About: Inhibition of alcohol dehydrogenase by bismuth

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An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Inhibition of alcohol dehydrogenase by bismuth
Creator	Zhang, Li Sun, Hongzhe Du, Weihong Jin, Lan Szeto, Ka-Yee
Source	Elsevier; Medline; PMC
abstract	Abstract Bismuth compounds have been widely used for the treatment of ulcers and Helicobacter pylori infection, and enzyme inhibition was thought to be crucial for bismuth anti-microbial activity. We have investigated the interaction of colloidal bismuth subcitrate (CBS) with alcohol dehydrogenase and our results demonstrate that bismuth can effectively inhibit the enzyme. Kinetic analysis revealed that CBS acted as a non-competitive inhibitor of yeast alcohol dehydrogenase. Both UV–vis and fluorescence data show that interaction of CBS with the enzyme exhibits biphasic processes. Bismuth can replace only half of Zn(II) from the enzyme (i.e., about one Zn(II) per monomer). Surprisingly, binding of CBS also induces the enzyme dissociation from its native form, tetramer into dimers. The inhibition of Bi(III) on the enzyme is probably due to its direct interference with the zinc sites. This study is likely to provide an insight into the mechanism of action of bismuth drugs.
has issue date	2004-08-31(xsd:dateTime)
bibo:doi	10.1016/j.jinorgbio.2004.03.016
bibo:pmid	15271509
has license	els-covid
sha1sum (hex)	fca4772bf9a088376d86d549e861c7fcb78c8b3c
schema:url	https://doi.org/10.1016/j.jinorgbio.2004.03.016
resource representing a document's title	Inhibition of alcohol dehydrogenase by bismuth
has PubMed Central identifier	PMC7126473
has PubMed identifier	15271509
schema:publication	Journal of Inorganic Biochemistry
resource representing a document's body	covid:fca4772bf9a088376d86d549e861c7fcb78c8b3c#body_text
is schema:about of	named entity 'ALCOHOL DEHYDROGENASE' named entity 'effectively' named entity 'data' named entity 'CBS' named entity 'CBS' named entity 'STUDY' named entity 'TREATMENT' named entity 'USED' named entity 'BISMUTH COMPOUNDS' named entity 'CBS' named entity 'ABOUT' named entity 'BISMUTH' named entity 'BIPHASIC' named entity 'ENZYME' named entity 'INVESTIGATED' named entity 'MICROBIAL ACTIVITY' named entity 'DRUGS' named entity 'THOUGHT' named entity 'INSIGHT' named entity 'RESULTS' named entity 'ANALYSIS' named entity 'INHIBITION' named entity 'UV-VIS' named entity 'YEAST ALCOHOL DEHYDROGENASE' named entity 'INTERFERENCE' named entity 'DATA' named entity 'MONOMER' named entity 'BINDING' named entity 'OUR' named entity '28I' named entity 'ENZYME INHIBITION' named entity 'REVEALED' named entity 'INHIBITION' named entity 'BISMUTH' named entity 'SITES' named entity 'TO PROVIDE' named entity 'COLLOIDAL BISMUTH SUBCITRATE' named entity 'LIKELY' named entity 'ZINC' named entity 'ULCERS' named entity 'DIRECT' named entity 'HALF' named entity 'ALCOHOL DEHYDROGENASE' named entity 'PROCESSES' named entity 'HAVE' named entity 'MECHANISM OF ACTION' named entity 'DIMERS' named entity 'PROBABLY' named entity 'DISSOCIATION' named entity 'FLUORESCENCE' named entity 'HELICOBACTER PYLORI INFECTION' named entity 'EXHIBITS' named entity 'DUE TO' named entity 'NATIVE FORM' named entity 'REPLACE' named entity 'INTERACTION' named entity 'ITS' named entity 'KINETIC' covid:arg/fca4772bf9a088376d86d549e861c7fcb78c8b3c named entity 'enzyme' named entity 'tetramer' named entity 'alcohol dehydrogenase' named entity 'sites' named entity 'ulcers' named entity 'CBS' named entity 'dissociation' named entity 'revealed' named entity 'induces' named entity 'CBS' named entity 'dimers' named entity 'bismuth' named entity 'bismuth' named entity 'tetramer' named entity 'colloidal' named entity 'enzyme inhibition' named entity 'HCl' named entity 'solubilized'

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