Chemical and Functional Aspects of Posttranslational Modification of Proteins

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This paper reviews the chemical and functional aspects of the posttranslational modifications of proteins, which are achieved by the addition of various groups to the side chain of the amino acid residue backbone of proteins. It describes the main prosthetic groups and the interaction of these groups and the apoenzyme in the process of catalysis, using pyridoxal catalysis as an example. Much attention is paid to the role of posttranslational modification of proteins in the regulation of biochemical processes in live organisms, and especially to the role of protein kinases and their respective phosphotases. Methylation and acetylation reactions and their role in the “histone code,” which regulates genome expression on the transcription level, are also reviewed. This paper also describes the modification of proteins by large hydrophobic residues and their role in the function of membrane-associated proteins. Much attention is paid to the glycosylation of proteins, which leads to the formation of glycoproteins. We also describe the main non-enzymatic protein modifications such as glycation, homocysteination, and desamidation of amide residues in dibasic acids.

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Modification of proteins by addition of prosthetic gro ups In some cases, the last step in the biosynthesis of a functional protein is the covalent binding of a prosthetic group, which forms part of the active site [1, 2]. Table 1 shows the structural formulas of side chain modification products after the covalent binding of certain cofactors to proteins, as well as the types of reactions in which the corresponding prosthetic groups take part. Most of the listed prosthetic groups remain covalently bound to the apoenzyme through the whole catalytic process. Introd uction Template biosynthesis of polypeptide chains on ribosomes most often does not immediately produce a fully functional protein. The newly formed polypeptide chain must undergo certain chemical modifications outside the ribosome. These modifications are most often driven by enzymes and take place after all the information supplied by the template RN A (mRN A) has been read, that is after mRN A translation: thus, these additional processes are called posttranslational modifications. Posttranslational protein modification processes can be divided into two main groups. The first group unites proteolytic processes, which are mainly cleavages of certain peptide bonds, resulting in the removal of some of the formed polypeptide fragments.
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