Metallo-β-Lactamases: Influence of the Active Site Structure on the Mechanisms of Antibiotic Resistance and Inhibition
The review focuses on bacterial metallo-β-lactamases (MβLs) responsible for the inactivation of β-lactams and associated antibiotic resistance. The diversity of the active site structure in the members of different MβL subclasses explains different mechanisms of antibiotic hydrolysis and should be t...
Gespeichert in:
Veröffentlicht in: | Biochemistry (Moscow) 2021, Vol.86 (Suppl 1), p.S24-S37 |
---|---|
Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | S37 |
---|---|
container_issue | Suppl 1 |
container_start_page | S24 |
container_title | Biochemistry (Moscow) |
container_volume | 86 |
creator | Levina, Elena O. Khrenova, Maria G. |
description | The review focuses on bacterial metallo-β-lactamases (MβLs) responsible for the inactivation of β-lactams and associated antibiotic resistance. The diversity of the active site structure in the members of different MβL subclasses explains different mechanisms of antibiotic hydrolysis and should be taken into account when searching for potential MβL inhibitors. The review describes the features of the antibiotic inactivation mechanisms by various MβLs studied by X-ray crystallography, NMR, kinetic measurements, and molecular modeling. The mechanisms of enzyme inhibition for each MβL subclass are discussed. |
doi_str_mv | 10.1134/S0006297921140030 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2510265699</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2510265699</sourcerecordid><originalsourceid>FETCH-LOGICAL-c372t-f1fde74c0b3c2007829588419a9d7a83780cf8b510d4c872e88d9933598e73a53</originalsourceid><addsrcrecordid>eNp1kc1O3DAURq0KVIZpH6AbFIlNN4FrO4ltdqNRC0iDkEq7jjzODWOUONR2qPpafRCeCYfhRypiY8s65_uupUvIFwpHlPLi-AoAKqaEYpQWABw-kBmtQOYcCtghswnnE98j-yHcpCcDxT-SPc4lE1zJGflzgVF33ZDf_8tX2kTd64DhJDt3bTeiM5gNbRY3mC1MtHeYXdmYjuhHE0efoHuEF2g22tnQh0lfuGjXdojWZD8w2BD11KNdk1o3iUQ7uE9kt9VdwM9P95z8-v7t5_IsX12eni8Xq9xwwWLe0rZBURhYc8MAhGSqlLKgSqtGaMmFBNPKdUmhKYwUDKVslOK8VBIF1yWfk6_b3ls__B4xxLq3wWDXaYfDGGqWoqwqqxSak8P_1Jth9C79rmaF4qyUlYRk0a1l_BCCx7a-9bbX_m9NoZ62Ur_ZSsocPDWP6x6bl8TzGpLAtkJIyF2jfx39fusDpfCV-Q</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2493258680</pqid></control><display><type>article</type><title>Metallo-β-Lactamases: Influence of the Active Site Structure on the Mechanisms of Antibiotic Resistance and Inhibition</title><source>SpringerNature Journals</source><creator>Levina, Elena O. ; Khrenova, Maria G.</creator><creatorcontrib>Levina, Elena O. ; Khrenova, Maria G.</creatorcontrib><description>The review focuses on bacterial metallo-β-lactamases (MβLs) responsible for the inactivation of β-lactams and associated antibiotic resistance. The diversity of the active site structure in the members of different MβL subclasses explains different mechanisms of antibiotic hydrolysis and should be taken into account when searching for potential MβL inhibitors. The review describes the features of the antibiotic inactivation mechanisms by various MβLs studied by X-ray crystallography, NMR, kinetic measurements, and molecular modeling. The mechanisms of enzyme inhibition for each MβL subclass are discussed.</description><identifier>ISSN: 0006-2979</identifier><identifier>EISSN: 1608-3040</identifier><identifier>DOI: 10.1134/S0006297921140030</identifier><identifier>PMID: 33827398</identifier><language>eng</language><publisher>Moscow: Pleiades Publishing</publisher><subject>Antibiotic resistance ; Antibiotics ; Biochemistry ; Biomedical and Life Sciences ; Biomedicine ; Bioorganic Chemistry ; Crystallography ; Deactivation ; Drug resistance ; Inactivation ; Life Sciences ; Metallography ; Microbiology ; Molecular modelling ; NMR ; Nuclear magnetic resonance ; Review ; X-ray crystallography ; β Lactamase ; β-Lactam antibiotics</subject><ispartof>Biochemistry (Moscow), 2021, Vol.86 (Suppl 1), p.S24-S37</ispartof><rights>Pleiades Publishing, Ltd. 2021</rights><rights>Pleiades Publishing, Ltd. 2021.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c372t-f1fde74c0b3c2007829588419a9d7a83780cf8b510d4c872e88d9933598e73a53</citedby><cites>FETCH-LOGICAL-c372t-f1fde74c0b3c2007829588419a9d7a83780cf8b510d4c872e88d9933598e73a53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1134/S0006297921140030$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1134/S0006297921140030$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33827398$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Levina, Elena O.</creatorcontrib><creatorcontrib>Khrenova, Maria G.</creatorcontrib><title>Metallo-β-Lactamases: Influence of the Active Site Structure on the Mechanisms of Antibiotic Resistance and Inhibition</title><title>Biochemistry (Moscow)</title><addtitle>Biochemistry Moscow</addtitle><addtitle>Biochemistry (Mosc)</addtitle><description>The review focuses on bacterial metallo-β-lactamases (MβLs) responsible for the inactivation of β-lactams and associated antibiotic resistance. The diversity of the active site structure in the members of different MβL subclasses explains different mechanisms of antibiotic hydrolysis and should be taken into account when searching for potential MβL inhibitors. The review describes the features of the antibiotic inactivation mechanisms by various MβLs studied by X-ray crystallography, NMR, kinetic measurements, and molecular modeling. The mechanisms of enzyme inhibition for each MβL subclass are discussed.</description><subject>Antibiotic resistance</subject><subject>Antibiotics</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Bioorganic Chemistry</subject><subject>Crystallography</subject><subject>Deactivation</subject><subject>Drug resistance</subject><subject>Inactivation</subject><subject>Life Sciences</subject><subject>Metallography</subject><subject>Microbiology</subject><subject>Molecular modelling</subject><subject>NMR</subject><subject>Nuclear magnetic resonance</subject><subject>Review</subject><subject>X-ray crystallography</subject><subject>β Lactamase</subject><subject>β-Lactam antibiotics</subject><issn>0006-2979</issn><issn>1608-3040</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kc1O3DAURq0KVIZpH6AbFIlNN4FrO4ltdqNRC0iDkEq7jjzODWOUONR2qPpafRCeCYfhRypiY8s65_uupUvIFwpHlPLi-AoAKqaEYpQWABw-kBmtQOYcCtghswnnE98j-yHcpCcDxT-SPc4lE1zJGflzgVF33ZDf_8tX2kTd64DhJDt3bTeiM5gNbRY3mC1MtHeYXdmYjuhHE0efoHuEF2g22tnQh0lfuGjXdojWZD8w2BD11KNdk1o3iUQ7uE9kt9VdwM9P95z8-v7t5_IsX12eni8Xq9xwwWLe0rZBURhYc8MAhGSqlLKgSqtGaMmFBNPKdUmhKYwUDKVslOK8VBIF1yWfk6_b3ls__B4xxLq3wWDXaYfDGGqWoqwqqxSak8P_1Jth9C79rmaF4qyUlYRk0a1l_BCCx7a-9bbX_m9NoZ62Ur_ZSsocPDWP6x6bl8TzGpLAtkJIyF2jfx39fusDpfCV-Q</recordid><startdate>2021</startdate><enddate>2021</enddate><creator>Levina, Elena O.</creator><creator>Khrenova, Maria G.</creator><general>Pleiades Publishing</general><general>Springer Nature B.V</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8C1</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>2021</creationdate><title>Metallo-β-Lactamases: Influence of the Active Site Structure on the Mechanisms of Antibiotic Resistance and Inhibition</title><author>Levina, Elena O. ; Khrenova, Maria G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c372t-f1fde74c0b3c2007829588419a9d7a83780cf8b510d4c872e88d9933598e73a53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Antibiotic resistance</topic><topic>Antibiotics</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Bioorganic Chemistry</topic><topic>Crystallography</topic><topic>Deactivation</topic><topic>Drug resistance</topic><topic>Inactivation</topic><topic>Life Sciences</topic><topic>Metallography</topic><topic>Microbiology</topic><topic>Molecular modelling</topic><topic>NMR</topic><topic>Nuclear magnetic resonance</topic><topic>Review</topic><topic>X-ray crystallography</topic><topic>β Lactamase</topic><topic>β-Lactam antibiotics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Levina, Elena O.</creatorcontrib><creatorcontrib>Khrenova, Maria G.</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Moscow)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Levina, Elena O.</au><au>Khrenova, Maria G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Metallo-β-Lactamases: Influence of the Active Site Structure on the Mechanisms of Antibiotic Resistance and Inhibition</atitle><jtitle>Biochemistry (Moscow)</jtitle><stitle>Biochemistry Moscow</stitle><addtitle>Biochemistry (Mosc)</addtitle><date>2021</date><risdate>2021</risdate><volume>86</volume><issue>Suppl 1</issue><spage>S24</spage><epage>S37</epage><pages>S24-S37</pages><issn>0006-2979</issn><eissn>1608-3040</eissn><abstract>The review focuses on bacterial metallo-β-lactamases (MβLs) responsible for the inactivation of β-lactams and associated antibiotic resistance. The diversity of the active site structure in the members of different MβL subclasses explains different mechanisms of antibiotic hydrolysis and should be taken into account when searching for potential MβL inhibitors. The review describes the features of the antibiotic inactivation mechanisms by various MβLs studied by X-ray crystallography, NMR, kinetic measurements, and molecular modeling. The mechanisms of enzyme inhibition for each MβL subclass are discussed.</abstract><cop>Moscow</cop><pub>Pleiades Publishing</pub><pmid>33827398</pmid><doi>10.1134/S0006297921140030</doi></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0006-2979 |
ispartof | Biochemistry (Moscow), 2021, Vol.86 (Suppl 1), p.S24-S37 |
issn | 0006-2979 1608-3040 |
language | eng |
recordid | cdi_proquest_miscellaneous_2510265699 |
source | SpringerNature Journals |
subjects | Antibiotic resistance Antibiotics Biochemistry Biomedical and Life Sciences Biomedicine Bioorganic Chemistry Crystallography Deactivation Drug resistance Inactivation Life Sciences Metallography Microbiology Molecular modelling NMR Nuclear magnetic resonance Review X-ray crystallography β Lactamase β-Lactam antibiotics |
title | Metallo-β-Lactamases: Influence of the Active Site Structure on the Mechanisms of Antibiotic Resistance and Inhibition |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-23T02%3A52%3A12IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Metallo-%CE%B2-Lactamases:%20Influence%20of%20the%20Active%20Site%20Structure%20on%20the%20Mechanisms%20of%20Antibiotic%20Resistance%20and%20Inhibition&rft.jtitle=Biochemistry%20(Moscow)&rft.au=Levina,%20Elena%20O.&rft.date=2021&rft.volume=86&rft.issue=Suppl%201&rft.spage=S24&rft.epage=S37&rft.pages=S24-S37&rft.issn=0006-2979&rft.eissn=1608-3040&rft_id=info:doi/10.1134/S0006297921140030&rft_dat=%3Cproquest_cross%3E2510265699%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2493258680&rft_id=info:pmid/33827398&rfr_iscdi=true |