These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Inactivation of adenylate cyclase by phenylglyoxal and other dicarbonyls. Evidence for existence of essential arginyl residues.
    Author: Franks DJ, Tunnicliff G, Ngo TT.
    Journal: Biochim Biophys Acta; 1980 Feb 14; 611(2):358-62. PubMed ID: 7357013.
    Abstract:
    Rat brain adenylate cyclase (ATP pyrophosphate-lyase (cyclizing), EC 4.6.1.1) activity was markedly reduced when the enzyme was preincubated at 23 degrees C for periods up to 30 min with phenylglyoxyal (2.5-20 mM), an agent that binds specifically to arinyl residues. The kinetics indicated the interaction of phenylgloxal with one arginyl residue was responsible for the inactivation. Protection of inactivation of the enzyme by phenylglyoxal was attained in the presence of ATP and to a lesser extent by ADP and 5'-AMP but not by cyclic-AMP or Mg2+. In addition, 2,3-butanedione and 1,2-hexanedione, compounds that also react with arginyl residues, each inactivated adenylate cyclase to varying degrees. Furthermore, this inactivation was enhanced in the presence of borate ions. These observations strongly suggest that brain adenylate cyclase possesses essential arginyl residues.
    [Abstract] [Full Text] [Related] [New Search]