Allosteric inhibition by phosphoenolpyruvate of glucose-6-phosphate dehydrogenase from bacteria and its taxonomic importance
Purified glucose-6-phosphate dehydrogenase from Zymomonas mobilis was examined with respect to inhibition by phosphoenolpyruvate, ADP and ATP. Its molecular weight was 260,000 and the kinetics of substrate conversion indicated a random bi bi mechanism. This enzyme and the dehydrogenases from Z. anae...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1978 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Biochemical Systematics and Ecology - Amsterdam : Elsevier, 6(1978), 3, Seite 149-155 |
| Übergeordnetes Werk: |
volume:6 ; year:1978 ; number:3 ; pages:149-155 |
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| 520 | |a Purified glucose-6-phosphate dehydrogenase from Zymomonas mobilis was examined with respect to inhibition by phosphoenolpyruvate, ADP and ATP. Its molecular weight was 260,000 and the kinetics of substrate conversion indicated a random bi bi mechanism. This enzyme and the dehydrogenases from Z. anaerobia, Azotobacter chroococcum, A. vinelandii, and ''Corynebacterium'' autotrophicum strain 19/-/x were found to be allosterically inhibited by phosphoenolpyruvate, while those from several coryneform bacteria and from Escherichia coli or Pseudomonas fluorescens were not. | ||
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(DE-627)NLEJ187232881 (DE-599)GBVNLZ187232881 DE-627 ger DE-627 rakwb eng Allosteric inhibition by phosphoenolpyruvate of glucose-6-phosphate dehydrogenase from bacteria and its taxonomic importance 1978 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Purified glucose-6-phosphate dehydrogenase from Zymomonas mobilis was examined with respect to inhibition by phosphoenolpyruvate, ADP and ATP. Its molecular weight was 260,000 and the kinetics of substrate conversion indicated a random bi bi mechanism. This enzyme and the dehydrogenases from Z. anaerobia, Azotobacter chroococcum, A. vinelandii, and ''Corynebacterium'' autotrophicum strain 19/-/x were found to be allosterically inhibited by phosphoenolpyruvate, while those from several coryneform bacteria and from Escherichia coli or Pseudomonas fluorescens were not. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Opitz, R. oth Schlegel, H.G. oth in Biochemical Systematics and Ecology Amsterdam : Elsevier 6(1978), 3, Seite 149-155 (DE-627)NLEJ185648193 (DE-600)1499902-X 0305-1978 nnns volume:6 year:1978 number:3 pages:149-155 http://linkinghub.elsevier.com/retrieve/pii/0305-1978(78)90001-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 6 1978 3 149-155 |
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(DE-627)NLEJ187232881 (DE-599)GBVNLZ187232881 DE-627 ger DE-627 rakwb eng Allosteric inhibition by phosphoenolpyruvate of glucose-6-phosphate dehydrogenase from bacteria and its taxonomic importance 1978 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Purified glucose-6-phosphate dehydrogenase from Zymomonas mobilis was examined with respect to inhibition by phosphoenolpyruvate, ADP and ATP. Its molecular weight was 260,000 and the kinetics of substrate conversion indicated a random bi bi mechanism. This enzyme and the dehydrogenases from Z. anaerobia, Azotobacter chroococcum, A. vinelandii, and ''Corynebacterium'' autotrophicum strain 19/-/x were found to be allosterically inhibited by phosphoenolpyruvate, while those from several coryneform bacteria and from Escherichia coli or Pseudomonas fluorescens were not. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Opitz, R. oth Schlegel, H.G. oth in Biochemical Systematics and Ecology Amsterdam : Elsevier 6(1978), 3, Seite 149-155 (DE-627)NLEJ185648193 (DE-600)1499902-X 0305-1978 nnns volume:6 year:1978 number:3 pages:149-155 http://linkinghub.elsevier.com/retrieve/pii/0305-1978(78)90001-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 6 1978 3 149-155 |
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(DE-627)NLEJ187232881 (DE-599)GBVNLZ187232881 DE-627 ger DE-627 rakwb eng Allosteric inhibition by phosphoenolpyruvate of glucose-6-phosphate dehydrogenase from bacteria and its taxonomic importance 1978 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Purified glucose-6-phosphate dehydrogenase from Zymomonas mobilis was examined with respect to inhibition by phosphoenolpyruvate, ADP and ATP. Its molecular weight was 260,000 and the kinetics of substrate conversion indicated a random bi bi mechanism. This enzyme and the dehydrogenases from Z. anaerobia, Azotobacter chroococcum, A. vinelandii, and ''Corynebacterium'' autotrophicum strain 19/-/x were found to be allosterically inhibited by phosphoenolpyruvate, while those from several coryneform bacteria and from Escherichia coli or Pseudomonas fluorescens were not. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Opitz, R. oth Schlegel, H.G. oth in Biochemical Systematics and Ecology Amsterdam : Elsevier 6(1978), 3, Seite 149-155 (DE-627)NLEJ185648193 (DE-600)1499902-X 0305-1978 nnns volume:6 year:1978 number:3 pages:149-155 http://linkinghub.elsevier.com/retrieve/pii/0305-1978(78)90001-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 6 1978 3 149-155 |
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(DE-627)NLEJ187232881 (DE-599)GBVNLZ187232881 DE-627 ger DE-627 rakwb eng Allosteric inhibition by phosphoenolpyruvate of glucose-6-phosphate dehydrogenase from bacteria and its taxonomic importance 1978 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Purified glucose-6-phosphate dehydrogenase from Zymomonas mobilis was examined with respect to inhibition by phosphoenolpyruvate, ADP and ATP. Its molecular weight was 260,000 and the kinetics of substrate conversion indicated a random bi bi mechanism. This enzyme and the dehydrogenases from Z. anaerobia, Azotobacter chroococcum, A. vinelandii, and ''Corynebacterium'' autotrophicum strain 19/-/x were found to be allosterically inhibited by phosphoenolpyruvate, while those from several coryneform bacteria and from Escherichia coli or Pseudomonas fluorescens were not. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Opitz, R. oth Schlegel, H.G. oth in Biochemical Systematics and Ecology Amsterdam : Elsevier 6(1978), 3, Seite 149-155 (DE-627)NLEJ185648193 (DE-600)1499902-X 0305-1978 nnns volume:6 year:1978 number:3 pages:149-155 http://linkinghub.elsevier.com/retrieve/pii/0305-1978(78)90001-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 6 1978 3 149-155 |
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(DE-627)NLEJ187232881 (DE-599)GBVNLZ187232881 DE-627 ger DE-627 rakwb eng Allosteric inhibition by phosphoenolpyruvate of glucose-6-phosphate dehydrogenase from bacteria and its taxonomic importance 1978 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Purified glucose-6-phosphate dehydrogenase from Zymomonas mobilis was examined with respect to inhibition by phosphoenolpyruvate, ADP and ATP. Its molecular weight was 260,000 and the kinetics of substrate conversion indicated a random bi bi mechanism. This enzyme and the dehydrogenases from Z. anaerobia, Azotobacter chroococcum, A. vinelandii, and ''Corynebacterium'' autotrophicum strain 19/-/x were found to be allosterically inhibited by phosphoenolpyruvate, while those from several coryneform bacteria and from Escherichia coli or Pseudomonas fluorescens were not. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Opitz, R. oth Schlegel, H.G. oth in Biochemical Systematics and Ecology Amsterdam : Elsevier 6(1978), 3, Seite 149-155 (DE-627)NLEJ185648193 (DE-600)1499902-X 0305-1978 nnns volume:6 year:1978 number:3 pages:149-155 http://linkinghub.elsevier.com/retrieve/pii/0305-1978(78)90001-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 6 1978 3 149-155 |
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Allosteric inhibition by phosphoenolpyruvate of glucose-6-phosphate dehydrogenase from bacteria and its taxonomic importance |
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Purified glucose-6-phosphate dehydrogenase from Zymomonas mobilis was examined with respect to inhibition by phosphoenolpyruvate, ADP and ATP. Its molecular weight was 260,000 and the kinetics of substrate conversion indicated a random bi bi mechanism. This enzyme and the dehydrogenases from Z. anaerobia, Azotobacter chroococcum, A. vinelandii, and ''Corynebacterium'' autotrophicum strain 19/-/x were found to be allosterically inhibited by phosphoenolpyruvate, while those from several coryneform bacteria and from Escherichia coli or Pseudomonas fluorescens were not. |
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Purified glucose-6-phosphate dehydrogenase from Zymomonas mobilis was examined with respect to inhibition by phosphoenolpyruvate, ADP and ATP. Its molecular weight was 260,000 and the kinetics of substrate conversion indicated a random bi bi mechanism. This enzyme and the dehydrogenases from Z. anaerobia, Azotobacter chroococcum, A. vinelandii, and ''Corynebacterium'' autotrophicum strain 19/-/x were found to be allosterically inhibited by phosphoenolpyruvate, while those from several coryneform bacteria and from Escherichia coli or Pseudomonas fluorescens were not. |
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Purified glucose-6-phosphate dehydrogenase from Zymomonas mobilis was examined with respect to inhibition by phosphoenolpyruvate, ADP and ATP. Its molecular weight was 260,000 and the kinetics of substrate conversion indicated a random bi bi mechanism. This enzyme and the dehydrogenases from Z. anaerobia, Azotobacter chroococcum, A. vinelandii, and ''Corynebacterium'' autotrophicum strain 19/-/x were found to be allosterically inhibited by phosphoenolpyruvate, while those from several coryneform bacteria and from Escherichia coli or Pseudomonas fluorescens were not. |
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