Identification of amino acid substitutions that alter the substrate specificity of TEM-1 (beta)-lactamase
TEM-1 beta-lactamase is the most prevalent plasmid-mediated beta-lactamase in gram-negative bacteria. To identify amino acid substitutions that alter the activity of TEM-1 towards extended-spectrum cephalosporins, regions around the active-site pocket were probed by random-replacement mutagenesis.
Gespeichert in:
Veröffentlicht in: | Journal of bacteriology 1992-08, Vol.174 (16), p.5237 |
---|---|
Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | |
---|---|
container_issue | 16 |
container_start_page | 5237 |
container_title | Journal of bacteriology |
container_volume | 174 |
creator | Palzkill, Timothy Botstein, David |
description | TEM-1 beta-lactamase is the most prevalent plasmid-mediated beta-lactamase in gram-negative bacteria. To identify amino acid substitutions that alter the activity of TEM-1 towards extended-spectrum cephalosporins, regions around the active-site pocket were probed by random-replacement mutagenesis. |
format | Article |
fullrecord | <record><control><sourceid>proquest</sourceid><recordid>TN_cdi_proquest_journals_227077313</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>5851654</sourcerecordid><originalsourceid>FETCH-proquest_journals_2270773133</originalsourceid><addsrcrecordid>eNqNjL0OgjAURhujifjzDo2TDk1aCkFmg9HBjZ1cSokl0CK9DL69EH0Ap-8k58tZkEDw9MziWPIlCTgPBUtFKtdk433DuYiiOAyIuVfaoqmNAjTOUldT6Ix1FJSpqB9LjwbHWXmKT0AKLephQv2VA-BEvVZzwuB7DuTZgwl6LDXCibWgEDrwekdWNbRe73-7JYdrll9urB_ca9Qei8aNg51UEYYJTxIppPzr9AE-S0i5</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>227077313</pqid></control><display><type>article</type><title>Identification of amino acid substitutions that alter the substrate specificity of TEM-1 (beta)-lactamase</title><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central</source><creator>Palzkill, Timothy ; Botstein, David</creator><creatorcontrib>Palzkill, Timothy ; Botstein, David</creatorcontrib><description>TEM-1 beta-lactamase is the most prevalent plasmid-mediated beta-lactamase in gram-negative bacteria. To identify amino acid substitutions that alter the activity of TEM-1 towards extended-spectrum cephalosporins, regions around the active-site pocket were probed by random-replacement mutagenesis.</description><identifier>ISSN: 0021-9193</identifier><identifier>EISSN: 1098-5530</identifier><identifier>CODEN: JOBAAY</identifier><language>eng</language><publisher>Washington: American Society for Microbiology</publisher><subject>Antibiotics ; Bacteriology</subject><ispartof>Journal of bacteriology, 1992-08, Vol.174 (16), p.5237</ispartof><rights>Copyright American Society for Microbiology Aug 1992</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780</link.rule.ids></links><search><creatorcontrib>Palzkill, Timothy</creatorcontrib><creatorcontrib>Botstein, David</creatorcontrib><title>Identification of amino acid substitutions that alter the substrate specificity of TEM-1 (beta)-lactamase</title><title>Journal of bacteriology</title><description>TEM-1 beta-lactamase is the most prevalent plasmid-mediated beta-lactamase in gram-negative bacteria. To identify amino acid substitutions that alter the activity of TEM-1 towards extended-spectrum cephalosporins, regions around the active-site pocket were probed by random-replacement mutagenesis.</description><subject>Antibiotics</subject><subject>Bacteriology</subject><issn>0021-9193</issn><issn>1098-5530</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><recordid>eNqNjL0OgjAURhujifjzDo2TDk1aCkFmg9HBjZ1cSokl0CK9DL69EH0Ap-8k58tZkEDw9MziWPIlCTgPBUtFKtdk433DuYiiOAyIuVfaoqmNAjTOUldT6Ix1FJSpqB9LjwbHWXmKT0AKLephQv2VA-BEvVZzwuB7DuTZgwl6LDXCibWgEDrwekdWNbRe73-7JYdrll9urB_ca9Qei8aNg51UEYYJTxIppPzr9AE-S0i5</recordid><startdate>19920801</startdate><enddate>19920801</enddate><creator>Palzkill, Timothy</creator><creator>Botstein, David</creator><general>American Society for Microbiology</general><scope>7QL</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>19920801</creationdate><title>Identification of amino acid substitutions that alter the substrate specificity of TEM-1 (beta)-lactamase</title><author>Palzkill, Timothy ; Botstein, David</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-proquest_journals_2270773133</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Antibiotics</topic><topic>Bacteriology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Palzkill, Timothy</creatorcontrib><creatorcontrib>Botstein, David</creatorcontrib><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Journal of bacteriology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Palzkill, Timothy</au><au>Botstein, David</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of amino acid substitutions that alter the substrate specificity of TEM-1 (beta)-lactamase</atitle><jtitle>Journal of bacteriology</jtitle><date>1992-08-01</date><risdate>1992</risdate><volume>174</volume><issue>16</issue><spage>5237</spage><pages>5237-</pages><issn>0021-9193</issn><eissn>1098-5530</eissn><coden>JOBAAY</coden><abstract>TEM-1 beta-lactamase is the most prevalent plasmid-mediated beta-lactamase in gram-negative bacteria. To identify amino acid substitutions that alter the activity of TEM-1 towards extended-spectrum cephalosporins, regions around the active-site pocket were probed by random-replacement mutagenesis.</abstract><cop>Washington</cop><pub>American Society for Microbiology</pub></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0021-9193 |
ispartof | Journal of bacteriology, 1992-08, Vol.174 (16), p.5237 |
issn | 0021-9193 1098-5530 |
language | eng |
recordid | cdi_proquest_journals_227077313 |
source | Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
subjects | Antibiotics Bacteriology |
title | Identification of amino acid substitutions that alter the substrate specificity of TEM-1 (beta)-lactamase |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-03T15%3A02%3A19IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Identification%20of%20amino%20acid%20substitutions%20that%20alter%20the%20substrate%20specificity%20of%20TEM-1%20(beta)-lactamase&rft.jtitle=Journal%20of%20bacteriology&rft.au=Palzkill,%20Timothy&rft.date=1992-08-01&rft.volume=174&rft.issue=16&rft.spage=5237&rft.pages=5237-&rft.issn=0021-9193&rft.eissn=1098-5530&rft.coden=JOBAAY&rft_id=info:doi/&rft_dat=%3Cproquest%3E5851654%3C/proquest%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=227077313&rft_id=info:pmid/&rfr_iscdi=true |