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Re-assessment of ammonium-ion affinities of NADP-specific glutamate dehydrogenases. Activation of the Neurospora crassa enzyme by ammonium and rubidium ions
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Zeitschriftentitel: | Biochemical Journal |
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Personen und Körperschaften: | |
In: | Biochemical Journal, 209, 1983, 2, S. 527-531 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
Portland Press Ltd.
|
Schlagwörter: |
author_facet |
Wootton, J C Wootton, J C |
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author |
Wootton, J C |
spellingShingle |
Wootton, J C Biochemical Journal Re-assessment of ammonium-ion affinities of NADP-specific glutamate dehydrogenases. Activation of the Neurospora crassa enzyme by ammonium and rubidium ions Cell Biology Molecular Biology Biochemistry |
author_sort |
wootton, j c |
spelling |
Wootton, J C 0264-6021 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1042/bj2090527 <jats:p>The NADP-specific glutamate dehydrogenase of Neurospora crassa shows complex interactions with NH4+ ions, characterized by biphasic downwardly convex double-reciprocal plots. These kinetics are explained by the action of NH4+ both as a substrate and, acting at a separate cation-binding site, as an activator. Rb+ ions, and to a smaller extent other univalent cations, also activate by acting as analogues of NH4+. Previous failure to recognize this effect, which probably also occurs in homologous enzymes from some other species, has led to significant overestimates in published reports of the Km for NH4+ of some NADP-specific glutamate dehydrogenases.</jats:p> Re-assessment of ammonium-ion affinities of NADP-specific glutamate dehydrogenases. Activation of the Neurospora crassa enzyme by ammonium and rubidium ions Biochemical Journal |
doi_str_mv |
10.1042/bj2090527 |
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Online Free |
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Biologie Chemie und Pharmazie |
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Portland Press Ltd., 1983 |
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Portland Press Ltd., 1983 |
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0264-6021 |
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1983 |
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Portland Press Ltd. |
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series |
Biochemical Journal |
source_id |
49 |
title |
Re-assessment of ammonium-ion affinities of NADP-specific glutamate dehydrogenases. Activation of the Neurospora crassa enzyme by ammonium and rubidium ions |
title_unstemmed |
Re-assessment of ammonium-ion affinities of NADP-specific glutamate dehydrogenases. Activation of the Neurospora crassa enzyme by ammonium and rubidium ions |
title_full |
Re-assessment of ammonium-ion affinities of NADP-specific glutamate dehydrogenases. Activation of the Neurospora crassa enzyme by ammonium and rubidium ions |
title_fullStr |
Re-assessment of ammonium-ion affinities of NADP-specific glutamate dehydrogenases. Activation of the Neurospora crassa enzyme by ammonium and rubidium ions |
title_full_unstemmed |
Re-assessment of ammonium-ion affinities of NADP-specific glutamate dehydrogenases. Activation of the Neurospora crassa enzyme by ammonium and rubidium ions |
title_short |
Re-assessment of ammonium-ion affinities of NADP-specific glutamate dehydrogenases. Activation of the Neurospora crassa enzyme by ammonium and rubidium ions |
title_sort |
re-assessment of ammonium-ion affinities of nadp-specific glutamate dehydrogenases. activation of the neurospora crassa enzyme by ammonium and rubidium ions |
topic |
Cell Biology Molecular Biology Biochemistry |
url |
http://dx.doi.org/10.1042/bj2090527 |
publishDate |
1983 |
physical |
527-531 |
description |
<jats:p>The NADP-specific glutamate dehydrogenase of Neurospora crassa shows complex interactions with NH4+ ions, characterized by biphasic downwardly convex double-reciprocal plots. These kinetics are explained by the action of NH4+ both as a substrate and, acting at a separate cation-binding site, as an activator. Rb+ ions, and to a smaller extent other univalent cations, also activate by acting as analogues of NH4+. Previous failure to recognize this effect, which probably also occurs in homologous enzymes from some other species, has led to significant overestimates in published reports of the Km for NH4+ of some NADP-specific glutamate dehydrogenases.</jats:p> |
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author | Wootton, J C |
author_facet | Wootton, J C, Wootton, J C |
author_sort | wootton, j c |
container_issue | 2 |
container_start_page | 527 |
container_title | Biochemical Journal |
container_volume | 209 |
description | <jats:p>The NADP-specific glutamate dehydrogenase of Neurospora crassa shows complex interactions with NH4+ ions, characterized by biphasic downwardly convex double-reciprocal plots. These kinetics are explained by the action of NH4+ both as a substrate and, acting at a separate cation-binding site, as an activator. Rb+ ions, and to a smaller extent other univalent cations, also activate by acting as analogues of NH4+. Previous failure to recognize this effect, which probably also occurs in homologous enzymes from some other species, has led to significant overestimates in published reports of the Km for NH4+ of some NADP-specific glutamate dehydrogenases.</jats:p> |
doi_str_mv | 10.1042/bj2090527 |
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id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA0Mi9iajIwOTA1Mjc |
imprint | Portland Press Ltd., 1983 |
imprint_str_mv | Portland Press Ltd., 1983 |
institution | DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Zi4, DE-Gla1, DE-15, DE-Pl11, DE-Rs1, DE-14, DE-105, DE-Ch1, DE-L229 |
issn | 0264-6021 |
issn_str_mv | 0264-6021 |
language | English |
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match_str | wootton1983reassessmentofammoniumionaffinitiesofnadpspecificglutamatedehydrogenasesactivationoftheneurosporacrassaenzymebyammoniumandrubidiumions |
mega_collection | Portland Press Ltd. (CrossRef) |
physical | 527-531 |
publishDate | 1983 |
publishDateSort | 1983 |
publisher | Portland Press Ltd. |
record_format | ai |
recordtype | ai |
series | Biochemical Journal |
source_id | 49 |
spelling | Wootton, J C 0264-6021 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1042/bj2090527 <jats:p>The NADP-specific glutamate dehydrogenase of Neurospora crassa shows complex interactions with NH4+ ions, characterized by biphasic downwardly convex double-reciprocal plots. These kinetics are explained by the action of NH4+ both as a substrate and, acting at a separate cation-binding site, as an activator. Rb+ ions, and to a smaller extent other univalent cations, also activate by acting as analogues of NH4+. Previous failure to recognize this effect, which probably also occurs in homologous enzymes from some other species, has led to significant overestimates in published reports of the Km for NH4+ of some NADP-specific glutamate dehydrogenases.</jats:p> Re-assessment of ammonium-ion affinities of NADP-specific glutamate dehydrogenases. Activation of the Neurospora crassa enzyme by ammonium and rubidium ions Biochemical Journal |
spellingShingle | Wootton, J C, Biochemical Journal, Re-assessment of ammonium-ion affinities of NADP-specific glutamate dehydrogenases. Activation of the Neurospora crassa enzyme by ammonium and rubidium ions, Cell Biology, Molecular Biology, Biochemistry |
title | Re-assessment of ammonium-ion affinities of NADP-specific glutamate dehydrogenases. Activation of the Neurospora crassa enzyme by ammonium and rubidium ions |
title_full | Re-assessment of ammonium-ion affinities of NADP-specific glutamate dehydrogenases. Activation of the Neurospora crassa enzyme by ammonium and rubidium ions |
title_fullStr | Re-assessment of ammonium-ion affinities of NADP-specific glutamate dehydrogenases. Activation of the Neurospora crassa enzyme by ammonium and rubidium ions |
title_full_unstemmed | Re-assessment of ammonium-ion affinities of NADP-specific glutamate dehydrogenases. Activation of the Neurospora crassa enzyme by ammonium and rubidium ions |
title_short | Re-assessment of ammonium-ion affinities of NADP-specific glutamate dehydrogenases. Activation of the Neurospora crassa enzyme by ammonium and rubidium ions |
title_sort | re-assessment of ammonium-ion affinities of nadp-specific glutamate dehydrogenases. activation of the neurospora crassa enzyme by ammonium and rubidium ions |
title_unstemmed | Re-assessment of ammonium-ion affinities of NADP-specific glutamate dehydrogenases. Activation of the Neurospora crassa enzyme by ammonium and rubidium ions |
topic | Cell Biology, Molecular Biology, Biochemistry |
url | http://dx.doi.org/10.1042/bj2090527 |