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dc.contributor.authorQiu, L
dc.contributor.authorChen, QX
dc.contributor.author陈清西
dc.contributor.authorWang, Q
dc.contributor.author王勤
dc.contributor.authorHuang, H
dc.contributor.authorSong, KK
dc.date.accessioned2011-09-30T08:08:17Z
dc.date.available2011-09-30T08:08:17Z
dc.date.issued2005
dc.identifier.citationBioorg Med Chem. 2005 Nov 15;13(22):6206-11. Epub 2005 Jul 21zh_CN
dc.identifier.issn0968-0896
dc.identifier.urihttp://dx.doi.org/doi:10.1016/j.bmc.2005.06.034
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/10784
dc.description.abstract3,5-Dihydroxyphenyl decanoate (DPD) is found to inhibit the diphenolase activity of tyrosinase from mushroom (Agaricus bisporus). The effects of DPD on the diphenolase activity of mushroom tyrosinase have been studied. The results show that the enzyme activity decreases very slowly with an increase in DPD concentrations at lower concentrations of DPD (between 5 and 60 mu M). But at higher concentrations of DPD, DPD can strongly inhibit the diphenolase activity of the enzyme and the inhibition is irreversible. The IC50 value was estimated to be 96.5 mu M. The inhibition mechanism of DPD has been investigated and the results show that DPD can bind to the free enzyme molecule and enzyme-substrate complex and lose the enzyme activity completely. The inhibition kinetics has been studied in detail by using the kinetic method of the substrate reaction described by Tsou. The microscopic rate constants of the enzyme inhibited by DPD at higher concentrations have been determined. (c) 2005 Elsevier Ltd. All rights reserved.zh_CN
dc.language.isoenzh_CN
dc.publisherPERGAMON-ELSEVIER SCIENCE LTDzh_CN
dc.subjectmushroom tyrosinasezh_CN
dc.subject3,5-dihydroxyphenyl decanoatezh_CN
dc.subjectinhibitionzh_CN
dc.subjectmechanismzh_CN
dc.subjectkineticszh_CN
dc.titleIrreversibly inhibitory kinetics of 3,5-dihydroxyphenyl decanoate on mushroom (Agaricus bisporus) tyrosinasezh_CN
dc.typeArticlezh_CN


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