Two types of enzymes control the reversibility of the acetylation of amino acid lysine residues in histone molecules in the posttranslational modifications of proteins – histone acetyltransferases (HAT) and histone deacetylases (HDAC). HAT enzymes catalyze the transfer of an acetyl group to the amino acid lysine in the N-terminal parts of histones H2A, H2B, H3, and H4. HDAC enzymes are members of the hydrolases family and play an important role in signal transmission by deacetylating histones, inducing changes in gene expression in skeletal muscle in different functional states in humans. Of the 18 histone deacetylases, class IIa includes four enzymes (HDAC 4, 5, 7, and 9), which are tissue-specific and are involved in regulating metabolism in skeletal and cardiac muscles. Class IIa enzymes react with specific transcription factors to form multicomponent protein complexes, nuclear-cytoplasmic transfer of which in muscle cells influences the expression of regulatory and metabolic genes. Studies in recent years have provided evidence of the important role of this group of histone deacetylases in controlling intracellular metabolism and point to the need for studies of the molecular mechanisms involved in gene expression in skeletal muscles.