Kinetics and mechanism study of competitive inhibition of jack-bean urease by baicalin.
Baicalin (BA) is the principal component of Radix Scutellariae responsible for its pharmacological activity. In this study, kinetics and mechanism of inhibition by BA against jack-bean urease were investigated for its therapeutic potential. It was revealed that the IC₅₀ of BA against jack-bean ureas...
| Publicado en: | Scientific World Journal pp. 879501 - 879502 |
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| Autores principales: | , , , , , , , , , , |
| Formato: | research Journal Article |
| Publicado: |
Wiley-Blackwell
2013
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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=104111869&site=ehost-live header: @attributes: shortDbName: ccm uiTerm: 104111869 longDbName: CINAHL Complete uiTag: AN controlInfo: bkinfo: dissinfo: jinfo: jid: 1537744X 1BX5 jtl: Scientific World Journal issn: 1537744X maglogo: N pubinfo: dt: 2013 pid: 480 pub: Wiley-Blackwell place: Malden, Massachusetts artinfo: ui: 104111869 NLM24198731 2012363003 10.1155/2013/879501 NLM24198731 PMC3807542 104111869 ppf: 879501 ppct: 1 formats: tig: atl: Kinetics and mechanism study of competitive inhibition of jack-bean urease by baicalin. aug: au: Tan, Lirong Su, Jiyan Wu, Dianwei Yu, Xiaodan Su, Zuqing He, Jingjin Wu, Xiaoli Kong, Songzhi Lai, Xiaoping Lin, Ji Su, Ziren affil: School of Chinese Materia Medica, Guangzhou University of Chinese Medicine, Guangzhou, Guangdong 510006, China. sug: subj: Legumes Flavonoids Metabolism Urease Metabolism Kinetics ab: Baicalin (BA) is the principal component of Radix Scutellariae responsible for its pharmacological activity. In this study, kinetics and mechanism of inhibition by BA against jack-bean urease were investigated for its therapeutic potential. It was revealed that the IC₅₀ of BA against jack-bean urease was 2.74 ± 0.51 mM, which was proved to be a competitive and concentration-dependent inhibition with slow-binding progress curves. The rapid formation of initial BA-urease complex with an inhibition constant of K(i) = 3.89 × 10⁻³ mM was followed by a slow isomerization into the final complex with an overall inhibition constant of K(i)* = 1.47 × 10⁻⁴ mM. High effectiveness of thiol protectors against BA inhibition indicated that the strategic role of the active-site sulfhydryl group of the urease was involved in the blocking process. Moreover, the inhibition of BA was proved to be reversible due to the fact that urease could be reactivated by dithiothreitol but not reactant dilution. Molecular docking assay suggested that BA made contacts with the important activating sulfhydryl group Cys-592 residues and restricted the mobility of the active-site flap. Taken together, it could be deduced that BA was a competitive inhibitor targeting thiol groups of urease in a slow-binding manner both reversibly and concentration-dependently, serving as a promising urease inhibitor for treatments on urease-related diseases. pubtype: Academic Journal doctype: research Journal Article ougenre: Article language: English refInfo: holdings: @attributes: islocal: N |
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