Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1990-1-19
pubmed:abstractText
An enzymatic assay for delta 8,14-sterol delta 14-reductase, an enzyme involved in sterol biosynthesis, has been developed for the first time in higher plants. The properties of the microsomal enzyme have been established with respect to cofactor requirements, kinetics and substrate specificity. This enzymatic double-bound reduction is thought to proceed through an electrophilic addition mechanism, involving a C14 putative carbonium ion high-energy intermediate. Using this in vitro assay, ammonium and iminium analogues of this cationic intermediate were shown to be potent inhibitors of the reduction reaction. Thus, compounds of the N-alkyl-8-aza-4 alpha,10-dimethyl-trans-decal-3 beta-ol series strongly inhibited sterol reductase (I50 = 0.07 - 4 microM) (I50/Km = 10(-4) - 10(-3), as did the antimycotic agent 15-azasterol (I50 = 0.03 microM); all of these compounds act as reaction-intermediate analogues of the proposed C14 carbonium ion intermediate. Moreover, the in vitro inhibition of the plant sterol reductase by a series of ammonium-ion-containing fungicides was demonstrated. The relative specificity of these different series of inhibitors toward cycloeucalenol-obtusifoliol isomerase, delta 8----delta 7-sterol isomerase and delta 8,14-sterol delta 14-reductase, was directly studied.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
185
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
605-14
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Microsomal delta 8,14-sterol delta 14-reductase in higher plants. Characterization and inhibition by analogues of a presumptive carbocationic intermediate of the reduction reaction.
pubmed:affiliation
Institut de Botanique, Unité Associée 1182 du Centre National de la Recherche Scientifique, Strasbourg, France.
pubmed:publicationType
Journal Article, Comparative Study