Linked Life Data

647082

Source:http://linkedlifedata.com/resource/pubmed/id/647082

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SubjectPredicateObjectContext
pubmed-article:647082rdf:typepubmed:Citationlld:pubmed
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pubmed-article:647082pubmed:issue2lld:pubmed
pubmed-article:647082pubmed:dateCreated1978-7-15lld:pubmed
pubmed-article:647082pubmed:abstractTextThe kinetics of acetylcholinesterase-catalyzed hydrolysis of the two cationic substrates (I and II in Russian text) was analyzed by means of the integrated Michaelis equation (3). The constants kII, kcat Km and the enzyme-product complex dissociation constant Ki were determined. (Table 1). It was shown that acetylcholine (II) binds to to the enzyme active center more effectively than the alcohol product of its hydrolysis. In case of the pipecholine derivative (I) reversed situation occurs. The different dependence of the ester substrate and appropriate alcohol binding effectiveness upon the reagent structure indicates the dissimilar location of the molecules in the active center of acetylcholinesterase. Some structural implications of the enzyme active center were discussed.lld:pubmed
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pubmed-article:647082pubmed:volume43lld:pubmed
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pubmed-article:647082pubmed:pagination334-9lld:pubmed
pubmed-article:647082pubmed:dateRevised2007-7-23lld:pubmed
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pubmed-article:647082pubmed:year1978lld:pubmed
pubmed-article:647082pubmed:articleTitle[Inhibition of acetylcholinesterase hydrolysis of cationic substrates by the reaction product].lld:pubmed
pubmed-article:647082pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:647082pubmed:publicationTypeEnglish Abstractlld:pubmed