Conservation, evolution, and specificity in cellular control by protein phosphorylation
Abstract The glycolytic control enzyme phosphofructokinase from the parasitic nematodeAscaris lumbricodies is regulated by reversible phosphorylation. The enzyme is phosphorylated by an atypical cyclic adenosine monophosphate (cAMP)-dependent protein kinase whose substrate specificity deviates from...
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| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1996 |
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| Umfang: |
6 |
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| Reproduktion: |
Springer Online Journal Archives 1860-2002 |
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| Übergeordnetes Werk: |
in: Cellular and molecular life sciences - 1945, 52(1996) vom: Mai, Seite 449-454 |
| Übergeordnetes Werk: |
volume:52 ; year:1996 ; month:05 ; pages:449-454 ; extent:6 |
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| 520 | |a Abstract The glycolytic control enzyme phosphofructokinase from the parasitic nematodeAscaris lumbricodies is regulated by reversible phosphorylation. The enzyme is phosphorylated by an atypical cyclic adenosine monophosphate (cAMP)-dependent protein kinase whose substrate specificity deviates from that of the mammalian protein kinase. This variation is explained by structural peculiarities on the surface part of the catalytic groove of the protein kinase. Also, the protein phosphatases responsible for the reversal of phosphorylation appear to act specifically in glycolysis and are different from those participating in regulation of glycogenolysis. | ||
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(DE-627)NLEJ18940079X DE-627 ger DE-627 rakwb eng Conservation, evolution, and specificity in cellular control by protein phosphorylation 1996 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract The glycolytic control enzyme phosphofructokinase from the parasitic nematodeAscaris lumbricodies is regulated by reversible phosphorylation. The enzyme is phosphorylated by an atypical cyclic adenosine monophosphate (cAMP)-dependent protein kinase whose substrate specificity deviates from that of the mammalian protein kinase. This variation is explained by structural peculiarities on the surface part of the catalytic groove of the protein kinase. Also, the protein phosphatases responsible for the reversal of phosphorylation appear to act specifically in glycolysis and are different from those participating in regulation of glycogenolysis. Springer Online Journal Archives 1860-2002 Hofer, H. W. oth in Cellular and molecular life sciences 1945 52(1996) vom: Mai, Seite 449-454 (DE-627)NLEJ188987495 (DE-600)1458497-9 1420-9071 nnns volume:52 year:1996 month:05 pages:449-454 extent:6 http://dx.doi.org/10.1007/BF01919314 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 52 1996 5 449-454 6 |
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(DE-627)NLEJ18940079X DE-627 ger DE-627 rakwb eng Conservation, evolution, and specificity in cellular control by protein phosphorylation 1996 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract The glycolytic control enzyme phosphofructokinase from the parasitic nematodeAscaris lumbricodies is regulated by reversible phosphorylation. The enzyme is phosphorylated by an atypical cyclic adenosine monophosphate (cAMP)-dependent protein kinase whose substrate specificity deviates from that of the mammalian protein kinase. This variation is explained by structural peculiarities on the surface part of the catalytic groove of the protein kinase. Also, the protein phosphatases responsible for the reversal of phosphorylation appear to act specifically in glycolysis and are different from those participating in regulation of glycogenolysis. Springer Online Journal Archives 1860-2002 Hofer, H. W. oth in Cellular and molecular life sciences 1945 52(1996) vom: Mai, Seite 449-454 (DE-627)NLEJ188987495 (DE-600)1458497-9 1420-9071 nnns volume:52 year:1996 month:05 pages:449-454 extent:6 http://dx.doi.org/10.1007/BF01919314 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 52 1996 5 449-454 6 |
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(DE-627)NLEJ18940079X DE-627 ger DE-627 rakwb eng Conservation, evolution, and specificity in cellular control by protein phosphorylation 1996 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract The glycolytic control enzyme phosphofructokinase from the parasitic nematodeAscaris lumbricodies is regulated by reversible phosphorylation. The enzyme is phosphorylated by an atypical cyclic adenosine monophosphate (cAMP)-dependent protein kinase whose substrate specificity deviates from that of the mammalian protein kinase. This variation is explained by structural peculiarities on the surface part of the catalytic groove of the protein kinase. Also, the protein phosphatases responsible for the reversal of phosphorylation appear to act specifically in glycolysis and are different from those participating in regulation of glycogenolysis. Springer Online Journal Archives 1860-2002 Hofer, H. W. oth in Cellular and molecular life sciences 1945 52(1996) vom: Mai, Seite 449-454 (DE-627)NLEJ188987495 (DE-600)1458497-9 1420-9071 nnns volume:52 year:1996 month:05 pages:449-454 extent:6 http://dx.doi.org/10.1007/BF01919314 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 52 1996 5 449-454 6 |
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(DE-627)NLEJ18940079X DE-627 ger DE-627 rakwb eng Conservation, evolution, and specificity in cellular control by protein phosphorylation 1996 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract The glycolytic control enzyme phosphofructokinase from the parasitic nematodeAscaris lumbricodies is regulated by reversible phosphorylation. The enzyme is phosphorylated by an atypical cyclic adenosine monophosphate (cAMP)-dependent protein kinase whose substrate specificity deviates from that of the mammalian protein kinase. This variation is explained by structural peculiarities on the surface part of the catalytic groove of the protein kinase. Also, the protein phosphatases responsible for the reversal of phosphorylation appear to act specifically in glycolysis and are different from those participating in regulation of glycogenolysis. Springer Online Journal Archives 1860-2002 Hofer, H. W. oth in Cellular and molecular life sciences 1945 52(1996) vom: Mai, Seite 449-454 (DE-627)NLEJ188987495 (DE-600)1458497-9 1420-9071 nnns volume:52 year:1996 month:05 pages:449-454 extent:6 http://dx.doi.org/10.1007/BF01919314 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 52 1996 5 449-454 6 |
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(DE-627)NLEJ18940079X DE-627 ger DE-627 rakwb eng Conservation, evolution, and specificity in cellular control by protein phosphorylation 1996 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract The glycolytic control enzyme phosphofructokinase from the parasitic nematodeAscaris lumbricodies is regulated by reversible phosphorylation. The enzyme is phosphorylated by an atypical cyclic adenosine monophosphate (cAMP)-dependent protein kinase whose substrate specificity deviates from that of the mammalian protein kinase. This variation is explained by structural peculiarities on the surface part of the catalytic groove of the protein kinase. Also, the protein phosphatases responsible for the reversal of phosphorylation appear to act specifically in glycolysis and are different from those participating in regulation of glycogenolysis. Springer Online Journal Archives 1860-2002 Hofer, H. W. oth in Cellular and molecular life sciences 1945 52(1996) vom: Mai, Seite 449-454 (DE-627)NLEJ188987495 (DE-600)1458497-9 1420-9071 nnns volume:52 year:1996 month:05 pages:449-454 extent:6 http://dx.doi.org/10.1007/BF01919314 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 52 1996 5 449-454 6 |
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conservation, evolution, and specificity in cellular control by protein phosphorylation |
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Conservation, evolution, and specificity in cellular control by protein phosphorylation |
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Abstract The glycolytic control enzyme phosphofructokinase from the parasitic nematodeAscaris lumbricodies is regulated by reversible phosphorylation. The enzyme is phosphorylated by an atypical cyclic adenosine monophosphate (cAMP)-dependent protein kinase whose substrate specificity deviates from that of the mammalian protein kinase. This variation is explained by structural peculiarities on the surface part of the catalytic groove of the protein kinase. Also, the protein phosphatases responsible for the reversal of phosphorylation appear to act specifically in glycolysis and are different from those participating in regulation of glycogenolysis. |
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Abstract The glycolytic control enzyme phosphofructokinase from the parasitic nematodeAscaris lumbricodies is regulated by reversible phosphorylation. The enzyme is phosphorylated by an atypical cyclic adenosine monophosphate (cAMP)-dependent protein kinase whose substrate specificity deviates from that of the mammalian protein kinase. This variation is explained by structural peculiarities on the surface part of the catalytic groove of the protein kinase. Also, the protein phosphatases responsible for the reversal of phosphorylation appear to act specifically in glycolysis and are different from those participating in regulation of glycogenolysis. |
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Abstract The glycolytic control enzyme phosphofructokinase from the parasitic nematodeAscaris lumbricodies is regulated by reversible phosphorylation. The enzyme is phosphorylated by an atypical cyclic adenosine monophosphate (cAMP)-dependent protein kinase whose substrate specificity deviates from that of the mammalian protein kinase. This variation is explained by structural peculiarities on the surface part of the catalytic groove of the protein kinase. Also, the protein phosphatases responsible for the reversal of phosphorylation appear to act specifically in glycolysis and are different from those participating in regulation of glycogenolysis. |
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