pubmed-article:11880619 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11880619 | lifeskim:mentions | umls-concept:C0162594 | lld:lifeskim |
pubmed-article:11880619 | lifeskim:mentions | umls-concept:C0178555 | lld:lifeskim |
pubmed-article:11880619 | lifeskim:mentions | umls-concept:C0449445 | lld:lifeskim |
pubmed-article:11880619 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:11880619 | pubmed:dateCreated | 2002-3-7 | lld:pubmed |
pubmed-article:11880619 | pubmed:abstractText | A strategy for the preparation of semisynthetic copper(II)-based catalytic metalloproteins is described in which a metal-binding bis-imidazole cofactor is incorporated into the combining site of the aldolase antibody 38C2. Antibody 38C2 features a large hydrophobic-combining site pocket with a highly nucleophilic lysine residue, Lys(H93), that can be covalently modified. A comparison of several lactone and anhydride reagents shows that the latter are the most effective and general derivatizing agents for the 38C2 Lys residue. A bis-imidazole anhydride (5) was efficiently prepared from N-methyl imidazole. The 38C2-5-Cu conjugate was prepared by either (i) initial derivatization of 38C2 with 5 followed by metallation with CuCl2, or (ii) precoordination of 5 with CuCl2 followed by conjugation with 38C2. The resulting 38C2-5-Cu conjugate was an active catalyst for the hydrolysis of the coordinating picolinate ester 11, following Michaelis-Menten kinetics [kcat(11) = 2.3 min(-1) and Km(11) 2.2 mM] with a rate enhancement [kcat(11)k(uncat)(11)] of 2.1 x 10(5). Comparison of the second-order rate constants of the modified 38C2 and the Cu(II)-bis-imidazolyl complex k(6-CuCl2) gives a rate enhancement of 3.5 x 10(4) in favor of the antibody complex with an effective molarity of 76.7 M, revealing a significant catalytic benefit to the binding of the bis-imidazolyl ligand into 38C2. | lld:pubmed |
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pubmed-article:11880619 | pubmed:language | eng | lld:pubmed |
pubmed-article:11880619 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11880619 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11880619 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11880619 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:11880619 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11880619 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:11880619 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11880619 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11880619 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11880619 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11880619 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11880619 | pubmed:month | Mar | lld:pubmed |
pubmed-article:11880619 | pubmed:issn | 0027-8424 | lld:pubmed |
pubmed-article:11880619 | pubmed:author | pubmed-author:JandaKim DKD | lld:pubmed |
pubmed-article:11880619 | pubmed:author | pubmed-author:NicholasKenne... | lld:pubmed |
pubmed-article:11880619 | pubmed:author | pubmed-author:WentworthPaul... | lld:pubmed |
pubmed-article:11880619 | pubmed:author | pubmed-author:HarwigCurtis... | lld:pubmed |
pubmed-article:11880619 | pubmed:author | pubmed-author:WentworthAnit... | lld:pubmed |
pubmed-article:11880619 | pubmed:author | pubmed-author:ShaftonAsherA | lld:pubmed |
pubmed-article:11880619 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11880619 | pubmed:day | 5 | lld:pubmed |
pubmed-article:11880619 | pubmed:volume | 99 | lld:pubmed |
pubmed-article:11880619 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11880619 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11880619 | pubmed:pagination | 2648-53 | lld:pubmed |
pubmed-article:11880619 | pubmed:dateRevised | 2010-9-14 | lld:pubmed |
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pubmed-article:11880619 | pubmed:meshHeading | pubmed-meshheading:11880619... | lld:pubmed |
pubmed-article:11880619 | pubmed:year | 2002 | lld:pubmed |
pubmed-article:11880619 | pubmed:articleTitle | A cofactor approach to copper-dependent catalytic antibodies. | lld:pubmed |
pubmed-article:11880619 | pubmed:affiliation | Department of Chemistry and Biochemistry, University of Oklahoma, Norman, OK 73019, USA. kmnicholas@chemdept.chem.ou.edu | lld:pubmed |
pubmed-article:11880619 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11880619 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:11880619 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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