| pubmed-article:3055170 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3055170 | lifeskim:mentions | umls-concept:C0004611 | lld:lifeskim |
| pubmed-article:3055170 | lifeskim:mentions | umls-concept:C0018150 | lld:lifeskim |
| pubmed-article:3055170 | lifeskim:mentions | umls-concept:C0070235 | lld:lifeskim |
| pubmed-article:3055170 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:3055170 | pubmed:dateCreated | 1988-12-13 | lld:pubmed |
| pubmed-article:3055170 | pubmed:abstractText | beta-Lactam antibiotics exert their antibacterial effects by inactivating the high-molecular-weight penicillin-binding proteins (PBPs) that are responsible for the final stages of peptidoglycan biosynthesis. The availability of the amino acid sequences of several low-molecular-weight PBPs, high-molecular-weight PBPs, and active-site serine beta-lactamases has provided evidence that these groups of enzymes have a common, but distant, evolutionary origin. This view is strongly supported by the recent finding of a similarity in the three-dimensional structures of a low-molecular-weight PBP and class A beta-lactamases. The high-molecular-weight PBPs of Escherichia coli are believed to possess an amino-terminal peptidoglycan transglycosylase domain and a carboxy-terminal penicillin-sensitive transpeptidase domain. These enzymes are inserted in the cytoplasmic membrane only at their amino termini, and water-soluble forms have been obtained that should be suitable for crystallization and X-ray analysis. Resistance to beta-lactam antibiotics mediated by alterations of PBPs has been reported in some gram-negative bacteria. In isolates of Neisseria gonorrhoeae with chromosomally mediated resistance, penicillin-resistant PBPs have arisen from the introduction of multiple amino acid substitutions within the transpeptidase domain of the enzymes. | lld:pubmed |
| pubmed-article:3055170 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3055170 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:3055170 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3055170 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3055170 | pubmed:issn | 0162-0886 | lld:pubmed |
| pubmed-article:3055170 | pubmed:author | pubmed-author:SprattB GBG | lld:pubmed |
| pubmed-article:3055170 | pubmed:author | pubmed-author:CromieK DKD | lld:pubmed |
| pubmed-article:3055170 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3055170 | pubmed:volume | 10 | lld:pubmed |
| pubmed-article:3055170 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3055170 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3055170 | pubmed:pagination | 699-711 | lld:pubmed |
| pubmed-article:3055170 | pubmed:dateRevised | 2009-9-29 | lld:pubmed |
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| pubmed-article:3055170 | pubmed:articleTitle | Penicillin-binding proteins of gram-negative bacteria. | lld:pubmed |
| pubmed-article:3055170 | pubmed:affiliation | Microbial Genetics Group, School of Biological Sciences, University of Sussex, Brighton, United Kingdom. | lld:pubmed |
| pubmed-article:3055170 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3055170 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:3055170 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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