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dc.contributor.authorAhmed, Sen_US
dc.contributor.authorOwen, CPen_US
dc.contributor.authorJames, Ken_US
dc.contributor.authorPatel, CKen_US
dc.contributor.authorSampson, Len_US
dc.identifier.citationThe Journal of Steroid Biochemistry and Molecular Biology, 2002, 80 pp. 429 - 440en_US
dc.description.abstractIn our search for the mechanism of the enzyme oestrone sulphatase (ES) we have synthesised and evaluated a number of compounds that were predicted to possess some inhibitory activity. Some of these compounds were indeed found to be inhibitors of ES, whilst other compounds were not. From a consideration of the structure–activity relationship (SAR) of the inhibitors and non-inhibitors of this enzyme, we discovered a factor which we now believe is the main inhibitory moiety within the aminosulphonated inhibitors. We therefore report the results of our study into a series of phenyl and alkyl sulphamated compounds as inhibitors of ES. The results of the study show that the substituted phenyl sulphamates are potent inhibitors, whereas the alkyl compounds are, in general, non-inhibitors. Using the results of our SAR study, we postulate the probable mechanism for the irreversible and reversible inhibition of ES, and rationalise the role of the different physicochemical factors in the inhibition of this crucial enzyme.en_US
dc.format.extent429 - 440en_US
dc.titleEvidence for the mechanism of the irreversible inhibition of oestrone sulphatase (ES) by aminosulphonate based compoundsen_US
dc.typeJournal Article
rioxxterms.typeJournal Article/Reviewen_US
dc.relation.isPartOfThe Journal of Steroid Biochemistry and Molecular Biologyen_US
pubs.noteskeywords: Oestrone, Sulphatase, Mechanism, Inhibitors, Aminosulphamateen_US
pubs.notesNot knownen_US
pubs.embargo.termsNot knownen_US
dc.contributor.icrauthorJames, Karenen_US

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