Inactivation of jack bean urease by scutellarin: Elucidation of inhibitory efficacy, kinetics and mechanism.
Abstract: In the present study, the inactivation effect of scutellarin (SL) on jack bean urease was investigated to elucidate the inhibitory potency, kinetics and mechanism of inhibition. It was revealed that SL acted as a concentration- and time-dependent inactivator of urease characteristic of slo...
| Publicado en: | Fitoterapia Vol. 91; pp. 60 - 68 |
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| Autores principales: | , , , , , , , , |
| Formato: | Journal Article |
| Publicado: |
Elsevier B.V.
Dec2013
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| Acceso en línea: | Ver este registro en EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=ccm&AN=91743240&site=ehost-live header: @attributes: shortDbName: ccm uiTerm: 91743240 longDbName: CINAHL Complete uiTag: AN controlInfo: bkinfo: dissinfo: jinfo: jid: 0367326X JF4 jtl: Fitoterapia issn: 0367326X maglogo: N pubinfo: dt: Dec2013 vid: 91 pid: 467 pub: Elsevier B.V. place: New York, New York artinfo: ui: 91743240 104151164 10.1016/j.fitote.2013.08.012 91743240 ppf: 60 ppct: 8 formats: tig: atl: Inactivation of jack bean urease by scutellarin: Elucidation of inhibitory efficacy, kinetics and mechanism. aug: au: Wu, Dian-Wei Yu, Xiao-Dan Xie, Jian-Hui Su, Zu-Qing Su, Ji-Yan Tan, Li-Rong Huang, Xiao-Qi Chen, Jian-Nan Su, Zi-Ren affil: College of Chinese Medicine, Guangzhou University of Chinese Medicine, Guangzhou 510006, PR China sug: subj: Plants, Medicinal Plant Extracts Pharmacodynamics Enzyme Inhibitors Pharmacodynamics Alternative Therapies Legumes Drug Effects Dose-Response Relationship, Drug Descriptive Statistics Molecular Biology ab: Abstract: In the present study, the inactivation effect of scutellarin (SL) on jack bean urease was investigated to elucidate the inhibitory potency, kinetics and mechanism of inhibition. It was revealed that SL acted as a concentration- and time-dependent inactivator of urease characteristic of slow-binding inhibition with an IC50 of 1.35±0.15mM. The rapid formation of the initial SL–urease complex with an inhibition constant of Ki =5.37×10−2 mM was followed by a slow isomerization into the final complex with the overall inhibition constant of Ki* =3.49×10−3 mM. High effectiveness of thiol protectors, such as L-cysteine (L-cys), 2-mercaptoethanol (2-ME) and dithiothreitol (DTT) significantly slowed down the rate of inactivation, indicating the strategic role of the active site sulfhydryl group in the blocking process. While the insignificant protection by boric acid and fluoride from the inactivation further confirmed that the active site cysteine should be obligatory for urease inhibition, which was also rationalized by the molecular docking study. The inhibition of SL on urease proved to be reversible since SL-blocked urease could be reactivated by DTT application and multidilution. The results obtained indicated that urease inactivation resulted from the reaction between SL and the sulfhydryl group. pubtype: Academic Journal doctype: Journal Article ougenre: Article language: English refInfo: holdings: @attributes: islocal: N |
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