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Regulation of mammalian muscle type 6-phosphofructo-1-kinase and its implication for the control of the metabolism

✍ Scribed by Mauro Sola-Penna; Daniel Da Silva; Wagner S. Coelho; Monica M. Marinho-Carvalho; Patricia Zancan

Publisher
John Wiley and Sons
Year
2010
Tongue
English
Weight
207 KB
Volume
62
Category
Article
ISSN
1521-6543

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✦ Synopsis

Abstract

Phosphofructokinase (PFK) is a major regulatory glycolytic enzyme and is considered to be the pacemaker of glycolysis. This enzyme presents a puzzling regulatory mechanism that is modulated by a large variety of metabolites, drugs, and intracellular proteins. To date, the mammalian enzyme structure has not yet been resolved. However, it is known that PFK undergoes an intricate oligomerization process, shifting among monomers, dimers, tetramers, and more complex oligomeric structures. The equilibrium between PFK dimers and tetramers is directly correlated with the enzyme regulation, because the dimer exhibits very low catalytic activity, whereas the tetramer is fully active. Several PFK ligands modulate the enzyme, favoring the formation of its dimers or tetramers. The present review integrates recent findings regarding the regulatory aspects of muscle type PFK and discusses their relation to the control of metabolism. Β© IUBMB IUBMB Life, 62(11): 791–796, 2010.

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