The C1 homodimer of adenylyl cyclase binds nucleotides with high affinity but possesses exceedingly low catalytic activity

@article{Suryanarayana2009TheCH,
  title={The C1 homodimer of adenylyl cyclase binds nucleotides with high affinity but possesses exceedingly low catalytic activity},
  author={Srividya Suryanarayana and Cibele Secundino Pinto and Tung-Chung Mou and Mark Richter and Roland Seifert},
  journal={Neuroscience Letters},
  year={2009},
  volume={467},
  pages={1-5}
}
Membranous adenylyl cyclase (AC) subtypes play differential roles in the regulation of cell functions. The C1- and C2-subunits of AC form a heterodimer that efficiently catalyzes cAMP formation and constitutes a very useful model system for AC analysis at a molecular level. Intriguingly, C1 and C2 homodimers exist, too. The C2 homodimer is catalytically inactive and possesses two forskolin binding sites. However, little is known about the C1 homodimer. Therefore, in this study, we examined the… CONTINUE READING
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