Linked Life Data

15053743

Source:http://linkedlifedata.com/resource/pubmed/id/15053743

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pubmed-article:15053743pubmed:abstractTextThe substrate selectivities of an anti-phosphonate and an anti-phosphate kinetically homogeneous polyclonal catalytic antibody preparation and two hydrolytic enzymes were compared by using hapten-analogous and truncated carbonate and ester substrates each containing a 4-nitrophenolate leaving group. Syntheses of the truncated substrates devoid of recognition features in the non-leaving group parts of the substrates are reported. The relatively high kinetic selectivity of the more active anti-phosphonate antibody preparation is considered to depend on a relatively rigid catalytic site with substantial reaction centre specificity together with other important recognition interactions with the extended non-leaving group part of the substrate. In contrast, the less catalytically active, more flexible anti-phosphate antibody exhibits much lower kinetic selectivity for the substrate reaction centre comparable with that of the hydrolytic enzymes with activity much less dependent on recognition interactions with the non-leaving group part of the substrate. The ways in which haptenic flexibility and IgG architecture might contribute to the differential kinetic selectivities are indicated.lld:pubmed
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pubmed-article:15053743pubmed:articleTitleEvidence for 'lock and key' character in an anti-phosphonate hydrolytic antibody catalytic site augmented by non-reaction centre recognition: variation in substrate selectivity between an anti-phosphonate antibody, an anti-phosphate antibody and two hydrolytic enzymes.lld:pubmed
pubmed-article:15053743pubmed:affiliationLaboratory of Structural and Mechanistic Enzymology, School of Biological Sciences, Queen Mary, University of London, Mile End Road, London E1 4NS, UK.lld:pubmed
pubmed-article:15053743pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:15053743pubmed:publicationTypeComparative Studylld:pubmed
pubmed-article:15053743pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed