filmov
tv
Protein kinase a
Показать описание
Download the study materials here-
Remember Shomu’s Biology is created to spread the knowledge of life science and biology by sharing all this free biology lectures video and animation presented by Suman Bhattacharjee in YouTube. All these tutorials are brought to you for free. Please subscribe to our channel so that we can grow together. You can check for any of the following services from Shomu’s Biology-
We are social. Find us on different sites here-
Thank you for watching
In cell biology, Protein kinase A (PKA) refers to a family of enzymes whose activity is dependent on cellular levels of cyclic AMP (cAMP). PKA is also known as cAMP-dependent protein kinase (EC 2.7.11.11). Protein kinase A has several functions in the cell, including regulation of glycogen, sugar, and lipid metabolism.
It should not be confused with AMP-activated protein kinase - which, although being of similar nature, may have opposite effects - [1] nor with cyclin-dependent kinases (Cdks), nor with the acid dissociation constant, pKa.
Activation
Each PKA is a holoenzyme that consists of a regulatory subunit dimer with each regulatory subunit being bound to a catalytic subunit. Under low levels of cAMP, the holoenzyme remains intact and is catalytically inactive. When the concentration of cAMP rises (e.g., activation of adenylate cyclases by G protein-coupled receptors coupled to Gs, inhibition of phosphodiesterases that degrade cAMP), cAMP binds to the two binding sites on the regulatory subunits, which leads to the release of the catalytic subunits. For maximal function, each catalytic subunit must also be phosphorylated, which occurs on Thr 197 and helps orientate catalytic residues in the active site.[2]
1. Cytosolic cAMP increases. 2. Two cAMP molecules bind to each PKA regulatory subunit. 3. The regulatory subunits move out of the active sites of the catalytic subunits and the R2C2 complex dissociates 4. The free catalytic subunits interact with proteins to phosphorylate Ser or Thr residues. Source of the article published in description is Wikipedia. I am sharing their material. © by original content developers of Wikipedia.
Remember Shomu’s Biology is created to spread the knowledge of life science and biology by sharing all this free biology lectures video and animation presented by Suman Bhattacharjee in YouTube. All these tutorials are brought to you for free. Please subscribe to our channel so that we can grow together. You can check for any of the following services from Shomu’s Biology-
We are social. Find us on different sites here-
Thank you for watching
In cell biology, Protein kinase A (PKA) refers to a family of enzymes whose activity is dependent on cellular levels of cyclic AMP (cAMP). PKA is also known as cAMP-dependent protein kinase (EC 2.7.11.11). Protein kinase A has several functions in the cell, including regulation of glycogen, sugar, and lipid metabolism.
It should not be confused with AMP-activated protein kinase - which, although being of similar nature, may have opposite effects - [1] nor with cyclin-dependent kinases (Cdks), nor with the acid dissociation constant, pKa.
Activation
Each PKA is a holoenzyme that consists of a regulatory subunit dimer with each regulatory subunit being bound to a catalytic subunit. Under low levels of cAMP, the holoenzyme remains intact and is catalytically inactive. When the concentration of cAMP rises (e.g., activation of adenylate cyclases by G protein-coupled receptors coupled to Gs, inhibition of phosphodiesterases that degrade cAMP), cAMP binds to the two binding sites on the regulatory subunits, which leads to the release of the catalytic subunits. For maximal function, each catalytic subunit must also be phosphorylated, which occurs on Thr 197 and helps orientate catalytic residues in the active site.[2]
1. Cytosolic cAMP increases. 2. Two cAMP molecules bind to each PKA regulatory subunit. 3. The regulatory subunits move out of the active sites of the catalytic subunits and the R2C2 complex dissociates 4. The free catalytic subunits interact with proteins to phosphorylate Ser or Thr residues. Source of the article published in description is Wikipedia. I am sharing their material. © by original content developers of Wikipedia.
Комментарии