Conformations of purine ribosyl 5'-nucleotides bound to glycogen phosphorylase b. A proton T2 relaxation time investigation.

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  • Author(s): Morange M; Kolb A; Buc H; Chachaty C; Langlet G
  • Source:
    European journal of biochemistry [Eur J Biochem] 1977 Mar 15; Vol. 74 (1), pp. 99-106.
  • Publication Type:
    Journal Article
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID: 0107600 Publication Model: Print Cited Medium: Print ISSN: 0014-2956 (Print) Linking ISSN: 00142956 NLM ISO Abbreviation: Eur J Biochem Subsets: MEDLINE
    • Publication Information:
      Publication: -2004: Oxford, UK : Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
      Original Publication: Berlin, New York, Springer.
    • Subject Terms:
    • Abstract:
      The conformation of 5'-nucleotides in the active site of glycogen phosphorylase b has been deduced from linewidth measurements of protons H-1', H-8 and H-2. It is shown by selective deuteration of the purine ring in position 8 that the orientation of the base is anti in the case of strong activators like AMP and syn in that of weak activators like IMP. The orientation correlation time of the nucleotides in the active site is nearly that of the enzyme, i.e. 160 ns at 21 degrees C.
    • Accession Number:
      0 (Inosine Nucleotides)
      415SHH325A (Adenosine Monophosphate)
      EC 2.4.1.- (Phosphorylases)
    • Publication Date:
      Date Created: 19770315 Date Completed: 19770611 Latest Revision: 20190620
    • Publication Date:
      20231215
    • Accession Number:
      10.1111/j.1432-1033.1977.tb11371.x
    • Accession Number:
      856577