HYPOTHESIS CONCERNING STRUCTURE OF CAMP-DEPENDENT AND CGMP-DEPENDENT PROTEIN-KINASES
- 1 January 1977
- journal article
- research article
- Vol. 3 (3) , 153-162
Abstract
C[cyclic]AMP- and cGMP-dependent protein kinases were purified from mammalian and non-mammalian sources. Each enzyme demonstrated high specificity and affinity for the cyclic nucleotide with binding of 2 mol of nucleotide per holoenzyme and each enzyme was an ATP:phosphotransferase. The holoenzymes have similar MW and demonstrated similar molecular asymmetry. A structural model relating the 2 enzymes was proposed. cGMP-dependent protein kinase was proposed to be a dimer composed of 2 identical protomers in isologous association with the chains arranged in anti-parallel fashion. cAMP-dependent protein kinase was proposed to have a similar structure with a dyad axis of symmetry but with a discontinuity in each chain. These structures account for the differing mechanisms of cyclic nucleotide activation of the 2 enzymes.This publication has 16 references indexed in Scilit:
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