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Based on the calcuation of free energy in the 13 possible methods of class III the image above is the proposed mechanism for Adenylyl cyclase form cAMP. The Mechanism is listed below:ACS [1] 10.1021-acs.biochem.5b00655Figure1 (1) — Preceding unsigned comment added by Aflores66 (talkcontribs) 14:32, 6 November 2018 (UTC) Hello, This is my sandbox for editing Adenylyl Cyclase structure as there isn't enough information on it's Wikipedia page. This is an assignment for my biochem course at Roosevelt University.[reply]

I think that the enzyme adenylyl cyclase primary structure has transmembrane regions and cytoplasmic regions. Which are already mentioned in the wikipedia article for type III to be M1 and M2 as transmembrane regions, but it doesn't update on what we know about their function. I found a source claiming that their function is not fully known, except for considering them to be transporters in theory. The cytoplasmic regions C1 and C2 are divided into C1a, C1b, C2a, and C2b. All of these parts are slightly explained in the article obviously, but I would like to add that the C1b region is the largest and contains many regulatory sites in mammalian adenylyl cyclase. I want to signify the fact that this information is about mammalian adenylyl cyclase. I am on the look out for more information to help me distinguish other types from each other. This is my source Silverhoma (talk) 04:51, 6 November 2018 (UTC)[reply]

The most well known function of adenylyl cyclase is its role in activating cyclic adenosine monophosphate (cAMP/cyclic AMP) in signal transduction pathways (specifically extracellular to intracellular via protein kinase A).[2] These pathways occur via a cascade effect where a G protein is activated and it in turn activates adenylyl cyclase which catalyzes the synthesis of the secondary messenger cAMP from ATP.[2] Cyclic AMP thereby induces a cellular response.

Adenylyl cyclase has also been indicated to have a role in “memory formation...as a coincidence detector.”[3][4][5][6] “A soluble (non-membrane bound) form of adenylyl cyclase…” was also found to be characterized in mammalian sperm where it is activated by a bicarbonate ion.[2] The final two functions listed being still in need of further research.

References

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  1. ^ Cite error: The named reference undefined was invoked but never defined (see the help page).
  2. ^ a b c "Adenylyl Cyclase". www.vivo.colostate.edu. Retrieved 2018-11-02.
  3. ^ Willoughby, Debbie; Cooper, Dermot M. F. (2007-07). "Organization and Ca2+ Regulation of Adenylyl Cyclases in cAMP Microdomains". Physiological Reviews. 87 (3): 965–1010. doi:10.1152/physrev.00049.2006. ISSN 0031-9333. {{cite journal}}: Check date values in: |date= (help)
  4. ^ Mons, N.; Guillou, J.-L.; Jaffard, R. (1999-04-01). "The role of Ca 2+ /calmodulin-stimulable adenylyl cyclases as molecular coincidence detectors in memory formation". Cellular and Molecular Life Sciences (CMLS). 55 (4): 525–533. doi:10.1007/s000180050311. ISSN 1420-682X.
  5. ^ Hanoune, Jacques; Defer, Nicole (2001-04). "REGULATION ANDROLE OFADENYLYLCYCLASEISOFORMS". Annual Review of Pharmacology and Toxicology. 41 (1): 145–174. doi:10.1146/annurev.pharmtox.41.1.145. ISSN 0362-1642. {{cite journal}}: Check date values in: |date= (help)
  6. ^ Neve, Kim A.; Seamans, Jeremy K.; Trantham-Davidson, Heather (2004-01). "Dopamine Receptor Signaling". Journal of Receptors and Signal Transduction. 24 (3): 165–205. doi:10.1081/rrs-200029981. ISSN 1079-9893. {{cite journal}}: Check date values in: |date= (help)