Dual effects of aliphatic carboxylic acids on cresolase and catecholase reactions of mushroom tyrosinase

Gheibi, Nematollah; Saboury, Ali Akbar; Haghbeen, K.; Rajaei, Farzad; Pahlevan, Ali Asghar

doi:10.1080/14756360802632658

Cited by 24 publications

(16 citation statements)

References 38 publications

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“…But the way the residues of these substrates lay in the pocket of the active site would be predictably different. Thus, the overall conformational changes of mushroom tyrosinase results from the sum of the interactions of both head and body of the substrate with the active site and the pocket of the active site [21]. In the process of catalysis, tyrosinase has three existing forms, E met , E oxy , and E deoxy .…”

Section: Discussionmentioning

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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Section: Discussionmentioning

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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“…Gulcin et al reported that sodium diethyl dithiocarbamate was the most effective inhibitor (Ki: 1.79 nM) on nettle PPO 28 . It was reported that the enzyme inhibited with diarylureas 15 and phenylthiourea 29 , propanoic acid 30 , alkyldithiocarbonates 31 and coumarin schiff-bases 32 , n-alkyl dithiocarbamate compounds 33 , sodium diethyl dithiocarbamate 28 . In order to understand and explain the experimental results obtained, molecular calculations were performed using Gaussian software 34a,b , for the synthesized compounds and some of the molecular structures are shown in Figure 2.…”

Section: Resultsmentioning

confidence: 99%

Synthesis and theoretical calculations of carbazole substituted chalcone urea derivatives and studies their polyphenol oxidase enzyme activity

Nixha

Arslan

Atalay

et al. 2012

Journal of Enzyme Inhibition and Medicinal Chemistry

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“…Considering some key structural requirements for competitive inhibition, we extended our studies on some molecules that could not be considered MT substrates. Consequently, we could demonstrate heterotropic activation of both activities of MT [17,18].…”

Section: Introductionmentioning

confidence: 92%

“…For instance, ethyl and propyl xanthate activated cresolase activity at low concentrations (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12) µM) but worked as inhibitors at higher concentrations [17]. In a different study, it was shown that some selected α-keto acids activated catecholase activity but worked as inhibitors in cresolase reaction [18]. Structural features and concentration of the effector were two determinant factors affecting the modulator impact on MT activities.…”

Section: Introductionmentioning

confidence: 97%