AMP-activated protein kinase
| AMP-activated protein kinase | ||
|---|---|---|
| Mass / length primary structure | 1150 = 550 + 269 + 331 amino acids | |
| Secondary to quaternary structure | α 1 + β 1 + γ 1 | |
| Isoforms | α: 2; β: 2; γ: 3 | |
| Identifier | ||
| Gene name (s) | PRKAA1 , PRKAA2 , PRKAB1 , PRKAB2 , PRKAG1 , PRKAG2 , PRKAG3 | |
| Enzyme classification | ||
| EC, category | 2.7.11.1 , Transferase | |
| Response type | Phosphorylation | |
| Substrate | ATP and a protein (ACC, HSL, HMG-CoA synthase, FRAP1, RAF1, EEF2K, TSC2, FNIP1, FNIP2) | |
| Products | ADP and a phosphoprotein | |
| Occurrence | ||
| Parent taxon | Euteleostomi | |
The AMP-activated protein kinase (AMPK) is an enzyme that plays an important role in the regulation of biosynthetic processes in cells of mammals plays. The three subunits α, β, γ each have several isoforms, so that there are several isoforms of AMPK, some of which are tissue-specific . Mutations in PRKAG2 - gene are rare hereditary types of Wolff-Parkinson-White syndrome and hypertrophic cardiomyopathy responsible.
function
AMPK is a heterotrimeric protein made up of the catalytic alpha-1 (PRKAA1), beta-1 (PRKAB1) and gamma-1 (PRKAG1) subunits; its task is to protect cells from a lack of ATP, i.e. a lack of energy. This is achieved by switching off energy-intensive biosyntheses in that the AMPK inhibits several enzymes responsible for cholesterol and fatty acid biosynthesis through phosphorylation (including HMG-CoA reductase and acetyl-CoA carboxylase ). AMPK is regulated by the cell's AMP and ATP levels, with another kinase , LKB1, also being involved. AMP is a breakdown product of ATP and therefore a suitable indicator of energy deficiency. The AMPK occurs as a homolog in many other species ( yeasts and even higher plants) and therefore appears to be a tool for protection against energy deficiency in cells that appeared at an early stage in evolution.
literature
- D. Grahame Hardie, David Carling: The AMP-Activated Protein Kinase. Fuel Gauge of the Mammalian Cell? In: European Journal of Biochemistry . tape 246 , no. 2 , 1997, ISSN 1432-1033 , pp. 259-273 , doi : 10.1111 / j.1432-1033.1997.00259.x .
- Georg Löffler: Biochemistry and Pathobiochemistry. Springer, 7th edition, 2003.
Web links
- alpha-1 subunit. In: Online Mendelian Inheritance in Man . (English).
- beta-1 subunit. In: Online Mendelian Inheritance in Man . (English).
- gamma-1 subunit. In: Online Mendelian Inheritance in Man . (English).
Individual evidence
- ↑ D. Stapleton, KI Mitchelhill, G. Gao, J. Widmer, BJ Michell: Mammalian AMP-activated protein kinase subfamily . In: Journal of Biological Chemistry . tape 271 , no. 2 , January 12, 1996, p. 611-614 , PMID 8557660 .
- ↑ [1] , Uwe Riek, Roland Scholz, Peter Konarev, Arne Rufer, Marianne Suter, Alexis Nazabal, Philippe Ringler, Mohamed Chami, Shirley A Müller, Dietbert Neumann, Michael Forstner, Michael Hennig, Renato Zenobi, Andreas Engel, Dmitri Svergun , Uwe Schlattner, Theo Wallimann; Structural properties of AMP-activated protein kinase: dimerization, molecular shape, and changes upon ligand binding
- ^ [2] , Marianne Suter, Uwe Riek, Roland Tuerk, Uwe Schlattner, Theo Wallimann, Dietbert Neumann; Dissecting the role of 5'-AMP for allosteric stimulation, and deactivation of AMP-activated protein kinase
- ↑ [3] Angela Woods 1, Stephen R Johnstone, Kristina Dickerson, Fiona C Leiper, Lee GD Fryer, Dietbert Neumann, Uwe Schlattner, Theo Wallimann, Marian Carlson, David Carling; LKB1 is the upstream kinase in the AMP-activated protein kinase cascade
- ↑ Sang-Min Jeon: Regulation and function of AMPK in physiology and diseases . In: Experimental & Molecular Medicine . tape 48 , no. 7 , July 15, 2016, ISSN 2092-6413 , p. e245 , doi : 10.1038 / emm.2016.81 , PMID 27416781 , PMC 4973318 (free full text).