Phosphoenolpyruvate, a new inhibitor of glucose-6-phosphate dehydrogenase
Using partially purified preparations of glucose-6-phosphate dehydrogenase from the hydrogen-bacterium Arthrobacter 7C, a new inhibitor of the enzyme has been characterized, phosphoenolpyruvate (PEP). PEP increases the sigmoidicity of the substrate (G-6-P)-saturation curve, displaying an apparent K&...
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| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1972 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Biochemical and Biophysical Research Communications - Amsterdam : Elsevier, 49(1972), 6, Seite 1554-1560 |
| Übergeordnetes Werk: |
volume:49 ; year:1972 ; number:6 ; pages:1554-1560 |
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| 520 | |a Using partially purified preparations of glucose-6-phosphate dehydrogenase from the hydrogen-bacterium Arthrobacter 7C, a new inhibitor of the enzyme has been characterized, phosphoenolpyruvate (PEP). PEP increases the sigmoidicity of the substrate (G-6-P)-saturation curve, displaying an apparent K"i-value of 0.05 mM at an 0.5 mM glucose-6-phosphate concentration, and acts as negative allosteric inhibitor. This enzyme is not subject to allosteric inhibition by ATP. The enzyme from Hydrogenomonas eutropha H 16 is inhibited in an allosteric fashion by ATP as well as by PEP. It is suggested that PEP may function as a general regulator for glucose-6-phosphate dehydrogenase of some of those organisms which depend on this enzyme for hexose catabolism. | ||
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(DE-627)NLEJ184207495 (DE-599)GBVNLZ184207495 DE-627 ger DE-627 rakwb eng Phosphoenolpyruvate, a new inhibitor of glucose-6-phosphate dehydrogenase 1972 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Using partially purified preparations of glucose-6-phosphate dehydrogenase from the hydrogen-bacterium Arthrobacter 7C, a new inhibitor of the enzyme has been characterized, phosphoenolpyruvate (PEP). PEP increases the sigmoidicity of the substrate (G-6-P)-saturation curve, displaying an apparent K"i-value of 0.05 mM at an 0.5 mM glucose-6-phosphate concentration, and acts as negative allosteric inhibitor. This enzyme is not subject to allosteric inhibition by ATP. The enzyme from Hydrogenomonas eutropha H 16 is inhibited in an allosteric fashion by ATP as well as by PEP. It is suggested that PEP may function as a general regulator for glucose-6-phosphate dehydrogenase of some of those organisms which depend on this enzyme for hexose catabolism. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Tunail, N. oth Schlegel, H.G. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 49(1972), 6, Seite 1554-1560 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:49 year:1972 number:6 pages:1554-1560 http://dx.doi.org/10.1016/0006-291X(72)90518-9 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 49 1972 6 1554-1560 |
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(DE-627)NLEJ184207495 (DE-599)GBVNLZ184207495 DE-627 ger DE-627 rakwb eng Phosphoenolpyruvate, a new inhibitor of glucose-6-phosphate dehydrogenase 1972 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Using partially purified preparations of glucose-6-phosphate dehydrogenase from the hydrogen-bacterium Arthrobacter 7C, a new inhibitor of the enzyme has been characterized, phosphoenolpyruvate (PEP). PEP increases the sigmoidicity of the substrate (G-6-P)-saturation curve, displaying an apparent K"i-value of 0.05 mM at an 0.5 mM glucose-6-phosphate concentration, and acts as negative allosteric inhibitor. This enzyme is not subject to allosteric inhibition by ATP. The enzyme from Hydrogenomonas eutropha H 16 is inhibited in an allosteric fashion by ATP as well as by PEP. It is suggested that PEP may function as a general regulator for glucose-6-phosphate dehydrogenase of some of those organisms which depend on this enzyme for hexose catabolism. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Tunail, N. oth Schlegel, H.G. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 49(1972), 6, Seite 1554-1560 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:49 year:1972 number:6 pages:1554-1560 http://dx.doi.org/10.1016/0006-291X(72)90518-9 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 49 1972 6 1554-1560 |
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(DE-627)NLEJ184207495 (DE-599)GBVNLZ184207495 DE-627 ger DE-627 rakwb eng Phosphoenolpyruvate, a new inhibitor of glucose-6-phosphate dehydrogenase 1972 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Using partially purified preparations of glucose-6-phosphate dehydrogenase from the hydrogen-bacterium Arthrobacter 7C, a new inhibitor of the enzyme has been characterized, phosphoenolpyruvate (PEP). PEP increases the sigmoidicity of the substrate (G-6-P)-saturation curve, displaying an apparent K"i-value of 0.05 mM at an 0.5 mM glucose-6-phosphate concentration, and acts as negative allosteric inhibitor. This enzyme is not subject to allosteric inhibition by ATP. The enzyme from Hydrogenomonas eutropha H 16 is inhibited in an allosteric fashion by ATP as well as by PEP. It is suggested that PEP may function as a general regulator for glucose-6-phosphate dehydrogenase of some of those organisms which depend on this enzyme for hexose catabolism. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Tunail, N. oth Schlegel, H.G. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 49(1972), 6, Seite 1554-1560 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:49 year:1972 number:6 pages:1554-1560 http://dx.doi.org/10.1016/0006-291X(72)90518-9 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 49 1972 6 1554-1560 |
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(DE-627)NLEJ184207495 (DE-599)GBVNLZ184207495 DE-627 ger DE-627 rakwb eng Phosphoenolpyruvate, a new inhibitor of glucose-6-phosphate dehydrogenase 1972 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Using partially purified preparations of glucose-6-phosphate dehydrogenase from the hydrogen-bacterium Arthrobacter 7C, a new inhibitor of the enzyme has been characterized, phosphoenolpyruvate (PEP). PEP increases the sigmoidicity of the substrate (G-6-P)-saturation curve, displaying an apparent K"i-value of 0.05 mM at an 0.5 mM glucose-6-phosphate concentration, and acts as negative allosteric inhibitor. This enzyme is not subject to allosteric inhibition by ATP. The enzyme from Hydrogenomonas eutropha H 16 is inhibited in an allosteric fashion by ATP as well as by PEP. It is suggested that PEP may function as a general regulator for glucose-6-phosphate dehydrogenase of some of those organisms which depend on this enzyme for hexose catabolism. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Tunail, N. oth Schlegel, H.G. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 49(1972), 6, Seite 1554-1560 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:49 year:1972 number:6 pages:1554-1560 http://dx.doi.org/10.1016/0006-291X(72)90518-9 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 49 1972 6 1554-1560 |
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(DE-627)NLEJ184207495 (DE-599)GBVNLZ184207495 DE-627 ger DE-627 rakwb eng Phosphoenolpyruvate, a new inhibitor of glucose-6-phosphate dehydrogenase 1972 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Using partially purified preparations of glucose-6-phosphate dehydrogenase from the hydrogen-bacterium Arthrobacter 7C, a new inhibitor of the enzyme has been characterized, phosphoenolpyruvate (PEP). PEP increases the sigmoidicity of the substrate (G-6-P)-saturation curve, displaying an apparent K"i-value of 0.05 mM at an 0.5 mM glucose-6-phosphate concentration, and acts as negative allosteric inhibitor. This enzyme is not subject to allosteric inhibition by ATP. The enzyme from Hydrogenomonas eutropha H 16 is inhibited in an allosteric fashion by ATP as well as by PEP. It is suggested that PEP may function as a general regulator for glucose-6-phosphate dehydrogenase of some of those organisms which depend on this enzyme for hexose catabolism. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Tunail, N. oth Schlegel, H.G. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 49(1972), 6, Seite 1554-1560 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:49 year:1972 number:6 pages:1554-1560 http://dx.doi.org/10.1016/0006-291X(72)90518-9 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 49 1972 6 1554-1560 |
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Phosphoenolpyruvate, a new inhibitor of glucose-6-phosphate dehydrogenase |
| abstract |
Using partially purified preparations of glucose-6-phosphate dehydrogenase from the hydrogen-bacterium Arthrobacter 7C, a new inhibitor of the enzyme has been characterized, phosphoenolpyruvate (PEP). PEP increases the sigmoidicity of the substrate (G-6-P)-saturation curve, displaying an apparent K"i-value of 0.05 mM at an 0.5 mM glucose-6-phosphate concentration, and acts as negative allosteric inhibitor. This enzyme is not subject to allosteric inhibition by ATP. The enzyme from Hydrogenomonas eutropha H 16 is inhibited in an allosteric fashion by ATP as well as by PEP. It is suggested that PEP may function as a general regulator for glucose-6-phosphate dehydrogenase of some of those organisms which depend on this enzyme for hexose catabolism. |
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Using partially purified preparations of glucose-6-phosphate dehydrogenase from the hydrogen-bacterium Arthrobacter 7C, a new inhibitor of the enzyme has been characterized, phosphoenolpyruvate (PEP). PEP increases the sigmoidicity of the substrate (G-6-P)-saturation curve, displaying an apparent K"i-value of 0.05 mM at an 0.5 mM glucose-6-phosphate concentration, and acts as negative allosteric inhibitor. This enzyme is not subject to allosteric inhibition by ATP. The enzyme from Hydrogenomonas eutropha H 16 is inhibited in an allosteric fashion by ATP as well as by PEP. It is suggested that PEP may function as a general regulator for glucose-6-phosphate dehydrogenase of some of those organisms which depend on this enzyme for hexose catabolism. |
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Using partially purified preparations of glucose-6-phosphate dehydrogenase from the hydrogen-bacterium Arthrobacter 7C, a new inhibitor of the enzyme has been characterized, phosphoenolpyruvate (PEP). PEP increases the sigmoidicity of the substrate (G-6-P)-saturation curve, displaying an apparent K"i-value of 0.05 mM at an 0.5 mM glucose-6-phosphate concentration, and acts as negative allosteric inhibitor. This enzyme is not subject to allosteric inhibition by ATP. The enzyme from Hydrogenomonas eutropha H 16 is inhibited in an allosteric fashion by ATP as well as by PEP. It is suggested that PEP may function as a general regulator for glucose-6-phosphate dehydrogenase of some of those organisms which depend on this enzyme for hexose catabolism. |
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