depigmentation agents and also in food and agriculture industries as antibrowning compounds. For this purpose, many natural, semi-synthetic and synthetic inhibitors have been developed by different screening methods to date. This review has focused on the tyrosinase inhibitors discovered from all sources and biochemically characterised in the last four decades.

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Section: Other Tyrosinase Inhibitorsmentioning

confidence: 99%

A comprehensive review on tyrosinase inhibitors

Zolghadri

Bahrami

Khan³

et al. 2019

Journal of Enzyme Inhibition and Medicinal Chemistry

735

471

View full text Add to dashboard Cite

show abstract

“…However, research about interaction mechanism between CA and PPO has not yet been conducted. Rosario Goyeneche, Yue-Xiu Si, Mareike E. Dirks-Hofmeister, and many other professors have reported that PPO is associated with the active ingredient in plant tissues [15][16][17]. At present, some researchers mostly pay attention to the active molecule interactions with enzymes on the binding reaction between animal's protease and drug molecules [18][19][20], while others are focused on the reactive molecules inhibited enzyme activity [21,22].…”

Section: Introductionmentioning

confidence: 99%

Three-Dimensional Fingerprint Spectroscopy Study on the Biopolymer System of Polyphenol Oxidase Binding with Cumalic Acid

Wu¹,

Ling²,

Yao³

et al. 2022

Bull. of the Kar. Univ. "Chem". Ser.

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The protection of Cumalic acid (CA), antioxidant, in the biochemical process in nature has aroused great interest.Polyphenol oxidase (PPO), an enzyme, plays a vital function in aging and browning of plants, such as vegetables, fruits and mushrooms. The interaction of CA and PPO reveals the important information in metabolism and aging. Thus, the molecular mechanism of CA binding with polyphenol oxidase (PPO) was explored by combining spectroscopic methods with molecular modeling. A three-dimensional fingerprint of the CA-PPO complex was built for the first time to characterize the interaction biopolymer between CA and PPO. Application of the spectroscopic methods indicated that CA effectively quenched the intrinsic fluorescence of PPO. The enthalpy change (ΔH°) and entropy change (ΔS°) suggested that the CA-PPO complex was predominantly stabilized by hydrophobic interactions CA and PPO. Building the λ-UV-F fingerprint of CA-PPO made it possible to demonstrate the three-dimensional interactions between CA and PPO. Subsequently, molecular modeling demonstrated that CA was primarily bound to PPO by hydrophobic interactions and hydrogen bonds located at amino acid residues Ala202, His38, His54 and Ser206. The computational simulations were consistent with the spectral experiments demonstrating confidence in the three-dimensional model determined of the CA-PPO interaction.

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“…The activity of enzymes varies with the presence of organic compounds, heavy metals and substrate analogues. Heavy metals such as cadmium (Cd), chromium (Cr), copper (Cu), ferrous (Fe), mercury (Hg), nickel (Ni), and silver (Ag) affect activity of various enzymes as reported by numerous studies (Attar et al 2014;Do and Lin 2016;Fopase et al 2019;Moyo et al 2014;Yue et al 2017). Cr, a well-known abundant element on earth, its different oxidative forms Cr 3+ and Cr 6+ have shown influence on the activity of various enzymes.…”

Section: Introductionmentioning

confidence: 99%

Inhibition assays of free and immobilized urease for detecting hexavalent chromium in water samples

et al. 2019

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The present work describes the inhibition studies of free as well as immobilized urease by different heavy metals. Porous silicon (PS) films prepared by electrochemical etching were used for urease immobilization by physical adsorption. The enzyme was subjected to varying concentrations of Cr 6+ , Cr 3+ , Cu 2+ , Fe 2+ , Cd 2+ and Ni 2+ and analyzed for the variation in the activity. To study the effect of other heavy metals on the interaction of urease and Cr 6+ , free as well as immobilized urease was subjected to the combination of each metal ion with Cr 6+. Results proved the sensitivity of free as well as immobilized urease towards heavy metals by observed reduction in activity. Immobilized urease showed less degree of inhibition compared to free urease when tested for inhibition by individual metal ions and in combination with Cr 6+. IC 50 values were found higher for inhibition by the combination of metal ions with Cr 6+. Interaction of heavy metal ions with functional groups in active site of urease and limitations of mass transfer are the two factors responsible for the variation in activity of urease. Relation between the variation of urease activity and amount of heavy metals can be applied in biosensor development for determining the concentration of Cr 6+ present in the water samples.

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Effect of Cd2+ on tyrosinase: Integration of inhibition kinetics with computational simulation

Cited by 9 publications

References 26 publications

A comprehensive review on tyrosinase inhibitors

A comprehensive review on tyrosinase inhibitors

Three-Dimensional Fingerprint Spectroscopy Study on the Biopolymer System of Polyphenol Oxidase Binding with Cumalic Acid

Inhibition assays of free and immobilized urease for detecting hexavalent chromium in water samples

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