Tobramycin Adenylyltransferase: A New Aminoglycoside-Inactivating Enzyme from Staphylococcus epidermidis

Certain strains of Staphylococcus epidermidis resistant to the aminoglycoside antibiotics were shown to contain an enzyme that inactivates the kanamycins, neomycins, butirosins, paromomycin, gentamicin A, amikacin, and tobramycin by adenylylation. Tobramycin adenylyltransferase, as this enzyme is ca...

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Veröffentlicht in:	The Journal of infectious diseases 1976-08, Vol.134, p.S33-S39
Hauptverfasser:	Santanam, Partha, Kayser, Fritz H.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate Aminoglycosides Aminoglycosides - metabolism Anti-Bacterial Agents - metabolism Antibiotics Bacteria Cell extracts Chemical suspensions Drug Resistance, Microbial Enzyme Activation - drug effects Enzyme substrates Enzymes Microbial Sensitivity Tests Microbiology and Biochemistry Nucleotidyltransferases - isolation & purification Plasmids Staphylococcus Staphylococcus - enzymology Staphylococcus epidermidis Tobramycin - metabolism
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container_title	The Journal of infectious diseases
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creator	Santanam, Partha Kayser, Fritz H.
description	Certain strains of Staphylococcus epidermidis resistant to the aminoglycoside antibiotics were shown to contain an enzyme that inactivates the kanamycins, neomycins, butirosins, paromomycin, gentamicin A, amikacin, and tobramycin by adenylylation. Tobramycin adenylyltransferase, as this enzyme is called, was found to be optimally active at pH 5.5. With paromomycin or neomycin B and C as substrates, however, two pH values (5.5 and 9.0) for optimal activity were observed. The enzyme requires Mg⁺⁺ for activity and is stabilized significantly by dithiothreitol. It is probable that the 4′-hydroxyl group of ring I of the antibiotics is adenylylated. Those aminoglycosides that are not substrates for the enzyme lack a hydroxyl group in the corresponding position.
doi_str_mv	10.1093/infdis/134.Supplement_1.S33
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Tobramycin adenylyltransferase, as this enzyme is called, was found to be optimally active at pH 5.5. With paromomycin or neomycin B and C as substrates, however, two pH values (5.5 and 9.0) for optimal activity were observed. The enzyme requires Mg⁺⁺ for activity and is stabilized significantly by dithiothreitol. It is probable that the 4′-hydroxyl group of ring I of the antibiotics is adenylylated. Those aminoglycosides that are not substrates for the enzyme lack a hydroxyl group in the corresponding position.</description><identifier>ISSN: 0022-1899</identifier><identifier>DOI: 10.1093/infdis/134.Supplement_1.S33</identifier><identifier>PMID: 972283</identifier><language>eng</language><publisher>United States: University of Chicago Press</publisher><subject>Adenosine Triphosphate ; Aminoglycosides ; Aminoglycosides - metabolism ; Anti-Bacterial Agents - metabolism ; Antibiotics ; Bacteria ; Cell extracts ; Chemical suspensions ; Drug Resistance, Microbial ; Enzyme Activation - drug effects ; Enzyme substrates ; Enzymes ; Microbial Sensitivity Tests ; Microbiology and Biochemistry ; Nucleotidyltransferases - isolation & purification ; Plasmids ; Staphylococcus ; Staphylococcus - enzymology ; Staphylococcus epidermidis ; Tobramycin - metabolism</subject><ispartof>The Journal of infectious diseases, 1976-08, Vol.134, p.S33-S39</ispartof><rights>Copyright 1976 University of Chicago</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/30106952$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/30106952$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,778,782,801,27907,27908,58000,58233</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/972283$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Santanam, Partha</creatorcontrib><creatorcontrib>Kayser, Fritz H.</creatorcontrib><title>Tobramycin Adenylyltransferase: A New Aminoglycoside-Inactivating Enzyme from Staphylococcus epidermidis</title><title>The Journal of infectious diseases</title><addtitle>J Infect Dis</addtitle><description>Certain strains of Staphylococcus epidermidis resistant to the aminoglycoside antibiotics were shown to contain an enzyme that inactivates the kanamycins, neomycins, butirosins, paromomycin, gentamicin A, amikacin, and tobramycin by adenylylation. Tobramycin adenylyltransferase, as this enzyme is called, was found to be optimally active at pH 5.5. With paromomycin or neomycin B and C as substrates, however, two pH values (5.5 and 9.0) for optimal activity were observed. The enzyme requires Mg⁺⁺ for activity and is stabilized significantly by dithiothreitol. It is probable that the 4′-hydroxyl group of ring I of the antibiotics is adenylylated. Those aminoglycosides that are not substrates for the enzyme lack a hydroxyl group in the corresponding position.</description><subject>Adenosine Triphosphate</subject><subject>Aminoglycosides</subject><subject>Aminoglycosides - metabolism</subject><subject>Anti-Bacterial Agents - metabolism</subject><subject>Antibiotics</subject><subject>Bacteria</subject><subject>Cell extracts</subject><subject>Chemical suspensions</subject><subject>Drug Resistance, Microbial</subject><subject>Enzyme Activation - drug effects</subject><subject>Enzyme substrates</subject><subject>Enzymes</subject><subject>Microbial Sensitivity Tests</subject><subject>Microbiology and Biochemistry</subject><subject>Nucleotidyltransferases - isolation & purification</subject><subject>Plasmids</subject><subject>Staphylococcus</subject><subject>Staphylococcus - enzymology</subject><subject>Staphylococcus epidermidis</subject><subject>Tobramycin - metabolism</subject><issn>0022-1899</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1976</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kF1LwzAYhXPh9_QfKBQE77rlo1kb78aYOhh6sXldsuTtltEkNWmV-ustbHh1Lp6Hw-Eg9EjwmGDBJsZV2sQJYdl43TVNDRZcW5LxmrEzdI0xpSkphLhCNzEeMMYZm-aX6ELklBbsGu03fhuk7ZVxyUyD6-u-boN0sYIgIzwns-QdfpKZNc7v6l75aDSkSydVa75la9wuWbjf3kJSBW-TdSubfV975ZXqYgLNYAdrhoW36LySdYS7U47Q58tiM39LVx-vy_lslR4IF23KZc7oVuXABGhV6azQhFFOtnSqNOEaFNeUcJAqlwXJpoOvskoUouJFwVXORujp2NsE_9VBbEtrooK6lg58F8uCZTkbbhnE-5PYbS3osgnGytCXx2cG_HDEh9j68E8ZJngqOGV_Dbh1eA</recordid><startdate>197608</startdate><enddate>197608</enddate><creator>Santanam, Partha</creator><creator>Kayser, Fritz H.</creator><general>University of Chicago Press</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>197608</creationdate><title>Tobramycin Adenylyltransferase: A New Aminoglycoside-Inactivating Enzyme from Staphylococcus epidermidis</title><author>Santanam, Partha ; Kayser, Fritz H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-j159t-5a732bc7e39edcfd48d13251b26cd15dec5d215eac7a81465a7c4f989f5885c73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1976</creationdate><topic>Adenosine Triphosphate</topic><topic>Aminoglycosides</topic><topic>Aminoglycosides - metabolism</topic><topic>Anti-Bacterial Agents - metabolism</topic><topic>Antibiotics</topic><topic>Bacteria</topic><topic>Cell extracts</topic><topic>Chemical suspensions</topic><topic>Drug Resistance, Microbial</topic><topic>Enzyme Activation - drug effects</topic><topic>Enzyme substrates</topic><topic>Enzymes</topic><topic>Microbial Sensitivity Tests</topic><topic>Microbiology and Biochemistry</topic><topic>Nucleotidyltransferases - isolation & purification</topic><topic>Plasmids</topic><topic>Staphylococcus</topic><topic>Staphylococcus - enzymology</topic><topic>Staphylococcus epidermidis</topic><topic>Tobramycin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Santanam, Partha</creatorcontrib><creatorcontrib>Kayser, Fritz H.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of infectious diseases</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Santanam, Partha</au><au>Kayser, Fritz H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tobramycin Adenylyltransferase: A New Aminoglycoside-Inactivating Enzyme from Staphylococcus epidermidis</atitle><jtitle>The Journal of infectious diseases</jtitle><addtitle>J Infect Dis</addtitle><date>1976-08</date><risdate>1976</risdate><volume>134</volume><spage>S33</spage><epage>S39</epage><pages>S33-S39</pages><issn>0022-1899</issn><abstract>Certain strains of Staphylococcus epidermidis resistant to the aminoglycoside antibiotics were shown to contain an enzyme that inactivates the kanamycins, neomycins, butirosins, paromomycin, gentamicin A, amikacin, and tobramycin by adenylylation. 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subjects	Adenosine Triphosphate Aminoglycosides Aminoglycosides - metabolism Anti-Bacterial Agents - metabolism Antibiotics Bacteria Cell extracts Chemical suspensions Drug Resistance, Microbial Enzyme Activation - drug effects Enzyme substrates Enzymes Microbial Sensitivity Tests Microbiology and Biochemistry Nucleotidyltransferases - isolation & purification Plasmids Staphylococcus Staphylococcus - enzymology Staphylococcus epidermidis Tobramycin - metabolism
title	Tobramycin Adenylyltransferase: A New Aminoglycoside-Inactivating Enzyme from Staphylococcus epidermidis
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