Energy conservation in fermentative glutarate degradation by the bacterial strain WoGl3
Abstract Dicarboxylic acids with 2–5 carbon atoms can be degraded fermentatively by pure cultures of various strictly anaerobic bacteria. The small amount of free energy released in these decarboxylations (about 20–25 kJ mol−1) is conserved as sole source of growth energy either through sodium-pumpi...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Matthies, Carola [verfasserIn] Schink, Bernhard [verfasserIn] |
|---|
| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1992 |
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| Schlagwörter: |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
|---|---|
| Übergeordnetes Werk: |
In: FEMS microbiology letters - Federation of European Microbiological Societies ; GKD-ID: 114439X, Oxford [u.a.] : Wiley-Blackwell, 1977, 100(1992), 1/3, Seite 0 |
| Übergeordnetes Werk: |
volume:100 ; year:1992 ; number:1/3 ; pages:0 |
| Links: |
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| DOI / URN: |
10.1111/j.1574-6968.1992.tb14044.x |
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NLEJ239806182 |
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| 520 | |a Abstract Dicarboxylic acids with 2–5 carbon atoms can be degraded fermentatively by pure cultures of various strictly anaerobic bacteria. The small amount of free energy released in these decarboxylations (about 20–25 kJ mol−1) is conserved as sole source of growth energy either through sodium-pumping decarboxylases or through electrogenic substrate/product transport devices. In the glutarate-fermenting bacterial strain WoGl3 a glutaconyl-CoA-decarboxylating enzyme activity was detected. This enzyme was inhibited by avidin and was stimulated by sodium ions. The enzyme activity was partially associated with the cytoplasmic membrane, indicating that energy conservation is accomplished through a sodium-ion-pumping glutaconyl-CoA decarboxylase enzyme. | ||
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10.1111/j.1574-6968.1992.tb14044.x doi (DE-627)NLEJ239806182 DE-627 ger DE-627 rakwb Matthies, Carola verfasserin aut Energy conservation in fermentative glutarate degradation by the bacterial strain WoGl3 Oxford, UK Blackwell Publishing Ltd 1992 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract Dicarboxylic acids with 2–5 carbon atoms can be degraded fermentatively by pure cultures of various strictly anaerobic bacteria. The small amount of free energy released in these decarboxylations (about 20–25 kJ mol−1) is conserved as sole source of growth energy either through sodium-pumping decarboxylases or through electrogenic substrate/product transport devices. In the glutarate-fermenting bacterial strain WoGl3 a glutaconyl-CoA-decarboxylating enzyme activity was detected. This enzyme was inhibited by avidin and was stimulated by sodium ions. The enzyme activity was partially associated with the cytoplasmic membrane, indicating that energy conservation is accomplished through a sodium-ion-pumping glutaconyl-CoA decarboxylase enzyme. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Decarboxylation Schink, Bernhard verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 100(1992), 1/3, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:100 year:1992 number:1/3 pages:0 http://dx.doi.org/10.1111/j.1574-6968.1992.tb14044.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 100 1992 1/3 0 |
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10.1111/j.1574-6968.1992.tb14044.x doi (DE-627)NLEJ239806182 DE-627 ger DE-627 rakwb Matthies, Carola verfasserin aut Energy conservation in fermentative glutarate degradation by the bacterial strain WoGl3 Oxford, UK Blackwell Publishing Ltd 1992 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract Dicarboxylic acids with 2–5 carbon atoms can be degraded fermentatively by pure cultures of various strictly anaerobic bacteria. The small amount of free energy released in these decarboxylations (about 20–25 kJ mol−1) is conserved as sole source of growth energy either through sodium-pumping decarboxylases or through electrogenic substrate/product transport devices. In the glutarate-fermenting bacterial strain WoGl3 a glutaconyl-CoA-decarboxylating enzyme activity was detected. This enzyme was inhibited by avidin and was stimulated by sodium ions. The enzyme activity was partially associated with the cytoplasmic membrane, indicating that energy conservation is accomplished through a sodium-ion-pumping glutaconyl-CoA decarboxylase enzyme. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Decarboxylation Schink, Bernhard verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 100(1992), 1/3, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:100 year:1992 number:1/3 pages:0 http://dx.doi.org/10.1111/j.1574-6968.1992.tb14044.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 100 1992 1/3 0 |
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10.1111/j.1574-6968.1992.tb14044.x doi (DE-627)NLEJ239806182 DE-627 ger DE-627 rakwb Matthies, Carola verfasserin aut Energy conservation in fermentative glutarate degradation by the bacterial strain WoGl3 Oxford, UK Blackwell Publishing Ltd 1992 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract Dicarboxylic acids with 2–5 carbon atoms can be degraded fermentatively by pure cultures of various strictly anaerobic bacteria. The small amount of free energy released in these decarboxylations (about 20–25 kJ mol−1) is conserved as sole source of growth energy either through sodium-pumping decarboxylases or through electrogenic substrate/product transport devices. In the glutarate-fermenting bacterial strain WoGl3 a glutaconyl-CoA-decarboxylating enzyme activity was detected. This enzyme was inhibited by avidin and was stimulated by sodium ions. The enzyme activity was partially associated with the cytoplasmic membrane, indicating that energy conservation is accomplished through a sodium-ion-pumping glutaconyl-CoA decarboxylase enzyme. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Decarboxylation Schink, Bernhard verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 100(1992), 1/3, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:100 year:1992 number:1/3 pages:0 http://dx.doi.org/10.1111/j.1574-6968.1992.tb14044.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 100 1992 1/3 0 |
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10.1111/j.1574-6968.1992.tb14044.x doi (DE-627)NLEJ239806182 DE-627 ger DE-627 rakwb Matthies, Carola verfasserin aut Energy conservation in fermentative glutarate degradation by the bacterial strain WoGl3 Oxford, UK Blackwell Publishing Ltd 1992 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract Dicarboxylic acids with 2–5 carbon atoms can be degraded fermentatively by pure cultures of various strictly anaerobic bacteria. The small amount of free energy released in these decarboxylations (about 20–25 kJ mol−1) is conserved as sole source of growth energy either through sodium-pumping decarboxylases or through electrogenic substrate/product transport devices. In the glutarate-fermenting bacterial strain WoGl3 a glutaconyl-CoA-decarboxylating enzyme activity was detected. This enzyme was inhibited by avidin and was stimulated by sodium ions. The enzyme activity was partially associated with the cytoplasmic membrane, indicating that energy conservation is accomplished through a sodium-ion-pumping glutaconyl-CoA decarboxylase enzyme. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Decarboxylation Schink, Bernhard verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 100(1992), 1/3, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:100 year:1992 number:1/3 pages:0 http://dx.doi.org/10.1111/j.1574-6968.1992.tb14044.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 100 1992 1/3 0 |
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10.1111/j.1574-6968.1992.tb14044.x doi (DE-627)NLEJ239806182 DE-627 ger DE-627 rakwb Matthies, Carola verfasserin aut Energy conservation in fermentative glutarate degradation by the bacterial strain WoGl3 Oxford, UK Blackwell Publishing Ltd 1992 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract Dicarboxylic acids with 2–5 carbon atoms can be degraded fermentatively by pure cultures of various strictly anaerobic bacteria. The small amount of free energy released in these decarboxylations (about 20–25 kJ mol−1) is conserved as sole source of growth energy either through sodium-pumping decarboxylases or through electrogenic substrate/product transport devices. In the glutarate-fermenting bacterial strain WoGl3 a glutaconyl-CoA-decarboxylating enzyme activity was detected. This enzyme was inhibited by avidin and was stimulated by sodium ions. The enzyme activity was partially associated with the cytoplasmic membrane, indicating that energy conservation is accomplished through a sodium-ion-pumping glutaconyl-CoA decarboxylase enzyme. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Decarboxylation Schink, Bernhard verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 100(1992), 1/3, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:100 year:1992 number:1/3 pages:0 http://dx.doi.org/10.1111/j.1574-6968.1992.tb14044.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 100 1992 1/3 0 |
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Abstract Dicarboxylic acids with 2–5 carbon atoms can be degraded fermentatively by pure cultures of various strictly anaerobic bacteria. The small amount of free energy released in these decarboxylations (about 20–25 kJ mol−1) is conserved as sole source of growth energy either through sodium-pumping decarboxylases or through electrogenic substrate/product transport devices. In the glutarate-fermenting bacterial strain WoGl3 a glutaconyl-CoA-decarboxylating enzyme activity was detected. This enzyme was inhibited by avidin and was stimulated by sodium ions. The enzyme activity was partially associated with the cytoplasmic membrane, indicating that energy conservation is accomplished through a sodium-ion-pumping glutaconyl-CoA decarboxylase enzyme. |
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Abstract Dicarboxylic acids with 2–5 carbon atoms can be degraded fermentatively by pure cultures of various strictly anaerobic bacteria. The small amount of free energy released in these decarboxylations (about 20–25 kJ mol−1) is conserved as sole source of growth energy either through sodium-pumping decarboxylases or through electrogenic substrate/product transport devices. In the glutarate-fermenting bacterial strain WoGl3 a glutaconyl-CoA-decarboxylating enzyme activity was detected. This enzyme was inhibited by avidin and was stimulated by sodium ions. The enzyme activity was partially associated with the cytoplasmic membrane, indicating that energy conservation is accomplished through a sodium-ion-pumping glutaconyl-CoA decarboxylase enzyme. |
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Abstract Dicarboxylic acids with 2–5 carbon atoms can be degraded fermentatively by pure cultures of various strictly anaerobic bacteria. The small amount of free energy released in these decarboxylations (about 20–25 kJ mol−1) is conserved as sole source of growth energy either through sodium-pumping decarboxylases or through electrogenic substrate/product transport devices. In the glutarate-fermenting bacterial strain WoGl3 a glutaconyl-CoA-decarboxylating enzyme activity was detected. This enzyme was inhibited by avidin and was stimulated by sodium ions. The enzyme activity was partially associated with the cytoplasmic membrane, indicating that energy conservation is accomplished through a sodium-ion-pumping glutaconyl-CoA decarboxylase enzyme. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ239806182</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707094526.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120426s1992 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1111/j.1574-6968.1992.tb14044.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ239806182</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Matthies, Carola</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Energy conservation in fermentative glutarate degradation by the bacterial strain WoGl3</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Publishing Ltd</subfield><subfield code="c">1992</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract Dicarboxylic acids with 2–5 carbon atoms can be degraded fermentatively by pure cultures of various strictly anaerobic bacteria. The small amount of free energy released in these decarboxylations (about 20–25 kJ mol−1) is conserved as sole source of growth energy either through sodium-pumping decarboxylases or through electrogenic substrate/product transport devices. In the glutarate-fermenting bacterial strain WoGl3 a glutaconyl-CoA-decarboxylating enzyme activity was detected. This enzyme was inhibited by avidin and was stimulated by sodium ions. The enzyme activity was partially associated with the cytoplasmic membrane, indicating that energy conservation is accomplished through a sodium-ion-pumping glutaconyl-CoA decarboxylase enzyme.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="d">2006</subfield><subfield code="f">Blackwell Publishing Journal Backfiles 1879-2005</subfield><subfield code="7">|2006||||||||||</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Decarboxylation</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Schink, Bernhard</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="a">Federation of European Microbiological Societies ; GKD-ID: 114439X</subfield><subfield code="t">FEMS microbiology letters</subfield><subfield code="d">Oxford [u.a.] : Wiley-Blackwell, 1977</subfield><subfield code="g">100(1992), 1/3, Seite 0</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)NLEJ243927053</subfield><subfield code="w">(DE-600)1501716-3</subfield><subfield code="x">1574-6968</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:100</subfield><subfield code="g">year:1992</subfield><subfield code="g">number:1/3</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1111/j.1574-6968.1992.tb14044.x</subfield><subfield code="q">text/html</subfield><subfield code="x">Verlag</subfield><subfield code="z">Deutschlandweit zugänglich</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-DJB</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">100</subfield><subfield code="j">1992</subfield><subfield code="e">1/3</subfield><subfield code="h">0</subfield></datafield></record></collection>
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7.400667 |