Abstract
Publisher Summary This chapter describes the enzyme (adenylyl cyclase) that effect the synthesis of Adenosine 3’,5’-cyclic monophosphate (cAMP) in various bacterial species. The content will rather reflect current major interests. The adenylyl cyclase from Escherichia coli has been a major subject of research interest ever since it was identified as the probable point for physiological regulation of cAMP levels in that organism and therefore a prime candidate for a protein mediator of the catabolite repression response mechanism. cAMP functions as a cytoplasmic element mediating some reactions crucial for efficient cellular function. An activity that has been found only in eukaryotic cells is the CAMP-dependent protein kinase. This enzyme is a well-known target of the action of cAMP as a second messenger, in which action this ligand transmits a signal generated by an extracellular hormone. The manner in which cAMP acts on the cAMP-dependent protein kinase involves a release of the catalytic moiety of the enzyme from a complex in which its activity is inhibited as a result of binding to a regulatory subunit.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Progress in Nucleic Acid Research and Molecular Biology
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
