{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,16]],"date-time":"2025-10-16T20:00:17Z","timestamp":1760644817732},"reference-count":30,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2004,7,1]]},"abstract":"<jats:p>The 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.<\/jats:p>","DOI":"10.1042\/bj20031966","type":"journal-article","created":{"date-parts":[[2004,6,22]],"date-time":"2004-06-22T13:45:11Z","timestamp":1087911911000},"page":"125-130","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":10,"title":["Evidence for \u2018lock and key\u2019 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"],"prefix":"10.1042","volume":"381","author":[{"given":"Sanjiv","family":"SONKARIA","sequence":"first","affiliation":[{"name":"Laboratory of Structural and Mechanistic Enzymology, School of Biological Sciences, Queen Mary, University of London, Mile End Road, London E1 4NS, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Guillaume","family":"BOUCHER","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, School of Pharmacy and Biomolecular Sciences, Cockcroft Building, Lewes Road, Moulsecoomb, Brighton BN2 4GJ, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jos\u00e9","family":"FL\u00d3REZ-\u00c1LVAREZ","sequence":"additional","affiliation":[{"name":"Laboratory of Structural and Mechanistic Enzymology, School of Biological Sciences, Queen Mary, University of London, Mile End Road, London E1 4NS, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bilal","family":"SAID","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, School of Pharmacy and Biomolecular Sciences, Cockcroft Building, Lewes Road, Moulsecoomb, Brighton BN2 4GJ, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Syeed","family":"HUSSAIN","sequence":"additional","affiliation":[{"name":"Laboratory of Structural and Mechanistic Enzymology, School of Biological Sciences, Queen Mary, University of London, Mile End Road, London E1 4NS, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Elizabeth\u00a0L.","family":"OSTLER","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, School of Pharmacy and Biomolecular Sciences, Cockcroft Building, Lewes Road, Moulsecoomb, Brighton BN2 4GJ, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sheraz","family":"GUL","sequence":"additional","affiliation":[{"name":"Laboratory of Structural and Mechanistic Enzymology, School of Biological Sciences, Queen Mary, University of London, Mile End Road, London E1 4NS, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Emrys\u00a0W.","family":"THOMAS","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, University of Salford, The Crescent, Salford M5 4JW, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marina","family":"RESMINI","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Queen Mary, University of London, Mile End Road, London E1 4NS, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gerard","family":"GALLACHER","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, School of Pharmacy and Biomolecular Sciences, Cockcroft Building, Lewes Road, Moulsecoomb, Brighton BN2 4GJ, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Keith","family":"BROCKLEHURST","sequence":"additional","affiliation":[{"name":"Laboratory of Structural and Mechanistic Enzymology, School of Biological Sciences, Queen Mary, University of London, Mile End Road, London E1 4NS, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2004,6,22]]},"reference":[{"key":"2021112213025221700_B1","first-page":"351","article-title":"Cysteine proteinases","volume-title":"Comprehensive Biological Catalysis","author":"Brocklehurst","year":"1998"},{"key":"2021112213025221700_B2","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1042\/bj3570343","article-title":"Variation in aspects of cysteine proteinase mechanism deduced by spectroscopic observation of dithioester intermediates, kinetic analysis and molecular dynamic simulations","volume":"357","author":"Reid","year":"2001","journal-title":"Biochem. 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