Inhibition of phosphofructokinases by copper(II)
Abstract The biochemical inhibition by Cu2+ on eight phylogenetically and biochemically different phosphofructokinases (PFKs) was investigated. The enzymes screened included representatives from thermophilic and mesophilic bacteria, a hyperthermophilic archaeon and a eukaryote, covering all three ph...
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| Veröffentlicht in: | FEMS microbiology letters 2001-04, Vol.197 (1), p.105-109 |
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| container_title | FEMS microbiology letters |
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| creator | Gebhard, Susanne Ronimus, Ron S. Morgan, Hugh W. |
| description | Abstract
The biochemical inhibition by Cu2+ on eight phylogenetically and biochemically different phosphofructokinases (PFKs) was investigated. The enzymes screened included representatives from thermophilic and mesophilic bacteria, a hyperthermophilic archaeon and a eukaryote, covering all three phosphoryl donor subtypes (ATP, ADP and pyrophosphate). The sensitivities of the enzymes to Cu2+ varied greatly, with the archaeal ADP-PFK being the least and the eukaryote ATP-PFK being the most sensitive. The bacterial ATP- and pyrophosphate-dependent PFKs showed intermediate sensitivity with the exception of the Spirochaeta thermophila enzyme (pyrophosphate-dependent) which was relatively resistant. |
| doi_str_mv | 10.1111/j.1574-6968.2001.tb10590.x |
| format | Article |
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The biochemical inhibition by Cu2+ on eight phylogenetically and biochemically different phosphofructokinases (PFKs) was investigated. The enzymes screened included representatives from thermophilic and mesophilic bacteria, a hyperthermophilic archaeon and a eukaryote, covering all three phosphoryl donor subtypes (ATP, ADP and pyrophosphate). The sensitivities of the enzymes to Cu2+ varied greatly, with the archaeal ADP-PFK being the least and the eukaryote ATP-PFK being the most sensitive. The bacterial ATP- and pyrophosphate-dependent PFKs showed intermediate sensitivity with the exception of the Spirochaeta thermophila enzyme (pyrophosphate-dependent) which was relatively resistant.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.2001.tb10590.x</identifier><identifier>PMID: 11287154</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Adenosine diphosphate ; Animals ; Bacteria ; Bacteria - enzymology ; Bacteriology ; Biohydrometallurgy. Microbial leaching ; Biological and medical sciences ; Biotechnology ; Copper ; Copper - pharmacology ; Copper compounds ; Copper(II) ; Enzyme Inhibitors - pharmacology ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Glycolysis ; Industrial applications and implications. Economical aspects ; Mesophilic bacteria ; Microbiology ; Muscle, Smooth - enzymology ; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains ; Phosphofructokinase ; Phosphofructokinase-1 - antagonists & inhibitors ; Phosphofructokinase-1 - metabolism ; Phylogeny ; Rabbits ; Sensitivity ; Spirochaeta thermophila ; Thermococcus - enzymology ; Thermophilic ; Thermophilic bacteria ; Toxicity</subject><ispartof>FEMS microbiology letters, 2001-04, Vol.197 (1), p.105-109</ispartof><rights>2001 Federation of European Microbiological Societies 2001</rights><rights>2002 INIST-CNRS</rights><rights>2001 Federation of European Microbiological Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4895-bf7283796693357a8f1fe8ad5b0c1d893d98242906fbdbb1297f2f1b409a59803</citedby><cites>FETCH-LOGICAL-c4895-bf7283796693357a8f1fe8ad5b0c1d893d98242906fbdbb1297f2f1b409a59803</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.1574-6968.2001.tb10590.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1574-6968.2001.tb10590.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14162239$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11287154$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gebhard, Susanne</creatorcontrib><creatorcontrib>Ronimus, Ron S.</creatorcontrib><creatorcontrib>Morgan, Hugh W.</creatorcontrib><title>Inhibition of phosphofructokinases by copper(II)</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>Abstract
The biochemical inhibition by Cu2+ on eight phylogenetically and biochemically different phosphofructokinases (PFKs) was investigated. The enzymes screened included representatives from thermophilic and mesophilic bacteria, a hyperthermophilic archaeon and a eukaryote, covering all three phosphoryl donor subtypes (ATP, ADP and pyrophosphate). The sensitivities of the enzymes to Cu2+ varied greatly, with the archaeal ADP-PFK being the least and the eukaryote ATP-PFK being the most sensitive. The bacterial ATP- and pyrophosphate-dependent PFKs showed intermediate sensitivity with the exception of the Spirochaeta thermophila enzyme (pyrophosphate-dependent) which was relatively resistant.</description><subject>Adenosine diphosphate</subject><subject>Animals</subject><subject>Bacteria</subject><subject>Bacteria - enzymology</subject><subject>Bacteriology</subject><subject>Biohydrometallurgy. Microbial leaching</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Copper</subject><subject>Copper - pharmacology</subject><subject>Copper compounds</subject><subject>Copper(II)</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycolysis</subject><subject>Industrial applications and implications. Economical aspects</subject><subject>Mesophilic bacteria</subject><subject>Microbiology</subject><subject>Muscle, Smooth - enzymology</subject><subject>Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains</subject><subject>Phosphofructokinase</subject><subject>Phosphofructokinase-1 - antagonists & inhibitors</subject><subject>Phosphofructokinase-1 - metabolism</subject><subject>Phylogeny</subject><subject>Rabbits</subject><subject>Sensitivity</subject><subject>Spirochaeta thermophila</subject><subject>Thermococcus - enzymology</subject><subject>Thermophilic</subject><subject>Thermophilic bacteria</subject><subject>Toxicity</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqVkNGK1DAUhoMo7uzqK8iguOhF6zlJ0yR7Icji6sCIN3odkjZhO3aamkxx5-1NmeKCKGIgJJDv_CfnI-Q5Qol5vdmVyEVV1KqWJQXA8mARuILy7gFZ_Xp6SFbAhCwQlDgj5yntAKCiUD8mZ4hUCuTVisBmuO1sd-jCsA5-Pd6GlLePU3MI37rBJJfW9rhuwji6-Gqzef2EPPKmT-7pcl6Qrzfvv1x_LLafP2yu322LppKKF9YLKplQda0Y48JIj95J03ILDbZSsVZJWlEFtbettUiV8NSjrUAZriSwC3J5yh1j-D65dND7LjWu783gwpS0EMAoR_VPEIXkolZz4ovfwF2Y4pCH0JRhNsgVZZm6OlFNDClF5_UYu72JR42gZ_16p2fHenasZ_160a_vcvGzpcVk9669L118Z-DlApjUmN5HMzRduucqrCll81BvT9yPrnfH__iCvvm0zdccwE8BYRr_Ul78aYKfbOeuyQ</recordid><startdate>200104</startdate><enddate>200104</enddate><creator>Gebhard, Susanne</creator><creator>Ronimus, Ron S.</creator><creator>Morgan, Hugh W.</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><general>Oxford University Press</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</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>FR3</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>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>200104</creationdate><title>Inhibition of phosphofructokinases by copper(II)</title><author>Gebhard, Susanne ; Ronimus, Ron S. ; Morgan, Hugh W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4895-bf7283796693357a8f1fe8ad5b0c1d893d98242906fbdbb1297f2f1b409a59803</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Adenosine diphosphate</topic><topic>Animals</topic><topic>Bacteria</topic><topic>Bacteria - enzymology</topic><topic>Bacteriology</topic><topic>Biohydrometallurgy. Microbial leaching</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Copper</topic><topic>Copper - pharmacology</topic><topic>Copper compounds</topic><topic>Copper(II)</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycolysis</topic><topic>Industrial applications and implications. 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The biochemical inhibition by Cu2+ on eight phylogenetically and biochemically different phosphofructokinases (PFKs) was investigated. The enzymes screened included representatives from thermophilic and mesophilic bacteria, a hyperthermophilic archaeon and a eukaryote, covering all three phosphoryl donor subtypes (ATP, ADP and pyrophosphate). The sensitivities of the enzymes to Cu2+ varied greatly, with the archaeal ADP-PFK being the least and the eukaryote ATP-PFK being the most sensitive. The bacterial ATP- and pyrophosphate-dependent PFKs showed intermediate sensitivity with the exception of the Spirochaeta thermophila enzyme (pyrophosphate-dependent) which was relatively resistant.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>11287154</pmid><doi>10.1111/j.1574-6968.2001.tb10590.x</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0378-1097 |
| ispartof | FEMS microbiology letters, 2001-04, Vol.197 (1), p.105-109 |
| issn | 0378-1097 1574-6968 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77032519 |
| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | Adenosine diphosphate Animals Bacteria Bacteria - enzymology Bacteriology Biohydrometallurgy. Microbial leaching Biological and medical sciences Biotechnology Copper Copper - pharmacology Copper compounds Copper(II) Enzyme Inhibitors - pharmacology Enzymes Fundamental and applied biological sciences. Psychology Glycolysis Industrial applications and implications. Economical aspects Mesophilic bacteria Microbiology Muscle, Smooth - enzymology Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains Phosphofructokinase Phosphofructokinase-1 - antagonists & inhibitors Phosphofructokinase-1 - metabolism Phylogeny Rabbits Sensitivity Spirochaeta thermophila Thermococcus - enzymology Thermophilic Thermophilic bacteria Toxicity |
| title | Inhibition of phosphofructokinases by copper(II) |
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