CREATINE KINASE: STRUCTURE AND FUNCTION

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Main Author: Ana Maria Teixeira
Format: Artículo científico
Language:en
Published: Universidade Iguaçu 2012
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author Ana Maria Teixeira
author_facet Ana Maria Teixeira
contents CREATINE KINASE: STRUCTURE AND FUNCTION Ana Maria Teixeira Grasiely F. Borges Salud creatine isoenzymes Creatine Kinase phosphocreatine TEIXEIRA, A. M.; BORGES, G. F. Creatine kinase: structure and function. Brazilian Journal of Biomotricity. v. 6, n. 2, p. 53-65, 2012. Found in all vertebrates, creatine kinase (CK) is a member of the phosphagen kinase family and catalyzes the reversible phosphotransfer between the ATP/ADP and Creatine/Phosphocreatine systems. CK is highly expressed in excitable tissues that require large energy fluxes and plays a significant role in the energy homeostasis of these tissue cells. The creatine kinase reaction was first identified in 1934 by K Lohman in the muscle tissue and it has undergone intensive investigation for over 80 years. The enzyme is of clinical importance and its levels are routinely used as an indicator of acute myocardial infarction. There are four major CK isoforms, which are named according to their tissue distribution or subcellular localization: two tissue (muscle or brain) cytosolic and two mitochondrial, which form dimers and octamers, respectively. In this paper we will include a brief summary of the history of the detection of creatine kinases isoforms, their main structural features, physical and catalitic properties and multiple functions such as an energy buffering function, metabolic regulatory functions and the energy transport function. 2012 artículo científico 1981-6324 https://www.redalyc.org/articulo.oa?id=93023658001 en http://www.redalyc.org/revista.oa?id=930 Brazilian Journal of Biomotricity application/pdf Universidade Iguaçu Brazilian Journal of Biomotricity (Brasil) Num.2 Vol.6
format Artículo científico
id redalyc_93023658001
institution Redalyc
language en
publishDate 2012
publisher Universidade Iguaçu
spellingShingle CREATINE KINASE: STRUCTURE AND FUNCTION
Ana Maria Teixeira
Salud
creatine
isoenzymes
Creatine Kinase
phosphocreatine
CREATINE KINASE: STRUCTURE AND FUNCTION Ana Maria Teixeira Grasiely F. Borges Salud creatine isoenzymes Creatine Kinase phosphocreatine TEIXEIRA, A. M.; BORGES, G. F. Creatine kinase: structure and function. Brazilian Journal of Biomotricity. v. 6, n. 2, p. 53-65, 2012. Found in all vertebrates, creatine kinase (CK) is a member of the phosphagen kinase family and catalyzes the reversible phosphotransfer between the ATP/ADP and Creatine/Phosphocreatine systems. CK is highly expressed in excitable tissues that require large energy fluxes and plays a significant role in the energy homeostasis of these tissue cells. The creatine kinase reaction was first identified in 1934 by K Lohman in the muscle tissue and it has undergone intensive investigation for over 80 years. The enzyme is of clinical importance and its levels are routinely used as an indicator of acute myocardial infarction. There are four major CK isoforms, which are named according to their tissue distribution or subcellular localization: two tissue (muscle or brain) cytosolic and two mitochondrial, which form dimers and octamers, respectively. In this paper we will include a brief summary of the history of the detection of creatine kinases isoforms, their main structural features, physical and catalitic properties and multiple functions such as an energy buffering function, metabolic regulatory functions and the energy transport function. 2012 artículo científico 1981-6324 https://www.redalyc.org/articulo.oa?id=93023658001 en http://www.redalyc.org/revista.oa?id=930 Brazilian Journal of Biomotricity application/pdf Universidade Iguaçu Brazilian Journal of Biomotricity (Brasil) Num.2 Vol.6
title CREATINE KINASE: STRUCTURE AND FUNCTION
topic Salud
creatine
isoenzymes
Creatine Kinase
phosphocreatine
url https://www.redalyc.org/articulo.oa?id=93023658001