AMP-activated protein kinase

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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
Gene name (s) PRKAA1 , PRKAA2 , PRKAB1 , PRKAB2 , PRKAG1 , PRKAG2 , PRKAG3
Enzyme classification
EC, category 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
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.


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.


Web links

Individual evidence

  1. 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 .
  2. [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
  3. ^ [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
  4. [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
  5. 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).