Literature DB >> 1066682

1,N6-etheno-AMP and 1,N6-etheno-2'-deoxy-AMP as probes of the activator site of glycogen phosphorylase from rabbit skeletal muscle.

B Vandenbunder, M Morange, H Buc.   

Abstract

Both 1,N6-etheno-AMP and 1,N6-etheno-2'-deoxy-AMP bind at the AMP site of phosphorylase b (1,4-alpha-D-glucan:orthophosphate alpha-glucosyltransferase, EC 2.4.1.1). Etheno-AMP induces the same activation as AMP, about 30-fold higher than the activation induced by etheno-dAMP. The fluorescence of etheno-AMP and etheno-dAMP is associated with the base moiety; therefore, when free in solution, the two derivatives have identical fluorescence properties. However, when bound to phosphorylase, the fluorescence of etheno-AMP is quenched more efficiently than the fluorescence of etheno-dAMP. This difference between the fluorescence properties of the bound nucleotides suggests that a modification in the ribose ring affects the position of the adenine in the AMP site of phosphorylase b. The observed quenching may be due to a stacking interaction between an aromatic residue and the base moiety of the bound nucleotide.

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Year:  1976        PMID： 1066682      PMCID： PMC430715          DOI： 10.1073/pnas.73.8.2696

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN： 0027-8424            Impact factor:   11.205


  10 in total

1.  PURIFICATION AND PROPERTIES OF RABBIT SKELETAL MUSCLE PHOSPHORYLASE B KINASE.

Authors:  E G KREBS; D S LOVE; G E BRATVOLD; K A TRAYSER; W L MEYER; E H FISCHER
Journal:  Biochemistry       Date:  1964-08       Impact factor: 3.162

2.  THE ROLE OF ADENYLIC ACID IN THE ACTIVATION OF PHOSPHORYLASE.

Authors:  E HELMREICH; C F CORI
Journal:  Proc Natl Acad Sci U S A       Date:  1964-01       Impact factor: 11.205

3.  The interaction of ribonuclease with purine and pyrimidine phosphates. I. Binding of adenosine 5'-monophosphate to ribonuclease.

Authors:  Y P MYER; J A SCHELLMAN
Journal:  Biochim Biophys Acta       Date:  1962-03-05

4.  AMP analogs: their function in the activation of glycogen phosphorylase b.

Authors:  M Morange; F G Blanco; B Vandenbunder; H Buc
Journal:  Eur J Biochem       Date:  1976-06-01

5.  Fluorescent modification of adenosine-containing coenzymes. Biological activities and spectroscopic properties.

Authors:  J A Secrist; J R Barrio; N J Leonard; G Weber
Journal:  Biochemistry       Date:  1972-09-12       Impact factor: 3.162

6.  Probes for the conformational transitions of phosphorylase b. Effect of ligands studied by proton relaxation enhancement, fluorescence and chemical reactivities.

Authors:  D J Birkett; R A Dwek; G K Radda; R E Richards; A G Salmon
Journal:  Eur J Biochem       Date:  1971-06-29

7.  The activity of -adenosine derivatives as allosteric modifiers of phosphorylase b.

Authors:  R F Steiner
Journal:  FEBS Lett       Date:  1972-06-15       Impact factor: 4.124

8.  Studies on the allosteric activation of glycogen phosphorylase b by Nucleotides. I. Activation of phosphorylase b by inosine monophosphate.

Authors:  W J Black; J H Wang
Journal:  J Biol Chem       Date:  1968-11-25       Impact factor: 5.157

9.  Studies on the interaction between regulatory enzymes and effectors. II. Effect of adenosine 5'-monophosphate analogues on glycogen phosphorylase B.

Authors:  T Okazaki; A Nakazawa; O Hayaishi
Journal:  J Biol Chem       Date:  1968-10-25       Impact factor: 5.157

10.  Dynamic and static quenching of 1,N6-ethenoadenine fluorescence in nicotinamide 1,N6-ethenoadenine dinucleotide and in 1,N6-etheno-9-(3-(indol-3-yl) propyl) adenine.

Authors:  B A Gruber; N J Leonard
Journal:  Proc Natl Acad Sci U S A       Date:  1975-10       Impact factor: 11.205
  10 in total

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