Nucleotide activation of glycogen phosphorylase b occurs only when the nucleotide phosphate is in a dianionic form
Adenosine monophosphofluoridate has been synthesised and purified to remove all contaminating AMP. This AMP analogue fails to activate glycogen phosphorylase b, even at high concentration, but inhibits the AMP activation with a Ki value of 3 mM. Activation of phosphorylase b by adenosine phosphorami...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1980 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Biochemical and Biophysical Research Communications - Amsterdam : Elsevier, 97(1980), 2, Seite 513-519 |
| Übergeordnetes Werk: |
volume:97 ; year:1980 ; number:2 ; pages:513-519 |
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| 520 | |a Adenosine monophosphofluoridate has been synthesised and purified to remove all contaminating AMP. This AMP analogue fails to activate glycogen phosphorylase b, even at high concentration, but inhibits the AMP activation with a Ki value of 3 mM. Activation of phosphorylase b by adenosine phosphoramidate has been re-investigated in the light of these findings and a purified sample of this nucleotide analogue has been shown to produce little or no activation of the enzyme. These findings are interpreted in terms of an absolute requirement of the nucleotide activatorsite in phosphorylase for a nucleotide with a dianionic phosphate. The implications of this for the role of the phosphate moiety in the proposed mechanism of activation are discussed. | ||
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(DE-627)NLEJ18423672X (DE-599)GBVNLZ18423672X DE-627 ger DE-627 rakwb eng Nucleotide activation of glycogen phosphorylase b occurs only when the nucleotide phosphate is in a dianionic form 1980 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Adenosine monophosphofluoridate has been synthesised and purified to remove all contaminating AMP. This AMP analogue fails to activate glycogen phosphorylase b, even at high concentration, but inhibits the AMP activation with a Ki value of 3 mM. Activation of phosphorylase b by adenosine phosphoramidate has been re-investigated in the light of these findings and a purified sample of this nucleotide analogue has been shown to produce little or no activation of the enzyme. These findings are interpreted in terms of an absolute requirement of the nucleotide activatorsite in phosphorylase for a nucleotide with a dianionic phosphate. The implications of this for the role of the phosphate moiety in the proposed mechanism of activation are discussed. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Withers, S.G. oth Madsen, N.B. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 97(1980), 2, Seite 513-519 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:97 year:1980 number:2 pages:513-519 http://dx.doi.org/10.1016/0006-291X(80)90293-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 97 1980 2 513-519 |
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(DE-627)NLEJ18423672X (DE-599)GBVNLZ18423672X DE-627 ger DE-627 rakwb eng Nucleotide activation of glycogen phosphorylase b occurs only when the nucleotide phosphate is in a dianionic form 1980 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Adenosine monophosphofluoridate has been synthesised and purified to remove all contaminating AMP. This AMP analogue fails to activate glycogen phosphorylase b, even at high concentration, but inhibits the AMP activation with a Ki value of 3 mM. Activation of phosphorylase b by adenosine phosphoramidate has been re-investigated in the light of these findings and a purified sample of this nucleotide analogue has been shown to produce little or no activation of the enzyme. These findings are interpreted in terms of an absolute requirement of the nucleotide activatorsite in phosphorylase for a nucleotide with a dianionic phosphate. The implications of this for the role of the phosphate moiety in the proposed mechanism of activation are discussed. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Withers, S.G. oth Madsen, N.B. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 97(1980), 2, Seite 513-519 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:97 year:1980 number:2 pages:513-519 http://dx.doi.org/10.1016/0006-291X(80)90293-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 97 1980 2 513-519 |
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(DE-627)NLEJ18423672X (DE-599)GBVNLZ18423672X DE-627 ger DE-627 rakwb eng Nucleotide activation of glycogen phosphorylase b occurs only when the nucleotide phosphate is in a dianionic form 1980 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Adenosine monophosphofluoridate has been synthesised and purified to remove all contaminating AMP. This AMP analogue fails to activate glycogen phosphorylase b, even at high concentration, but inhibits the AMP activation with a Ki value of 3 mM. Activation of phosphorylase b by adenosine phosphoramidate has been re-investigated in the light of these findings and a purified sample of this nucleotide analogue has been shown to produce little or no activation of the enzyme. These findings are interpreted in terms of an absolute requirement of the nucleotide activatorsite in phosphorylase for a nucleotide with a dianionic phosphate. The implications of this for the role of the phosphate moiety in the proposed mechanism of activation are discussed. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Withers, S.G. oth Madsen, N.B. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 97(1980), 2, Seite 513-519 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:97 year:1980 number:2 pages:513-519 http://dx.doi.org/10.1016/0006-291X(80)90293-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 97 1980 2 513-519 |
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(DE-627)NLEJ18423672X (DE-599)GBVNLZ18423672X DE-627 ger DE-627 rakwb eng Nucleotide activation of glycogen phosphorylase b occurs only when the nucleotide phosphate is in a dianionic form 1980 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Adenosine monophosphofluoridate has been synthesised and purified to remove all contaminating AMP. This AMP analogue fails to activate glycogen phosphorylase b, even at high concentration, but inhibits the AMP activation with a Ki value of 3 mM. Activation of phosphorylase b by adenosine phosphoramidate has been re-investigated in the light of these findings and a purified sample of this nucleotide analogue has been shown to produce little or no activation of the enzyme. These findings are interpreted in terms of an absolute requirement of the nucleotide activatorsite in phosphorylase for a nucleotide with a dianionic phosphate. The implications of this for the role of the phosphate moiety in the proposed mechanism of activation are discussed. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Withers, S.G. oth Madsen, N.B. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 97(1980), 2, Seite 513-519 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:97 year:1980 number:2 pages:513-519 http://dx.doi.org/10.1016/0006-291X(80)90293-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 97 1980 2 513-519 |
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(DE-627)NLEJ18423672X (DE-599)GBVNLZ18423672X DE-627 ger DE-627 rakwb eng Nucleotide activation of glycogen phosphorylase b occurs only when the nucleotide phosphate is in a dianionic form 1980 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Adenosine monophosphofluoridate has been synthesised and purified to remove all contaminating AMP. This AMP analogue fails to activate glycogen phosphorylase b, even at high concentration, but inhibits the AMP activation with a Ki value of 3 mM. Activation of phosphorylase b by adenosine phosphoramidate has been re-investigated in the light of these findings and a purified sample of this nucleotide analogue has been shown to produce little or no activation of the enzyme. These findings are interpreted in terms of an absolute requirement of the nucleotide activatorsite in phosphorylase for a nucleotide with a dianionic phosphate. The implications of this for the role of the phosphate moiety in the proposed mechanism of activation are discussed. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Withers, S.G. oth Madsen, N.B. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 97(1980), 2, Seite 513-519 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:97 year:1980 number:2 pages:513-519 http://dx.doi.org/10.1016/0006-291X(80)90293-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 97 1980 2 513-519 |
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nucleotide activation of glycogen phosphorylase b occurs only when the nucleotide phosphate is in a dianionic form |
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Nucleotide activation of glycogen phosphorylase b occurs only when the nucleotide phosphate is in a dianionic form |
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Adenosine monophosphofluoridate has been synthesised and purified to remove all contaminating AMP. This AMP analogue fails to activate glycogen phosphorylase b, even at high concentration, but inhibits the AMP activation with a Ki value of 3 mM. Activation of phosphorylase b by adenosine phosphoramidate has been re-investigated in the light of these findings and a purified sample of this nucleotide analogue has been shown to produce little or no activation of the enzyme. These findings are interpreted in terms of an absolute requirement of the nucleotide activatorsite in phosphorylase for a nucleotide with a dianionic phosphate. The implications of this for the role of the phosphate moiety in the proposed mechanism of activation are discussed. |
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Adenosine monophosphofluoridate has been synthesised and purified to remove all contaminating AMP. This AMP analogue fails to activate glycogen phosphorylase b, even at high concentration, but inhibits the AMP activation with a Ki value of 3 mM. Activation of phosphorylase b by adenosine phosphoramidate has been re-investigated in the light of these findings and a purified sample of this nucleotide analogue has been shown to produce little or no activation of the enzyme. These findings are interpreted in terms of an absolute requirement of the nucleotide activatorsite in phosphorylase for a nucleotide with a dianionic phosphate. The implications of this for the role of the phosphate moiety in the proposed mechanism of activation are discussed. |
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Adenosine monophosphofluoridate has been synthesised and purified to remove all contaminating AMP. This AMP analogue fails to activate glycogen phosphorylase b, even at high concentration, but inhibits the AMP activation with a Ki value of 3 mM. Activation of phosphorylase b by adenosine phosphoramidate has been re-investigated in the light of these findings and a purified sample of this nucleotide analogue has been shown to produce little or no activation of the enzyme. These findings are interpreted in terms of an absolute requirement of the nucleotide activatorsite in phosphorylase for a nucleotide with a dianionic phosphate. The implications of this for the role of the phosphate moiety in the proposed mechanism of activation are discussed. |
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