Is the Paracoccus halodenitrificans ATPase a chimeric enzyme?
Membranes from Paracoccus halodenitrificans contain an ATPase that is most active in the absence of NaCl. The most unusual characteristic of the enzyme is its pattern of sensitivity to various inhibitors. Azide and rhodamine 6G, inhibitors of F1F0-ATPases, inhibit ATP hydrolysis as do bafilomycin A1...
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| Veröffentlicht in: | FEMS microbiology letters 1996-06, Vol.140 (1), p.55-60 |
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| creator | Hochstein, L. I. |
| description | Membranes from Paracoccus halodenitrificans contain an ATPase that is most active in the absence of NaCl. The most unusual characteristic of the enzyme is its pattern of sensitivity to various inhibitors. Azide and rhodamine 6G, inhibitors of F1F0-ATPases, inhibit ATP hydrolysis as do bafilomycin A1, concanamycin A (folimycin), N-ethylmaleimide, and p-chloromercuriphenylsulfonate which are inhibitors of vacuolar ATPases. This indiscriminate sensitivity suggests that this ATPase may be a hybrid and that caution should be exercised when using inhibition as a diagnostic for distinguishing between F1F0-ATPases and vacuolar ATPases. |
| doi_str_mv | 10.1111/j.1574-6968.1996.tb08314.x |
| format | Article |
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I.</creator><creatorcontrib>Hochstein, L. I.</creatorcontrib><description>Membranes from Paracoccus halodenitrificans contain an ATPase that is most active in the absence of NaCl. The most unusual characteristic of the enzyme is its pattern of sensitivity to various inhibitors. Azide and rhodamine 6G, inhibitors of F1F0-ATPases, inhibit ATP hydrolysis as do bafilomycin A1, concanamycin A (folimycin), N-ethylmaleimide, and p-chloromercuriphenylsulfonate which are inhibitors of vacuolar ATPases. This indiscriminate sensitivity suggests that this ATPase may be a hybrid and that caution should be exercised when using inhibition as a diagnostic for distinguishing between F1F0-ATPases and vacuolar ATPases.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.1996.tb08314.x</identifier><identifier>PMID: 11536735</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Adenosine triphosphatase ; Adenosine Triphosphatases - antagonists & inhibitors ; Adenosine Triphosphatases - metabolism ; Anti-Bacterial Agents - pharmacology ; ATPase ; Azides - pharmacology ; Bacteriology ; Bafilomycin ; Biological and medical sciences ; Concanamycin ; Concanamycin A ; Diagnostic systems ; Dicyclohexylcarbodiimide - pharmacology ; Enzyme Inhibitors - pharmacology ; Enzymes ; Ethylmaleimide - pharmacology ; Fundamental and applied biological sciences. Psychology ; Halophile ; Inhibitors ; Life Sciences (General) ; Macrolides ; Membranes - drug effects ; Membranes - enzymology ; Metabolism. Enzymes ; Microbiology ; N-Ethylmaleimide ; Nitrates - pharmacology ; Paracoccus - enzymology ; Paracoccus halodenitrificans ; Potassium Chloride - pharmacology ; Proton-Translocating ATPases - antagonists & inhibitors ; Proton-Translocating ATPases - metabolism ; p‐Chloromercuriphenylsulfonate ; Rhodamine 6G ; Rhodamines - pharmacology ; Sensitivity ; Sodium chloride ; Sodium Chloride - pharmacology ; Vacuolar Proton-Translocating ATPases</subject><ispartof>FEMS microbiology letters, 1996-06, Vol.140 (1), p.55-60</ispartof><rights>1996 Federation of European Microbiological Societies. All rights reserved 1996</rights><rights>1996 INIST-CNRS</rights><rights>1996 Federation of European Microbiological Societies. All rights reserved</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4565-36306b1940a0b4e7e0d7f471e9a3c5eaa02776ba4e433991d33aaff430abbdb43</citedby><cites>FETCH-LOGICAL-c4565-36306b1940a0b4e7e0d7f471e9a3c5eaa02776ba4e433991d33aaff430abbdb43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1574-6968.1996.tb08314.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1574-6968.1996.tb08314.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,777,781,1412,27905,27906,45555,45556</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3104932$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11536735$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hochstein, L. I.</creatorcontrib><title>Is the Paracoccus halodenitrificans ATPase a chimeric enzyme?</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>Membranes from Paracoccus halodenitrificans contain an ATPase that is most active in the absence of NaCl. The most unusual characteristic of the enzyme is its pattern of sensitivity to various inhibitors. Azide and rhodamine 6G, inhibitors of F1F0-ATPases, inhibit ATP hydrolysis as do bafilomycin A1, concanamycin A (folimycin), N-ethylmaleimide, and p-chloromercuriphenylsulfonate which are inhibitors of vacuolar ATPases. This indiscriminate sensitivity suggests that this ATPase may be a hybrid and that caution should be exercised when using inhibition as a diagnostic for distinguishing between F1F0-ATPases and vacuolar ATPases.</description><subject>Adenosine triphosphatase</subject><subject>Adenosine Triphosphatases - antagonists & inhibitors</subject><subject>Adenosine Triphosphatases - metabolism</subject><subject>Anti-Bacterial Agents - pharmacology</subject><subject>ATPase</subject><subject>Azides - pharmacology</subject><subject>Bacteriology</subject><subject>Bafilomycin</subject><subject>Biological and medical sciences</subject><subject>Concanamycin</subject><subject>Concanamycin A</subject><subject>Diagnostic systems</subject><subject>Dicyclohexylcarbodiimide - pharmacology</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Enzymes</subject><subject>Ethylmaleimide - pharmacology</subject><subject>Fundamental and applied biological sciences. 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Enzymes</subject><subject>Microbiology</subject><subject>N-Ethylmaleimide</subject><subject>Nitrates - pharmacology</subject><subject>Paracoccus - enzymology</subject><subject>Paracoccus halodenitrificans</subject><subject>Potassium Chloride - pharmacology</subject><subject>Proton-Translocating ATPases - antagonists & inhibitors</subject><subject>Proton-Translocating ATPases - metabolism</subject><subject>p‐Chloromercuriphenylsulfonate</subject><subject>Rhodamine 6G</subject><subject>Rhodamines - pharmacology</subject><subject>Sensitivity</subject><subject>Sodium chloride</subject><subject>Sodium Chloride - pharmacology</subject><subject>Vacuolar Proton-Translocating ATPases</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>CYI</sourceid><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqVkl1r1EAUhgdR7Lb6D0SCFu-ynpP52ikUKcVqYcVe1OvhZDJhs-RjnUmw6683IaGC6IVzMxfzvHNeHg5jbxDWOJ73-zVKLVJl1GaNxqh1n8OGo1g_PGGrx6enbAVcb1IEo0_YaYx7ABAZqOfsBFFypblcscvbmPQ7n9xRINc5N8RkR3VX-LbqQ1VWjtqYXN3fUfQJJW5XNT5ULvHtz2PjP7xgz0qqo3-53Gfs283H--vP6fbrp9vrq23qhFQy5YqDytEIIMiF1x4KXQqN3hB30hNBprXKSXjBuTFYcE5UloID5XmRC37G3s3_HkL3ffCxt00Vna9ran03RItSgRGZHsG3f4D7bgjt2M1mnOMGZKbVSF3MlAtdjMGX9hCqhsLRIthJsd3byaOdPNpJsV0U24cx_HoZMeSNL35HF6cjcL4AFB3VZaDWVfGR4wjC8GzELmfsR1X74380sDdftnIaI-d8Nxz-kU7_3v_VnGspkm37MKoZFwMQswyR_wIGF664</recordid><startdate>19960615</startdate><enddate>19960615</enddate><creator>Hochstein, L. 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I.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4565-36306b1940a0b4e7e0d7f471e9a3c5eaa02776ba4e433991d33aaff430abbdb43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Adenosine triphosphatase</topic><topic>Adenosine Triphosphatases - antagonists & inhibitors</topic><topic>Adenosine Triphosphatases - metabolism</topic><topic>Anti-Bacterial Agents - pharmacology</topic><topic>ATPase</topic><topic>Azides - pharmacology</topic><topic>Bacteriology</topic><topic>Bafilomycin</topic><topic>Biological and medical sciences</topic><topic>Concanamycin</topic><topic>Concanamycin A</topic><topic>Diagnostic systems</topic><topic>Dicyclohexylcarbodiimide - pharmacology</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Enzymes</topic><topic>Ethylmaleimide - pharmacology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Halophile</topic><topic>Inhibitors</topic><topic>Life Sciences (General)</topic><topic>Macrolides</topic><topic>Membranes - drug effects</topic><topic>Membranes - enzymology</topic><topic>Metabolism. Enzymes</topic><topic>Microbiology</topic><topic>N-Ethylmaleimide</topic><topic>Nitrates - pharmacology</topic><topic>Paracoccus - enzymology</topic><topic>Paracoccus halodenitrificans</topic><topic>Potassium Chloride - pharmacology</topic><topic>Proton-Translocating ATPases - antagonists & inhibitors</topic><topic>Proton-Translocating ATPases - metabolism</topic><topic>p‐Chloromercuriphenylsulfonate</topic><topic>Rhodamine 6G</topic><topic>Rhodamines - pharmacology</topic><topic>Sensitivity</topic><topic>Sodium chloride</topic><topic>Sodium Chloride - pharmacology</topic><topic>Vacuolar Proton-Translocating ATPases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hochstein, L. 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I.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Is the Paracoccus halodenitrificans ATPase a chimeric enzyme?</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>1996-06-15</date><risdate>1996</risdate><volume>140</volume><issue>1</issue><spage>55</spage><epage>60</epage><pages>55-60</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><abstract>Membranes from Paracoccus halodenitrificans contain an ATPase that is most active in the absence of NaCl. The most unusual characteristic of the enzyme is its pattern of sensitivity to various inhibitors. Azide and rhodamine 6G, inhibitors of F1F0-ATPases, inhibit ATP hydrolysis as do bafilomycin A1, concanamycin A (folimycin), N-ethylmaleimide, and p-chloromercuriphenylsulfonate which are inhibitors of vacuolar ATPases. This indiscriminate sensitivity suggests that this ATPase may be a hybrid and that caution should be exercised when using inhibition as a diagnostic for distinguishing between F1F0-ATPases and vacuolar ATPases.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>11536735</pmid><doi>10.1111/j.1574-6968.1996.tb08314.x</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0378-1097 |
| ispartof | FEMS microbiology letters, 1996-06, Vol.140 (1), p.55-60 |
| issn | 0378-1097 1574-6968 |
| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Oxford University Press Journals All Titles (1996-Current); NASA Technical Reports Server; Alma/SFX Local Collection |
| subjects | Adenosine triphosphatase Adenosine Triphosphatases - antagonists & inhibitors Adenosine Triphosphatases - metabolism Anti-Bacterial Agents - pharmacology ATPase Azides - pharmacology Bacteriology Bafilomycin Biological and medical sciences Concanamycin Concanamycin A Diagnostic systems Dicyclohexylcarbodiimide - pharmacology Enzyme Inhibitors - pharmacology Enzymes Ethylmaleimide - pharmacology Fundamental and applied biological sciences. Psychology Halophile Inhibitors Life Sciences (General) Macrolides Membranes - drug effects Membranes - enzymology Metabolism. Enzymes Microbiology N-Ethylmaleimide Nitrates - pharmacology Paracoccus - enzymology Paracoccus halodenitrificans Potassium Chloride - pharmacology Proton-Translocating ATPases - antagonists & inhibitors Proton-Translocating ATPases - metabolism p‐Chloromercuriphenylsulfonate Rhodamine 6G Rhodamines - pharmacology Sensitivity Sodium chloride Sodium Chloride - pharmacology Vacuolar Proton-Translocating ATPases |
| title | Is the Paracoccus halodenitrificans ATPase a chimeric enzyme? |
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