| pubmed-article:11148033 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11148033 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:11148033 | lifeskim:mentions | umls-concept:C0233820 | lld:lifeskim |
| pubmed-article:11148033 | lifeskim:mentions | umls-concept:C1853126 | lld:lifeskim |
| pubmed-article:11148033 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:11148033 | lifeskim:mentions | umls-concept:C0006978 | lld:lifeskim |
| pubmed-article:11148033 | lifeskim:mentions | umls-concept:C0915340 | lld:lifeskim |
| pubmed-article:11148033 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:11148033 | pubmed:dateCreated | 2001-1-23 | lld:pubmed |
| pubmed-article:11148033 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11148033 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11148033 | pubmed:abstractText | PSE-4 is a class A beta-lactamase produced by strains of Pseudomonas aeruginosa and is highly active for the penicillin derivative carbenicillin. The crystal structure of the wild-type PSE-4 carbenicillinase has been determined to 1.95 A resolution by molecular replacement and represents the first structure of a carbenicillinase published to date. A superposition of the PSE-4 structure with that of TEM-1 shows a rms deviation of 1.3 A for 263 Calpha atoms. Most carbenicillinases are unique among class A beta-lactamases in that residue 234 is an arginine (ABL standard numbering scheme), while in all other class A enzymes this residue is a lysine. Kinetic characterization of a R234K PSE-4 mutant reveals a 50-fold reduction in k(cat)/K(m) and confirms the importance of Arg 234 for carbenicillinase activity. A comparison of the structure of the R234K mutant refined to 1.75 A resolution with the wild-type structure shows that Arg 234 stabilizes an alternate conformation of the Ser 130 side chain, not seen in other class A beta-lactamase structures. Our molecular modeling studies suggest that the position of a bound carbenicillin would be shifted relative to that of a bound benzylpenicillin in order to avoid a steric clash between the carbenicillin alpha-carboxylate group and the conserved side chain of Asn 170. The alternate conformation of the catalytic Ser 130 in wild-type PSE-4 may be involved in accommodating this shift in the bound substrate position. | lld:pubmed |
| pubmed-article:11148033 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11148033 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11148033 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11148033 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11148033 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11148033 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:11148033 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:11148033 | pubmed:author | pubmed-author:LiuLL | lld:pubmed |
| pubmed-article:11148033 | pubmed:author | pubmed-author:LevesqueR CRC | lld:pubmed |
| pubmed-article:11148033 | pubmed:author | pubmed-author:StrynadkaN... | lld:pubmed |
| pubmed-article:11148033 | pubmed:author | pubmed-author:De CastroLL | lld:pubmed |
| pubmed-article:11148033 | pubmed:author | pubmed-author:SanschagrinFF | lld:pubmed |
| pubmed-article:11148033 | pubmed:author | pubmed-author:PassmoreLL | lld:pubmed |
| pubmed-article:11148033 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11148033 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:11148033 | pubmed:volume | 40 | lld:pubmed |
| pubmed-article:11148033 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11148033 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11148033 | pubmed:pagination | 395-402 | lld:pubmed |
| pubmed-article:11148033 | pubmed:dateRevised | 2008-8-22 | lld:pubmed |
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| pubmed-article:11148033 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11148033 | pubmed:articleTitle | Insights into the molecular basis for the carbenicillinase activity of PSE-4 beta-lactamase from crystallographic and kinetic studies. | lld:pubmed |
| pubmed-article:11148033 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada. | lld:pubmed |
| pubmed-article:11148033 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11148033 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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